CRISPRimmunity

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Overview of predicted results

Overview of the results

Contig_ID	Contig_def	CRISPR array number	Contig Signature genes	Self targeting spacer number	Target MGE spacer number	Prophage number	Anti-CRISPR protein number
NZ_AP014940	Lysobacter enzymogenes strain M497-1	21 crisprs	DEDDh,cas3,WYL,DinG,Cas9_archaeal,csa3	2	4	1	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_AP014940_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_1

978813-978965

Orphan

Consensus_repeat	Method
GTCGCGACCGCGACATCGCGCTTGCGACGCAAGCCAGGTTTCGCGGTCGCG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP014940_1

>merge|NZ_AP014940|1|978813-978965|CRISPRCasFinder
GTCGCGACCGCGACATCGCGCTTGCGACGCAAGCCAGGTTTCGCGGTCGCGACTCGCGTCGCTCTTACAGGTAGCGGCCGCGACGTTCGCCGCGATCGGGCGGTCGCGACCGCGACATCGCGCTTACGACGCAAGCCAGGTTTCGCGGTCGCG

>NZ_AP014940|1|1|978813-978965|CRISPRCasFinder
GTCGCGACCGCGACATCGCGCTTGCGACGCAAGCCAGGTTTCGCGGTCGCG	ACTCGCGTCGCTCTTACAGGTAGCGGCCGCGACGTTCGCCGCGATCGGGCG
GTCGCGACCGCGACATCGCGCTTACGACGCAAGCCAGGTTTCGCGGTCGCG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_096376773.1\|973173_974076_+\|decarboxylating-6-phosphogluconate-dehydrogenase	unknown	unknown	gnl\|CDD\|236582
NZ_AP014940.1\|WP_096376777.1\|977271_978060_+\|N-acetylmuramoyl-L-alanine-amidase	unknown	unknown	gnl\|CDD\|225567
NZ_AP014940.1\|WP_096376772.1\|971186_972251_+\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|223669
NZ_AP014940.1\|WP_096376782.1\|984377_984881_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096376781.1\|982877_984020_-\|PQQ-dependent-sugar-dehydrogenase	unknown	unknown	gnl\|CDD\|369642
NZ_AP014940.1\|WP_074862131.1\|985093_985282_+\|CPXCG-motif-containing-cysteine-rich-protein	unknown	unknown	gnl\|CDD\|379524
NZ_AP014940.1\|WP_096376770.1\|969563_970451_+\|aldo/keto-reductase	unknown	unknown	gnl\|CDD\|381318
NZ_AP014940.1\|WP_096376769.1\|968918_969464_+\|HD-domain-containing-protein	unknown	unknown	gnl\|CDD\|223394
NZ_AP014940.1\|WP_096383064.1\|986195_987344_+\|winged-helix-DNA-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|377630
NZ_AP014940.1\|WP_096376784.1\|988435_989146_+\|HAD-family-hydrolase	unknown	unknown	gnl\|CDD\|319817
NZ_AP014940.1\|WP_096376775.1\|976260_976788_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096376774.1\|974722_975967_+\|chitosanase	unknown	unknown	gnl\|CDD\|366548
NZ_AP014940.1\|WP_096376776.1\|976876_977068_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096376783.1\|987801_988179_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|238008
NZ_AP014940.1\|WP_074862123.1\|981602_982406_+\|lytic-transglycosylase-domain-containing-protein	unknown	unknown	gnl\|CDD\|381594
NZ_AP014940.1\|WP_096376771.1\|970575_970965_-\|YciI-family-protein	unknown	unknown	gnl\|CDD\|226318
NZ_AP014940.1\|WP_096376780.1\|980883_981063_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096383061.1\|985299_986187_+\|PD40-domain-containing-protein	unknown	unknown	gnl\|CDD\|223893
NZ_AP014940.1\|WP_096376779.1\|979009_980377_-\|amino-acid-permease	unknown	unknown	gnl\|CDD\|129987
NZ_AP014940.1\|WP_096376778.1\|978145_978712_-\|NAD(P)H-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|377026

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_096376773.1\|973173_974076_+\|decarboxylating-6-phosphogluconate-dehydrogenase	gnl\|CDD\|236582	PRK09599, PRK09599, NADP-dependent phosphogluconate dehydrogenase.	0
NZ_AP014940.1\|WP_096376777.1\|977271_978060_+\|N-acetylmuramoyl-L-alanine-amidase	gnl\|CDD\|225567	COG3023, ampD, N-acetyl-anhydromuramyl-L-alanine amidase [Cell envelope biogenesis, outer membrane].	1.40413e-58
NZ_AP014940.1\|WP_096376772.1\|971186_972251_+\|alpha/beta-hydrolase	gnl\|CDD\|223669	COG0596, MhpC, Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily) [General function prediction only].	2.65643e-15
NZ_AP014940.1\|WP_096383061.1\|985299_986187_+\|PD40-domain-containing-protein	gnl\|CDD\|223893	COG0823, TolB, Periplasmic component of the Tol biopolymer transport system [Intracellular trafficking and secretion].	6.98942e-06
NZ_AP014940.1\|WP_096376781.1\|982877_984020_-\|PQQ-dependent-sugar-dehydrogenase	gnl\|CDD\|369642	pfam07995, GSDH, Glucose / Sorbosone dehydrogenase. Members of this family are glucose/sorbosone dehydrogenases that possess a beta-propeller fold.	4.55316e-168
NZ_AP014940.1\|WP_074862131.1\|985093_985282_+\|CPXCG-motif-containing-cysteine-rich-protein	gnl\|CDD\|379524	pfam14255, Cys_rich_CPXG, Cysteine-rich CPXCG. This family of proteins is found in bacteria. Proteins in this family are approximately 60 amino acids in length. There are 5 conserved cysteines which occur in a CPXCG motif and a DCXXCCXP motif.	3.27858e-18
NZ_AP014940.1\|WP_096376770.1\|969563_970451_+\|aldo/keto-reductase	gnl\|CDD\|381318	cd19092, AKR_BsYcsN_EcYdhF-like, Bacillus subtilis YcsN, Escherichia coli YdhF and similar proteins. Bacillus subtilis YcsN and Escherichia coli YdhF are prototypes of this family. They are uncharacterized aldo/keto reductase family oxidoreductases.	2.24343e-147
NZ_AP014940.1\|WP_096376769.1\|968918_969464_+\|HD-domain-containing-protein	gnl\|CDD\|223394	COG0317, SpoT, Guanosine polyphosphate pyrophosphohydrolases/synthetases [Signal transduction mechanisms / Transcription].	3.33116e-24
NZ_AP014940.1\|WP_096383064.1\|986195_987344_+\|winged-helix-DNA-binding-domain-containing-protein	gnl\|CDD\|377630	pfam06224, HTH_42, Winged helix DNA-binding domain. This family contains two copies of a winged helix domain.	1.8556e-56
NZ_AP014940.1\|WP_096376784.1\|988435_989146_+\|HAD-family-hydrolase	gnl\|CDD\|319817	cd07515, HAD-like, uncharacterized family of the haloacid dehalogenase-like (HAD) hydrolase superfamily. The haloacid dehalogenase-like (HAD) hydrolases are a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members include 2-L-haloalkanoic acid dehalogenase (C-Cl bond hydrolysis), azetidine hydrolase (C-N bond hydrolysis); phosphonoacetaldehyde hydrolase (C-P bond hydrolysis), phosphoserine phosphatase and phosphomannomutase (CO-P bond hydrolysis), P-type ATPases (PO-P bond hydrolysis) and many others. Members are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.	2.06878e-50
NZ_AP014940.1\|WP_096376774.1\|974722_975967_+\|chitosanase	gnl\|CDD\|366548	pfam01270, Glyco_hydro_8, Glycosyl hydrolases family 8.	1.23433e-20
NZ_AP014940.1\|WP_096376783.1\|987801_988179_+\|hypothetical-protein	gnl\|CDD\|238008	cd00051, EFh, EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.	4.4435e-06
NZ_AP014940.1\|WP_074862123.1\|981602_982406_+\|lytic-transglycosylase-domain-containing-protein	gnl\|CDD\|381594	cd00254, LT-like, lytic transglycosylase(LT)-like domain. Members include the soluble and insoluble membrane-bound LTs in bacteria and LTs in bacteriophage lambda. LTs catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc), as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue.	3.12352e-42
NZ_AP014940.1\|WP_096376771.1\|970575_970965_-\|YciI-family-protein	gnl\|CDD\|226318	COG3795, COG3795, Uncharacterized protein conserved in bacteria [Function unknown].	1.81443e-39
NZ_AP014940.1\|WP_096376779.1\|979009_980377_-\|amino-acid-permease	gnl\|CDD\|129987	TIGR00909, putative_amino_acid_transporter, amino acid transporter. [Transport and binding proteins, Amino acids, peptides and amines].	1.05096e-56
NZ_AP014940.1\|WP_096376778.1\|978145_978712_-\|NAD(P)H-dependent-oxidoreductase	gnl\|CDD\|377026	pfam03358, FMN_red, NADPH-dependent FMN reductase.	6.14764e-37

>NZ_AP014940.1|WP_096376778.1|978145_978712_-|NAD(P)H-dependent-oxidoreductase
MASNLRLALVYGSAREGRFCDVVGAWAQRRVAAHGGFDTDLIDPAQWPLSGRADEAPLQSLRQRLHAADAFLIVTPEYNHGYPAPLKALIDACYEPWRAKPVAFVSYGASSGGLRAIEQLRQVFGELHAATLRDCVCLVHAGRQFGADGELREPQATHRAMEVALARLRWWALALREAREAMPYEAAA
>NZ_AP014940.1|WP_096376777.1|977271_978060_+|N-acetylmuramoyl-L-alanine-amidase
MNLRRLPSLGAVALALVLAGCASAPPHNPLAQWRGSPNFNERRAQLIVLHHTQMESVGEALRTLQTANSQGKVSAHYLIGEDGRIYQLVAEERRAWHAGAGRWGDVSDLNSASIGIELDNDGSEPFAEAQIQSLLRLLADLTKRLGLPPQAILAHGDLAPERKSDPSVQFPWKRLADAGFGLWPREPLAAPPPGFDPWAALRLVGYDLRDPGAALAAFHRRFRGNEARDWQPGDAEVLYDLQRQLVALPEGAPPPLPAPPLR
>NZ_AP014940.1|WP_096376776.1|976876_977068_-|hypothetical-protein
MKRKSQAWLAAFALAAFGFGFGVQAASSAPPDKALCSIKVCQDRCGGLPGWNPGNGQPCRCCD
>NZ_AP014940.1|WP_096376775.1|976260_976788_+|hypothetical-protein
MRKIESNLLSHRFISSRAPVSRLLGQCVAGLLLAGVCAVASASGEPKPFDTASVLEQQKQIRGDVDAGRGDYAKLEPAKRDELRTRQDRLNQLLQGRSYDQLSASERDQAHQDLAWIGQASGNATASADPDEKVVCQRVRSIGSNRIEKVCKSVSQRRDEQKNRVEPQLERPGIR
>NZ_AP014940.1|WP_096376774.1|974722_975967_+|chitosanase
MHHATALPRRGLKLLSLVLATAAALGASLAAQAEPNYPFGSHRQAYVSGTLSPSVGRAAADQSTASFYRAWKQRYLVAGCKAGEYRVKASTDTAYVVSEGQGYGMLITVMMAGNDPDAQALFDGLHRYNRGHPSSGNPALLAWAQDANCKNVAGPDSATDGDLDIAYALLLADLQWGSAGSINYLSEARKVIAAIRSSNVNANTKLVTLGDWVSSSEPNYYNSTRSSDWMLGHFRGFASKLGDSYWTGVLDAHQTLIGKMQSSYAPNTGLLPDFIVNTNTTAKPAPANFLESEYDGAYSWNAGRVPWRIGIDAAVSGDSRSRSAARKLSQWIKAKAGNNANNIRSGYKLDGTVTENYNSTFFTAPFAVAATVDTDQAWLDKLWTYLANGSTSDYYGDSVKLLSMLAVTNNWLKP
>NZ_AP014940.1|WP_096376773.1|973173_974076_+|decarboxylating-6-phosphogluconate-dehydrogenase
MELGMVGLGRMGANMAERLVRGGHAVTGFDPGAAAREQAAARGIGAAASLAELVAALPAPRAVWLMVPAGAVDATLAELRPLLAPGDTVVDGGNSNYKDTVRRAGELREHGLHYVDSGTSGGVWGLQEGYSLMIGGDEAAVERLRPIFETLAPAAERGWGRVGPSGSGHFTKMIHNGIEYGMMQAYAEGFAILGRKAEFGLDLHQIAQIWRHGSVVRSWLLDLSADALGKNPSLQGIAPYVEDSGEGRWTVAEAIDLDVSAPVITASLMERLRSREKDSFADKLLAAMRNEFGGHAIRKE
>NZ_AP014940.1|WP_096376772.1|971186_972251_+|alpha/beta-hydrolase
MEAARGHFGRTTGAAMVMALMAAAAGAATPAKPGARPKPRPAPDASLDVYAEPGERIDIGGGRKLNLRCSGAGAPTVLLEAGFGSDSLAWAKAQPQIAQRNRVCSYDRAGLGFSDGGPLPRDLKADVADLRALIDAADLDTPLILVGHSYGSQLVRRYDELYPKQVAALVLVDPPEQNVGEFSASYAKTEAQMAPRMLAMYRGCEQGARDGRLGAARPPSDLKNCLRPPNPNYSDKLNASVRAWRSKPAFWETVISGSQDRLSLYGSAVAKSERHDGKPVIVLSAEQPYAGAPADDLKALLAAREQTHLALIGTSRYAKRVTIADSSHDIPNDQPAAPAIAVFEAMEMRKQIGR
>NZ_AP014940.1|WP_096376771.1|970575_970965_-|YciI-family-protein
MRFMMLMIPQGYESAAPGTLPSVERIESMTKYNHSLQEAGVLRALDGLHPPSMGARVSFRGGAARVVDGPFPEAKEVLGGYWVIEVGSREEAIEWARRCPATDNETIEVRQIMGMEDFPEDVQKAVGEP
>NZ_AP014940.1|WP_096376770.1|969563_970451_+|aldo/keto-reductase
MSAADSLSLSPIVAGCWRMAEWNLDAAQRLRWIGQALDLGIDSFDHADIYGDYSVEGLFGEALALQPALRSRIRLISKCGIKLTSAQRPGHTIKSYDSSRAHVLASVENSLRALRTDYLDLLLIHRPDLLMDADELAATFAELKAAGKVLHVGVSNHTPLQLALLHARHPLATHQVELSPLHLPPLDDGTLEQCQALRLRPMLWSPLAGGRLFGGGDERAERVRAVLADLGRRHGGASVATMAYAWLLRHPTRPWPITGSGREQGLRDAVEALAIELSAQEWYEVWQASAGREVA
>NZ_AP014940.1|WP_096376769.1|968918_969464_+|HD-domain-containing-protein
MHHDQALVLRAAAFAAQRHRRQRRLDPERSPYINHPLALADTLANLGGVADPVVLCAALLHDTVEDTATTFEELELAFGARIAAVVREVTDDKTLPKAERKRLQVEHAPHISREAQLVKLADKISNLGDLLDAPPPWPQQRKRDYFDWTAQVVAGLRGVHPVLEARFDALYARIDELTDSA
>NZ_AP014940.1|WP_096376779.1|979009_980377_-|amino-acid-permease
MSQPSSEPTSVRAPAVSPSASQSGPEPGDSGTVRAVSRWQIVGLSINDVIGSGIYLLPATAAMLLGPASLWAVLLAGFAVALLVLCYAQAASYFDQPGGGYLYAREAFGPFAGFEVGWMLLVTRISTAASLSNGLAEAVALFWPAAKAGPARVFIVAGSLGLLVLINVLGVRTAARAGVALAIGKLVPLVLFVAIGAFYFDPSLLHSDAPLPMDHLGEAALLLLFAYAGFENLPAAAGEYRNPRRDVPFALLTMIVLVTIIYFTVQLVALGTLPGIAASSSPLAEAAAHFSGTGLALVLTVGAAISILGTNSNTVMMGPRYLLALSRDGYGPRALGEIHPRFHTPARAVLFLGAIALVLALTGSFQQLALLSVVARLCTYIGTAVSVLVLQKHHRGREGALHLPGGPLIPIAAIVLSLGLLASASAQNLIAAAVALLVGAAIYKLRRKPEADAAA
>NZ_AP014940.1|WP_096376780.1|980883_981063_+|hypothetical-protein
MKIDLRFAAYAAIVLGALSLAACKSKGETTPDAPAASTAPASAPADAAAAPPPTSGDGG
>NZ_AP014940.1|WP_074862123.1|981602_982406_+|lytic-transglycosylase-domain-containing-protein
MIAAAPARTLALRLAAAVALLALASTAAQARTVYRCVRDGTVSLATAPEPGSRCEAKQIDDDAVKLPNLWGEMGVINGNLYERQQDGKTVYSTRNLPGSVRVMGFTVETPPGEPAHPGLGKVGKPQLDKFSAQFRSAAKANGLDDAWLRAIAHAESGFDAKAVSSKGAQGVMQLMPETAKEYGVGDPFSSEESIKAGARHLKSLLRRYNNDLTLATAAYNAGIGTVTRYRGVPPYRETQEYIAKVEALLQSYQLALGTRKPALRAAQ
>NZ_AP014940.1|WP_096376781.1|982877_984020_-|PQQ-dependent-sugar-dehydrogenase
MKLTSLSLLCAAALALPAAAAFAHDAQDAPADAAAAKANPFTATEVARFNEPWAMTFLPNGRLLVTEKRGQLKVLTIGGSAQTITGVPAVAYGGQGGLGDVILHPQFASNNLVYISYAEKGTTSGTAGATVARAKLTLTSTGGSLSNLQVLWRQPKVTGSNHYGHRLAFGPDHKLWITSSERQKFDPAQDLNSPLGKVIRLNDDGSVPTDNPFYNRGGVAATVWSYGHRNLLGIAFDAQNKLWIHEMGPAGGDELNLIERGSNYGWPVVSQGDHYDGTPIPRHSTRPDLNAPEAWWTPVIAPAGFVIYSGTRFPAWVGSGLIGGLASQALVRVKFNGNTAAEAERYPMGKRIREVEQGPNGDVWLLEDGTNARLLRLTPI
>NZ_AP014940.1|WP_096376782.1|984377_984881_-|hypothetical-protein
MKTRHVFSTPDLIVAQTAMDAAREAGVRDDDILLIARSDIELESIPNERKEADTDLMPAALRGAGYGGAAGLLAGLLAVVVTPIGLTVAGTAAALAAGAMVGCWASALMGSALPDPIRRKFDAHIRAGRILVVIDGDRDLLGRAEAYVLAHAPGVEILPFDAPTALA
>NZ_AP014940.1|WP_074862131.1|985093_985282_+|CPXCG-motif-containing-cysteine-rich-protein
MLPSVEVHCPYCGEPIELLIDESAGDQRYIEDCQVCCRPIVVAVSVDEDGEPDVAVYAEDDA
>NZ_AP014940.1|WP_096383061.1|985299_986187_+|PD40-domain-containing-protein
MAACLAAAPAFAAVPGFGARGESVEPWAPARIASARFESHPAFDPLTGDLYFVRSAADFTGWRILTSHCSADGWSEPVEPAFAGDGVEADPWFTPDGRTLYFISSRTPDGAAPLAAGGKRKDLDLWRVERDAQGRWGRPQRLPEPVNSPDAEWFPRLAPDGWLYFGSNRPGGLGKTDLWRARQGRDGAWAVQNLGPRLNTADDEYEPLVSADGKRMVLMAADGLYQSIRGAHGWSQRVKLGPAIDANGSEIGALLSPDGHSMLFARDLKGERSGELFLWRDGKGDPGWPPRCPRR
>NZ_AP014940.1|WP_096383064.1|986195_987344_+|winged-helix-DNA-binding-domain-containing-protein
MTTKTRGAAPPTLSARALNRALLARQSLLERSDESVEAMAERLVGLQAQAPNPPYLGLWTRLQRFALDDLTRALQERRIVRATMMRGTLHLVSAADYRALRPVLQPALQRLSLASGHAKALRGLELDALRRAGFEALRAAPLNAAELGDALRAHWPEHDCGELALLVRSAEALVHVPPAGCWDWHKPAAFATALDWLGAAVADEAGEDAADAMALRYLGAFGPASARDFGAWSGLSAPAERLRRLRPQLQVFRDEDGTELFDLPDAPRPPPELPAPPRLLPEFDNVLLAHAQRERILAPSARAAVYTRNGLVAATVLVDGFVAGVWKLQRDARAATLTVFPFRRLAAAERAELEAQAADCLRVAATDRQTHDVRYARVQKPV
>NZ_AP014940.1|WP_096376783.1|987801_988179_+|hypothetical-protein
MNIKSRKPLIATLALTAALAAPMAFAQSAADQAPPTGDAAASSAAQDPAAATAAPAPSAQKKSWADVDTDKSGNLSKGEAAAVPALSQVFEQADSDANGQLTPDEYKNYVAKAQSGGGAASSGGK
>NZ_AP014940.1|WP_096376784.1|988435_989146_+|HAD-family-hydrolase
MVGFDADDTLWRSQDYFDQAQLDFERIVGQYVDLGDARLHERLYEIEKNNIGVFGYGVKGMTLSMIEAAVAITGQRISAADLHRIVELGKDLLRHPVEMLPGIADAVAAIAADFEVVLITKGDLFHQEAKVKQCGLADLFRRIEIVSEKDAGTYARLLREFGLPAAQFAMIGNSLRSDIAPVLELGGWGIHVPYHTTWAHENEAEVAADAPRLRRVTSAAELPQTVGELARAAEAG

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Crispr_ID: NZ_AP014940_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_2

1171864-1171966

Orphan

Consensus_repeat	Method
TGGGTTCCGGCTTTCGCCGGAATG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP014940_2

>merge|NZ_AP014940|2|1171864-1171966|CRISPRCasFinder
TGGGTTCCGGCTTTCGCCGGAATGACGGTGTGGAGGTTTGTAGCTTCGGAGTGCGACGGCGGGGCTACGCAGCTTCGGTTGGATTCCGGCTTTCGCCGGAATG

>NZ_AP014940|2|2|1171864-1171966|CRISPRCasFinder
TGGGTTCCGGCTTTCGCCGGAATG	ACGGTGTGGAGGTTTGTAGCTTCGGAGTGCGACGGCGGGGCTACGCAGCTTCGGT
TGGATTCCGGCTTTCGCCGGAATG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_096376899.1\|1162127_1162925_+\|general-secretion-pathway-protein-GspN	unknown	unknown	gnl\|CDD\|237030
NZ_AP014940.1\|WP_096376909.1\|1177808_1178471_+\|energy-transducer-TonB	unknown	unknown	gnl\|CDD\|273570
NZ_AP014940.1\|WP_096376907.1\|1172817_1173228_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096376908.1\|1176526_1177816_+\|serine-hydroxymethyltransferase	unknown	unknown	gnl\|CDD\|234571
NZ_AP014940.1\|WP_096376900.1\|1162948_1165198_+\|type-II-secretion-system-secretin-GspD	unknown	unknown	gnl\|CDD\|274175
NZ_AP014940.1\|WP_074863295.1\|1175302_1176205_-\|lipid-A-hydroxylase-LpxO	unknown	unknown	gnl\|CDD\|380241
NZ_AP014940.1\|WP_074862543.1\|1173342_1175004_-\|energy-dependent-translational-throttle-protein-EttA	unknown	unknown	gnl\|CDD\|236992
NZ_AP014940.1\|WP_074862528.1\|1166622_1167471_+\|glycosyltransferase-family-2-protein	unknown	unknown	gnl\|CDD\|224137
NZ_AP014940.1\|WP_096376905.1\|1170653_1170908_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_172437144.1\|1165584_1165758_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_145959969.1\|1181245_1182079_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_145959968.1\|1179142_1180288_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|236090
NZ_AP014940.1\|WP_096376911.1\|1180364_1181219_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096376902.1\|1167628_1168597_-\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293805
NZ_AP014940.1\|WP_074862551.1\|1178523_1179042_+\|transcriptional-repressor-NrdR	unknown	unknown	gnl\|CDD\|234774
NZ_AP014940.1\|WP_074862540.1\|1171991_1172729_-\|type-I-methionyl-aminopeptidase	unknown	unknown	gnl\|CDD\|235576
NZ_AP014940.1\|WP_096376904.1\|1169733_1170612_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096376901.1\|1165754_1166594_+\|glycosyltransferase	unknown	unknown	gnl\|CDD\|224136
NZ_AP014940.1\|WP_096376906.1\|1170921_1171734_-\|orotidine-5'-phosphate-decarboxylase	unknown	unknown	gnl\|CDD\|234651
NZ_AP014940.1\|WP_096376903.1\|1168754_1169648_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_096376909.1\|1177808_1178471_+\|energy-transducer-TonB	gnl\|CDD\|273570	TIGR01352, Protein_TonB, TonB family C-terminal domain. This model represents the C-terminal of TonB and is homologs. TonB is an energy-transducer for TonB-dependent receptors of Gram-negative bacteria. Most members are designated as TonB or TonB-related proteins, but a few represent the paralogous TolA protein. Several bacteria have up to four TonB paralogs. In nearly every case, a proline-rich repetive region is found N-terminal to this domain; these low-complexity regions are highly divergent and cannot readily be aligned. The region is suggested to help span the periplasm. [Transport and binding proteins, Cations and iron carrying compounds].	9.56097e-09
NZ_AP014940.1\|WP_074863295.1\|1175302_1176205_-\|lipid-A-hydroxylase-LpxO	gnl\|CDD\|380241	NF033391, lipid_A_LpxO, lipid A hydroxylase LpxO. Members of this family are LpxO, an enzyme that modifies one of the lipid chains in lipid A by hydroxylation, with resulting changes in resistance to the host immune response and to the antibiotic colistin. This family, as built, includes LpxO1 from Pseudomonas aeruginosa, but not its paralog LpxO2.	0
NZ_AP014940.1\|WP_096376908.1\|1176526_1177816_+\|serine-hydroxymethyltransferase	gnl\|CDD\|234571	PRK00011, glyA, serine hydroxymethyltransferase; Reviewed.	0
NZ_AP014940.1\|WP_096376900.1\|1162948_1165198_+\|type-II-secretion-system-secretin-GspD	gnl\|CDD\|274175	TIGR02517, Putative_type_II_secretion_system_protein_D, type II secretion system protein D. In Gram-negative bacteria, proteins that have first crossed the inner member by Sec-dependent protein transport can be exported across the outer membrane by type II secretion, also called the main terminal branch of the general secretion pathway. Members of this family are general secretion pathway protein D. In Yersinia enterocolitica, a second member of this family is part of a novel second type II secretion system specifically associated with virulence (See ). This family is closely homologous to the type IV pilus outer membrane secretin PilQ (TIGR02515) and to the type III secretion system pore YscC/HrcC (TIGR02516). [Protein fate, Protein and peptide secretion and trafficking].	8.68251e-163
NZ_AP014940.1\|WP_074862543.1\|1173342_1175004_-\|energy-dependent-translational-throttle-protein-EttA	gnl\|CDD\|236992	PRK11819, PRK11819, putative ABC transporter ATP-binding protein; Reviewed.	0
NZ_AP014940.1\|WP_074862528.1\|1166622_1167471_+\|glycosyltransferase-family-2-protein	gnl\|CDD\|224137	COG1216, COG1216, Predicted glycosyltransferases [General function prediction only].	2.43115e-45
NZ_AP014940.1\|WP_096376899.1\|1162127_1162925_+\|general-secretion-pathway-protein-GspN	gnl\|CDD\|237030	PRK12270, kgd, multifunctional oxoglutarate decarboxylase/oxoglutarate dehydrogenase thiamine pyrophosphate-binding subunit/dihydrolipoyllysine-residue succinyltransferase subunit.	3.88594e-06
NZ_AP014940.1\|WP_145959968.1\|1179142_1180288_+\|hypothetical-protein	gnl\|CDD\|236090	PRK07764, PRK07764, DNA polymerase III subunits gamma and tau; Validated.	0.00335302
NZ_AP014940.1\|WP_096376902.1\|1167628_1168597_-\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293805	cd07719, arylsulfatase_AtsA-like_MBL-fold, Pseudoalteromonas carrageenovora arylsulfatase AtsA and related proteins; MBL-fold metallo-hydrolase domain. Arylsulfatase (also known as aryl-sulfate sulfohydrolase, EC 3.1.6.1). Pseudoalteromonas carrageenovora arylsulfatase AtsA may function as a glycosulfohydrolase involved with desulfation of sulfated polysaccharides, which catalyzes hydrolysis of the arylsulfate ester bond, producing the aryl compounds and inorganic sulfate. CD also includes some sequences annotated as ribonucleases. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily.	1.47277e-88
NZ_AP014940.1\|WP_074862551.1\|1178523_1179042_+\|transcriptional-repressor-NrdR	gnl\|CDD\|234774	PRK00464, nrdR, transcriptional repressor NrdR.	1.07454e-82
NZ_AP014940.1\|WP_096376906.1\|1170921_1171734_-\|orotidine-5'-phosphate-decarboxylase	gnl\|CDD\|234651	PRK00125, pyrF, orotidine 5'-phosphate decarboxylase; Reviewed.	6.99317e-125
NZ_AP014940.1\|WP_096376901.1\|1165754_1166594_+\|glycosyltransferase	gnl\|CDD\|224136	COG1215, COG1215, Glycosyltransferases, probably involved in cell wall biogenesis [Cell envelope biogenesis, outer membrane].	2.62047e-06
NZ_AP014940.1\|WP_074862540.1\|1171991_1172729_-\|type-I-methionyl-aminopeptidase	gnl\|CDD\|235576	PRK05716, PRK05716, methionine aminopeptidase; Validated.	5.56506e-103

>NZ_AP014940.1|WP_096376906.1|1170921_1171734_-|orotidine-5'-phosphate-decarboxylase
MSFMQALRRRWQQADTLVCVGLDPEPARFPTSFAADADAVFAFNRDIVDATAEFACAFKPQIAHFAALGAEDALTRLIAHIHARHPEVPVILDSKRGDIGSTAQHYVSEAFDRYRADAVTVNPYMGRDSAQPFLDRAERGVVVLCRTSNPGAGDLQDLDVGGRPLYQRVAEKVANEWNGHGNCALVVGATWPEQLREVRAIVGELPLLVPGVGAQGGDAQAVVGNAKSADGTGLMINSSRAILYASSGDDYAEAAAAATRALRDDINRYR
>NZ_AP014940.1|WP_096376905.1|1170653_1170908_-|hypothetical-protein
MAAKLHELDLTQLETAVTALHRRGRIEFLQRGMMPEADVFLCRSGGRRFNVKFDLAYGAQVDAVDAFSRQELAELEQALSEAAA
>NZ_AP014940.1|WP_096376904.1|1169733_1170612_+|hypothetical-protein
MSFLSKLFGRKPAAPSAASPALLDLSAFAQRFAGELRDAFPDAHIRIVPGAQNEARIDVSLPGEIQAGLQLGNAYQRYLSEPQALDAVLADQMASVREMQRRLSAEDEDDEAGVVLPVIKTRDWYDTAMNQLRASQPDMDAVPFVVEPLAGDLIVTYVLDTPASMSFLSPHEAEQRELRGDALRAHALENLARSLPQLELQGGGGRYAARLDRNYDAGMALLFERWRDRIELRGEPVFAIAARDELMVCGSEDGESVAALREIAQEIARSSPYGLSSGLFVWRDGGLRAFEG
>NZ_AP014940.1|WP_096376903.1|1168754_1169648_+|hypothetical-protein
MSLTLLNRLFGGRGSEPAQAAPLPADPLDLHTFAERHAQALRTAWPQARVRLSFGAHLADTRIDWSLADGFADAQFVGDGYRRYLAAPAALEQVLAEQVAAAREARRRFDRGAEAARDDAILPVLKTRAWHELALQQARSIGGGARSAFVIEPLAGDLVLTYAEDRPESMDYLSPAEAERRGLDREALRACALRNLRRFLPELEVQGEDGLYAARLDRNYDASMALLFEHWRERAPVRGEAVFAIAARDELLLCGSDDRPALRALRTVAQEIARDSAYGLSAQLFVQRDGALHAFEG
>NZ_AP014940.1|WP_096376902.1|1167628_1168597_-|MBL-fold-metallo-hydrolase
MNADSADSTAPASPSRRRALAAGLAALGAAALPGFAAADPAARTRIVLLGTAGGPTPKALRAAPASAVVVGDAVYVVDCGNGVARQLALAGLRLGALRGVFVTHQHSDHNADYGNLLLLAWAADLRTPVDAWGPPPLKRMTRQFLRMNDVDIRTRIADEGRPDPATLIRAHELRAGGEVMRDERVRVRAAVVEHPPLRPAFAYRFDTADRSVVFSGDTRPSAALIELARGADVLVHEVMYLPALEKLIASEPQAARLRQHLLDSHTTAEQVGRVASEAGVKTLVLNHFVPGGDAALTDEVWRAAVAPHFKGELVIGRDLLEV
>NZ_AP014940.1|WP_074862528.1|1166622_1167471_+|glycosyltransferase-family-2-protein
MFKAVVVSYRSAATIDECLERLRACDGVGAIRVVDNQSDDGTLDIVQRQASLDPRLRFIANPDNPGFSVGCNQGAADLEPAPDDDDWLAFVNPDCMVEPDTLRRLHALGAALGDCLLSADLVNEQGERDVAVRRRDPDFGAMLAGILRPWAAPKMAVAPIDSQPLQEVQATSGALMLMPRELFARIGGFDEGYRLHAEDLDLCRRVREAGGVVAVANGIRVVHVRGVSSRSRPFFVEWNKHRGLWRYFRKFEAPRRGALVRAGVFAAIWLRFPIAALRAALR
>NZ_AP014940.1|WP_096376901.1|1165754_1166594_+|glycosyltransferase
MSDLPIVVVPVGVDDDALDACLAALDACTPPGARVWLADDAQSGPRGYAIVERWLQSTRLRADYSRRQRSVGEVAHLDEILKACGDADVAVLAADAVPAPGWLSRLQASFAADGAIASATPWCNAGEAASWPRIGEIDPIPDAGDAERLARALAQMPAAHPELPAAIGHAVLLRGAARRRAGGLDAESYGSWYAALTDLSLRLSGLGWRNVLCDTAFVARAGEGRPHDGDMDALAARWPDWHARLAHFLMQDPLRDLRQRLADRLTQVGPPDMQRDLFL
>NZ_AP014940.1|WP_172437144.1|1165584_1165758_+|hypothetical-protein
MAEHRMPPPTHRRAAAPAARAVGVGVGVAAHGDGSRGSAGERRADGVSGRAYAEPRR
>NZ_AP014940.1|WP_096376900.1|1162948_1165198_+|type-II-secretion-system-secretin-GspD
MKQRTQQFATHALAAAIIATQLASCASVISPKLKRDGDPRAMKGASEEKAGVRMVHNGVEQEPLPTKTEEDGPTAQIRRGTGQVINRSAASKPPPGLPGTTGTASFNFEGESLHAVVKAILGEMLGQNYVIAPGVQGTVTLSTPKQVNASEAMNLLEMVLSWNNARLIYSGGRYNIVPADQALPGNVSARTGSAETARGFEVRTVPLRYVSATEMEKILKPYARPNAIVNVDNARNVITVGGTRAELEHYLRTIEVFDVDWLSGMSVGVFPLQSGKASKVVADLEKVFGEQSKSPVSGMFRFMPIEGANAVMVITPQAEYLDDIKDWLERIDSAGDGVQLYTQELKYIKAKDLADRLSEVFGGGRSGGGGGEGSPSLMPGLESTEVRDNGSGTSTADIGKSSSDSGLGSSGGGSGSGLGGGASLGQRQAGNGSVTLEVDGAKVGVAAVEETNSILVRSTPQAWKSIRNVIDKLDVMPMQVHIEAQVAEVTLTSGMKYGVQWFLEQAATDNGFPNLNRATNPAVPSKWSTIGASVGGKSGNGLVWSLIKNDAAAVISALDEVTDVHILQTPSVFVRNNAEATLNVGTRIPIESVSVNTGIGNNNTYSQVQYLDTGVILKVRPRVSRDGMVFLDIVQEVSSAGARVGTSNNVTIDTKKLKTEAAVQSGETVLLAGLINDKTDRNSKGLPGLSRIPVLGGLFGNQGTSTERRETIILLTPTLVRNPQESRDLTDEYSRRFRAMEPLNPKKKK
>NZ_AP014940.1|WP_096376899.1|1162127_1162925_+|general-secretion-pathway-protein-GspN
MRLDDASPRTWLLATAAGWALLTWVLALAGMGRHVDALPPDPTLVKPLPQARKSPPDALGPLSQYGEIAARPLFVDDRRPKPFFMQGKGEGENQQAAFDYLLTSVLITPQLSMAILQPADGSESVPVKLGEVPESHPSWRLSSLEPRRAVFEGPEGRRELDLRVFNGQGGQPPTAVAGPQPQPQPGGRPMPVPMPAPNRPVPQPQQQANVPPPPPPQPTPAPQGADATAAPLTEQAQMEAIRKRIEARRAQLRQQQAAQPPANSP
>NZ_AP014940.1|WP_074862540.1|1171991_1172729_-|type-I-methionyl-aminopeptidase
MTLMHAFELEGLRRAGALVSSILTTMREAAVPGAVSRELDAIGAAMLREAGARSAPQLTYDFPGATCISINEVAAHGIPDGTVLREGDLVNIDVSAELDGYFADTGGSFVVGAPNPTQRKLLDATLQARDAAIAQLRAGNLINSIGRTVESVAARHGLRVIRNLGSHGVGRALHEAPGNIPGYYDPRDTRRLHEGMVITIEPFLATHCTHTDEGADGWAMICRRGFAAQFEHTVVVTSGEPIVVT
>NZ_AP014940.1|WP_096376907.1|1172817_1173228_-|hypothetical-protein
MPAILIPLLLYIAFLAFAPAAAIKFGLWFALTTAVVRFAAAKVSGSDTGWSEAAKAVIYAAVLPMLALLGLFGFSGATGISHFENFGAIAVLTLLLGSFIGAFTISLGTSLKDSAIVAAIATACSAVAGWAIRAAG
>NZ_AP014940.1|WP_074862543.1|1173342_1175004_-|energy-dependent-translational-throttle-protein-EttA
MQYIYTMNGVSKTVPPKRQIIKDISLSFFPGAKIGLLGLNGAGKSTVLKIMAGVDTDFTGEARPASGIKVGYLPQEPQIDPEKTVREAVEEGVGEVLNAQAALDAIYAAYAEDGADFDALAKEQERLEAILAAGDAHTLENQLEVAADALRLPPWEAKVGNLSGGEKRRVALCRLLLQKPDMLLLDEPTNHLDAESVEWLEQFLARYTGTVVAVTHDRYFLDNAAEWILELDRGRGIPWKGNYTDWLVQKDERLKQEDNQEKARQKAIQKELEWARQNAKGGRSKGKARLARIEELQAVDYQRRQETNEIFIPPGERLGNKVMEFKNVSKKFGERLLIDNLSFVVPPGAIVGIIGPNGAGKSTLFRMIIGQETPDSGEIDMGPTVKLAYVDQSRDKLEGNHNVFHEVSGGLDILNINGIEIQSRAYIGRFNFKGQDQQKMVGSLSGGERGRLHLAKTLLQGGNVLLLDEPSNDLDVETLRALEDALLEFPGNTFVISHDRWFLDRIATHILAFEGDSHVEFFQGNYREYEEDKRRRLGEEGAKPHRLRFKALK
>NZ_AP014940.1|WP_074863295.1|1175302_1176205_-|lipid-A-hydroxylase-LpxO
MKWVFVFLFLAAAVYVHFRGRVRHRLGRQLLDHSTFMAPINVLMYACSRVPTTPFLTPEQHFPELAPLRARWQEVRAEALHLREMQQIKAADQYNDVGFNSFFRRGWKRFYLKWYDEAHPSAAELCPVTTQLLREVPSVKAAMFTELPPGSELRPHRDPYAGSLRLHLGLETPNDDACFIDVDGQRYSWRDGEWTMFDETYIHWAQNGSQHNRIILFCDIERPMRFAWARGLNRFIAKRLIAAGASPNSEGDKTGAINKIFKYFYALRLKSKALKERSKGTYYFFKYAAVAAVIALIVWL
>NZ_AP014940.1|WP_096376908.1|1176526_1177816_+|serine-hydroxymethyltransferase
MFPSTTRIAGFDDELAQAIADEARRQEDHVELIASENYASPRVLEAQGSVLTNKYAEGYPGKRYYGGCEYVDIAEQLAIDRVKELYGADYANVQPHSGSQANQAVYFALLNPGDTILGMSLAHGGHLTHGAKVNASGKLFNAVQYGVNDQGLIDYDEVERLALEHKPKMVVAGFSAYSQVVDWARFRAIADKIGAYLFVDMAHVAGLIAAGVYPSPVPHAHVVTSTTHKTLRGPRGGIIVAKRWDGAVGEGEGAVGFDDMQKKLQSIVFPGIQGGPLMHVIAAKAVAFKEALQPQFKDYQAQVVKNAQAMAKTIIARGYKIVSGGTENHLMLVDMIGKGITGKDAEAALGRAHITVNKNAVPNDPQKPFVTSGLRIGTPAVTTRGYKEADCVALAEWICDVLDNPKDEKVIAGVRENVTKQCAQFPVYG
>NZ_AP014940.1|WP_096376909.1|1177808_1178471_+|energy-transducer-TonB
MAKPLLRSAALGWLACVSVHAAEAPPGGDSAAPVIEYKTLTPAEAKEAIVVAPPSPPSPSSRPDFSQDIGMTETYYIPACQMGMQGGKYRASWREISDFHARNRVAWLSDHDRYGAPDWYAQPGSRAPEPDNRPDAAYPAAAGEKVGEVVVKVIIDAKGRTRDAIVICSNDTVFDAPALAFARKVAFKPALRDGRPVADYGNVSMRFYPDGPKYGFRRHK
>NZ_AP014940.1|WP_074862551.1|1178523_1179042_+|transcriptional-repressor-NrdR
MHCPFCQHHDTRVIDSRVSDDGATIRRRRVCEACGERFSTIETIELKLPVIIKGDGRREAFDARKLRAGFDRALQKRPVAEEQIEAAVRAVVHQLRMTAERELASRRVGEFVMAELRKLDHVGYVRFASVYRSFEDVADFREELDRLERDAPGDGQLPLLGEDDPRPDRKKR
>NZ_AP014940.1|WP_145959968.1|1179142_1180288_+|hypothetical-protein
MSTAYRSALLSLLLASLPVSAQAADPIEDRQRAPLAGRYTLQGASEGESELLLKPDGRFEWSLRYGPMVQSATGRWNVGADQILLTAQAPAQAKPLFSLDEVAPWNAGAQKRLDEFASERQQTLSEEACAYLKTYRLGLAQIEFTAASPAADPAHRSAAAASLAPALAVLERSRLALETAAAAVKPTPWGQPPLGNMEAAAAAAQAAAAGADPDGQAAADRAVRSYLQQREQLAALHAAAGRSLPALPDPRLGRERCLDPAAKADPSGGYAVVVGDPQRGARAEGIGVEFVYSDGRSERTQTSPGGWALAVRRAGVRLERAVLQAPDRPSETVALDESRGRIFAIRLDSAAAMPAPFEQLILHQDDGALVSPQLRGRYVRH
>NZ_AP014940.1|WP_096376911.1|1180364_1181219_+|hypothetical-protein
MRRGAARALVLAACLSASALATAAAAACAPPGDQALAAKYTTAVTNFAAPSEKQLSTLQMHADGRFRWYDLPPLPYPEIAGCWRRSGDTVVLVLGAPDGGDGVKRSMPVAWTQADLNQVRREGVQTIQQAVDAGLLAAGRVWAHQDRKAGEPVRVKLYEPTIGAPPGDAKVSLRLRDGRIVEGAAVPDEAQVIDNRPGPSGGEYLFASLPADAAVQAIGIRFPNQPDRPRWVGVEDRTKLLYMIEFDARATASLFGGTMTLIVNVDGSLSPAPPDRGEPFVRVP
>NZ_AP014940.1|WP_145959969.1|1181245_1182079_+|hypothetical-protein
MRADFVVRCRRSASRLGGAFAGLMACASLCAAPAAFACEPADAALSGRYVSAAADSAASSDKSLQLNKDGSFRLLGVPVQGADFSGCWQRSDDIVVLVEGAAIDGEGIKRALPEPLTQADLKAVRTDGIDTLEQAVDAGLLPLGRQWANQLRRAGETVRVSVYEPRVGLAVGDAKGMLRLADGTVIEQAPTPGEDGQFEFASLPARAVVTAIGVRFPEQPDQPRWLTVSDPTKRLYLIEFDARALGAVQGGFITLSRRADGSLTSDFPDATRFKRAP

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Crispr_ID: NZ_AP014940_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_3

1312955-1313031

Orphan

Consensus_repeat	Method
TGTGCGAGGGCCTTCTGGCCCGATGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP014940_3

>merge|NZ_AP014940|3|1312955-1313031|CRISPRCasFinder
TGTGCGAGGGCCTTCTGGCCCGATGCTTTCGTCCCCGTTCGCCGCAGCTTTTGTGCGAGGGCCTTCAGGCCCGATGC

>NZ_AP014940|3|3|1312955-1313031|CRISPRCasFinder
TGTGCGAGGGCCTTCTGGCCCGATGC	TTTCGTCCCCGTTCGCCGCAGCTTT
TGTGCGAGGGCCTTCAGGCCCGATGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_096377002.1\|1320590_1322888_+\|serine/threonine-protein-kinase	unknown	unknown	gnl\|CDD\|270916
NZ_AP014940.1\|WP_074862843.1\|1307346_1307790_+\|protein-TolR	unknown	unknown	gnl\|CDD\|274306
NZ_AP014940.1\|WP_096377003.1\|1324212_1324737_+\|ImmA/IrrE-family-metallo-endopeptidase	unknown	unknown	gnl\|CDD\|368753
NZ_AP014940.1\|WP_145959977.1\|1318893_1319667_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_172437153.1\|1320019_1320580_+\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|132044
NZ_AP014940.1\|WP_096376992.1\|1305768_1306224_+\|tol-pal-system-associated-acyl-CoA-thioesterase	unknown	unknown	gnl\|CDD\|274304
NZ_AP014940.1\|WP_096376994.1\|1308739_1309204_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|372476
NZ_AP014940.1\|WP_096376996.1\|1310869_1311394_+\|peptidoglycan-associated-lipoprotein-Pal	unknown	unknown	gnl\|CDD\|274307
NZ_AP014940.1\|WP_074862860.1\|1317004_1317703_+\|7-cyano-7-deazaguanine-synthase-QueC	unknown	unknown	gnl\|CDD\|284031
NZ_AP014940.1\|WP_096376993.1\|1307786_1308740_+\|cell-envelope-integrity-protein-TolA	unknown	unknown	gnl\|CDD\|372476
NZ_AP014940.1\|WP_145959979.1\|1323733_1324186_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096376998.1\|1312243_1312924_+\|7-carboxy-7-deazaguanine-synthase-QueE	unknown	unknown	gnl\|CDD\|275145
NZ_AP014940.1\|WP_145959976.1\|1316003_1316207_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_074862862.1\|1318315_1318864_-\|C39-family-peptidase	unknown	unknown	gnl\|CDD\|379241
NZ_AP014940.1\|WP_096376997.1\|1311437_1312235_+\|tol-pal-system-protein-YbgF	unknown	unknown	gnl\|CDD\|224643
NZ_AP014940.1\|WP_074862841.1\|1306458_1307241_+\|protein-TolQ	unknown	unknown	gnl\|CDD\|131843
NZ_AP014940.1\|WP_172437152.1\|1315462_1315885_-\|c-type-cytochrome	unknown	unknown	gnl\|CDD\|226005
NZ_AP014940.1\|WP_096376995.1\|1309452_1310772_+\|Tol-Pal-system-beta-propeller-repeat-protein-TolB	unknown	unknown	gnl\|CDD\|179892
NZ_AP014940.1\|WP_145960227.1\|1313165_1315322_-\|catalase/peroxidase-HPI	unknown	unknown	gnl\|CDD\|237891
NZ_AP014940.1\|WP_074862836.1\|1304678_1305719_+\|Holliday-junction-branch-migration-DNA-helicase-RuvB	unknown	unknown	gnl\|CDD\|234619

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_074862843.1\|1307346_1307790_+\|protein-TolR	gnl\|CDD\|274306	TIGR02801, Protein_TolR, TolR protein. The model describes the inner membrane protein TolR, part of the TolR/TolQ complex that transduces energy from the proton-motive force, through TolA, to an outer membrane complex made up of TolB and Pal (peptidoglycan-associated lipoprotein). The complex is required to maintain outer membrane integrity, and defects may cause a defect in the import of some organic compounds in addition to the resulting morphologic. While several gene pairs homologous to talR and tolQ may be found in a single genome, but the scope of this model is set to favor finding only bone fide TolR, supported by operon structure as well as by score. [Transport and binding proteins, Other, Cellular processes, Pathogenesis].	1.41051e-44
NZ_AP014940.1\|WP_096377003.1\|1324212_1324737_+\|ImmA/IrrE-family-metallo-endopeptidase	gnl\|CDD\|368753	pfam06114, Peptidase_M78, IrrE N-terminal-like domain. This entry includes the catalytic domain of the protein ImmA, which is a metallopeptidase containing an HEXXH zinc-binding motif from peptidase family M78. ImmA is encoded on a conjugative transposon. Conjugating bacteria are able to transfer conjugative transposons that can, for example, confer resistance to antibiotics. The transposon is integrated into the chromosome, but during conjugation excises itself and then moves to the recipient bacterium and re-integrate into its chromosome. Typically a conjugative tranposon encodes only the proteins required for this activity and the proteins that regulate it. During exponential growth, the ICEBs1 transposon of Bacillus subtilis is inactivated by the immunity repressor protein ImmR, which is encoded by the transposon and represses the genes for excision and transfer. Cleavage of ImmR relaxes repression and allows transfer of the transposon. ImmA has been shown to be essential for the cleavage of ImmR. This domain is also found in in metalloprotease IrrE, a central regulator of DNA damage repair in Deinococcaceae, HTH-type transcriptional regulators RamB and PrpC.	1.41157e-21
NZ_AP014940.1\|WP_096377002.1\|1320590_1322888_+\|serine/threonine-protein-kinase	gnl\|CDD\|270916	cd14014, STKc_PknB_like, Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.	1.02578e-53
NZ_AP014940.1\|WP_172437153.1\|1320019_1320580_+\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|132044	TIGR02999, Sig-70_X6, RNA polymerase sigma factor, TIGR02999 family. This group of sigma factors are members of the sigma-70 family (TIGR02937) and are found in a variety of species including Rhodopirellula baltica which encodes a paralogous group of five.	6.71292e-37
NZ_AP014940.1\|WP_096376992.1\|1305768_1306224_+\|tol-pal-system-associated-acyl-CoA-thioesterase	gnl\|CDD\|274304	TIGR02799, Acyl-CoA_thioesterase_YbgC, tol-pal system-associated acyl-CoA thioesterase. The tol-pal system consists of five critical genes. Inner membrane proteins TolQ and TolR convert protomotive force to energy that is transduced through TolA to an outer membrane complex of TolB and Pal. The system is known to be required to maintain outer membrane integrity. In a system with several homologous parts, ExbB and ExbD transduces energy through TonB to a variety of outer membrane proteins, many of which are siderophore receptors. The tol-pal system therefore may also be involved in transport. This family consists of a protein nearly always found in operons with the genes of the tol-pal system. The significance of this thioesterase to the tol-pal system is unclear, but either of two observations may be relevant. First, Pal, or peptidoglycan-associated lipoprotein, has a conserved N-terminal cleavage and acylation that makes it a lipoprotein. Second, the tol-pal system is implicated not only in the import of certain organics but also in the maintenance of outer membrane integrity (by an unknown mechanism).	5.32436e-62
NZ_AP014940.1\|WP_096376994.1\|1308739_1309204_+\|hypothetical-protein	gnl\|CDD\|372476	pfam13103, TonB_2, TonB C terminal. This family contains TonB members that are not captured by pfam03544.	5.23872e-05
NZ_AP014940.1\|WP_096376996.1\|1310869_1311394_+\|peptidoglycan-associated-lipoprotein-Pal	gnl\|CDD\|274307	TIGR02802, Peptidoglycan-associated_lipoprotein, peptidoglycan-associated lipoprotein. Members of this protein are Pal (also called OprL), the Peptidoglycan-Associated Lipoprotein of the Tol-Pal system. The system appears to be involved both in the maintenance of outer membrane integrity and in the import of certain organic molecules as nutrients. Members of this family contain a hydrodrophobic lipoprotein signal sequence, a conserved N-terminal cleavage and modification site, a poorly conserved low-complexity region, together comprising about 65 amino acids, and a well-conserved C-terminal domain. The seed alignment for this model includes only the conserved C-terminal domain.	8.58473e-58
NZ_AP014940.1\|WP_074862860.1\|1317004_1317703_+\|7-cyano-7-deazaguanine-synthase-QueC	gnl\|CDD\|284031	pfam06508, QueC, Queuosine biosynthesis protein QueC. This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyze the conversion of 7-deaza-7-carboxyguanine to preQ0.	4.48317e-105
NZ_AP014940.1\|WP_096376993.1\|1307786_1308740_+\|cell-envelope-integrity-protein-TolA	gnl\|CDD\|372476	pfam13103, TonB_2, TonB C terminal. This family contains TonB members that are not captured by pfam03544.	1.03343e-06
NZ_AP014940.1\|WP_096376998.1\|1312243_1312924_+\|7-carboxy-7-deazaguanine-synthase-QueE	gnl\|CDD\|275145	TIGR04349, Radical_SAM_domain_protein, putative 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE, gammaproteobacterial type. Members of this radical SAM domain protein family appear to be a form of the queuosine biosynthesis protein QueE. QueE is involved in making preQ0 (7-cyano-7-deazaquanine), a precursor of both the bacterial/eukaryotic modified tRNA base queuosine and the archaeal modified base archaeosine. Members occur in preQ0 operons species that lack members of related protein family TIGR03365.	2.8042e-156
NZ_AP014940.1\|WP_074862862.1\|1318315_1318864_-\|C39-family-peptidase	gnl\|CDD\|379241	pfam13529, Peptidase_C39_2, Peptidase_C39 like family.	1.54636e-13
NZ_AP014940.1\|WP_096376997.1\|1311437_1312235_+\|tol-pal-system-protein-YbgF	gnl\|CDD\|224643	COG1729, COG1729, Uncharacterized protein conserved in bacteria [Function unknown].	5.28396e-41
NZ_AP014940.1\|WP_074862841.1\|1306458_1307241_+\|protein-TolQ	gnl\|CDD\|131843	TIGR02796, Protein_TolQ, TolQ protein. TolQ is one of the essential components of the Tol-Pal system. Together with TolR, it harnesses protonmotive force to energize TolA, which spans the periplasm to reach the complex of TolB and Pal at the outer member. The tol-pal system proves to be important for maintaining outer membrane integrity. Gene pairs similar to the TolQ and TolR gene pair often number several per genome, but this model describes specificially TolQ per se, as found in tol-pal operons. A close homolog, excluded from this model, is ExbB of the ExbB/ExbD/TonB protein complex, which powers transport of siderophores and vitamin B12 across the bacterial outer membrane. The Tol-Pal system is exploited by colicin and filamentous phage DNA to enter the cell. It is also implicated in pathogenesis in several bacterial species [Transport and binding proteins, Other, Cellular processes, Pathogenesis].	5.25259e-99
NZ_AP014940.1\|WP_172437152.1\|1315462_1315885_-\|c-type-cytochrome	gnl\|CDD\|226005	COG3474, COG3474, Cytochrome c2 [Energy production and conversion].	5.3426e-29
NZ_AP014940.1\|WP_096376995.1\|1309452_1310772_+\|Tol-Pal-system-beta-propeller-repeat-protein-TolB	gnl\|CDD\|179892	PRK04922, tolB, Tol-Pal system beta propeller repeat protein TolB.	0
NZ_AP014940.1\|WP_145960227.1\|1313165_1315322_-\|catalase/peroxidase-HPI	gnl\|CDD\|237891	PRK15061, PRK15061, catalase/peroxidase.	0
NZ_AP014940.1\|WP_074862836.1\|1304678_1305719_+\|Holliday-junction-branch-migration-DNA-helicase-RuvB	gnl\|CDD\|234619	PRK00080, ruvB, Holliday junction branch migration DNA helicase RuvB.	0

>NZ_AP014940.1|WP_096376998.1|1312243_1312924_+|7-carboxy-7-deazaguanine-synthase-QueE
MNAVVSETAAAPSSERLRLTEIFLSLQGESDSIGWPTVFVRLTGCPLRCQYCDTAYAFHGGEWWTFEAILAEVAQHGARHVCVTGGEPLAQKRCIELLKRLCDAGYEVSLETSGAIDIAAVDPRVSRVLDIKTPDSKEAHRNLWSNLPLLSARDQIKFVICSREDYEWSKGIVTEHGLTSICAVMFSPSFHQVRPRDLADWIVADRLPVRFQLQLHKILWDDEPGR
>NZ_AP014940.1|WP_096376997.1|1311437_1312235_+|tol-pal-system-protein-YbgF
MRKFALALAVVAALAAATPAFAQRASLADRVATLEQRASDNQANMDLLNQVNQLKSEMQALRSQVEELQQQNRQLQESSKAQYLDTDNRLNRLESGAPAAAAPGPQASAKPSPPPPAVKDTPPSVHGDPGLLAQSGDERAAYDAAFNQLKAGQYVESARLFQEFLAAHPNGTYTPNALYWLGESYYVTQNYQLAQEQFQALLDRYPTHDKAAGALLKVGLAQFGLKQVDAAERTLADVANRYPGTDAARTAADRLNAIQLSRLRN
>NZ_AP014940.1|WP_096376996.1|1310869_1311394_+|peptidoglycan-associated-lipoprotein-Pal
MNNAARILLAAVLCTAAVACSKKVKETAPTDNGTGPTTTQPGGDTGPVASGAYGPNDLDTDACLRQRVVYFDLDQDSLKPEFQAIVGCHAKYLRDRPSSRMTLEGNADERGSREYNLGLGERRGNAVSSAIQANGGSGSQITVVSYGEERPVCTESNEDCWGKNRRVEIVYTAK
>NZ_AP014940.1|WP_096376995.1|1309452_1310772_+|Tol-Pal-system-beta-propeller-repeat-protein-TolB
MKRPLRWLTALLAVLLPLAASAQQKGLEIDIVGGLASATPIAVVPMPYQGGGAAPPTDVAEVVRNDLNRSGQFRGLPVEQMAAKPTRGNEISFPDWRALNQDYIVVGRVLDAGAGSYRVEYELYDVGKQQRLLGFALTARANAMRDVAHQVADAIYEKITGVRGAFFTRIAYVTATGTGRGSNYALMVADSDGYNPQTVVRSPEPLLSPSWSPDGNRLAYVSFEGGNSSIYIQNIGTGSRELVAKFRGINGAPAFSPDGRRLALTLSRSGNPEIYVMDLGSKALTQLTNHFGIDTEPTWSADGSKIYFTSDRGGKPQIYSVAASGGSATRVTFQGSYNASASVSFDGKKIATAQGAGNTYRIAVMDSSTGGALWSTLSPGSLDESPSFAPNASMIIYAAREGRRGVLYAVSADARVRQRLVLADGDVREPAWGPYRLPR
>NZ_AP014940.1|WP_096376994.1|1308739_1309204_+|hypothetical-protein
MRAAPGLFLSTLFSGALLAAAAAPAAAAKNEIGRACDSAEHCLPQNQLRYYEVLRQAIGQHWRPPDSAAADSVCTLELDQAAGGAVNAVRAIEPCGLDAAARDSLLAAVRAASPLPYQGYQQVFKPRLRLAVHVPEPDEREGRVKRWWRQVRER
>NZ_AP014940.1|WP_096376993.1|1307786_1308740_+|cell-envelope-integrity-protein-TolA
MKESRADTVQAVILVVLLHGLLIAALIISALLNWNSAAVSAAGSPVTTELAEMSDLSAAMQRTLRSKVKPVELPEPQPDEAEPLPQPVAEPKPQDAVAPQQQSPQDFIPVPDTTSQEQVVDTPTPNPAEEKKLQEAKARQEQVDLTEQKRQEEAQQKQRLAEQQEAERQKKLEEIRRERARLQREQSLAEQKLQQLADRRATQASQTAAATTPAAQAGNQGADTGLLARYQAALQSAIKSKWTRPDSVPLGAACRLNIRQLPGGQVIAVEVMEPCGYDEAGRRSVEAAVLKAQPLPYAGFESVFQRSLILNFRAEDR
>NZ_AP014940.1|WP_074862843.1|1307346_1307790_+|protein-TolR
MSGTIRRPNKRKLKADINVVPYIDVMLVLLIIFMVTAPLLTLGVDVDLPKSNAKSTNTTSDPVVVQVDERGNLFLTVRAGKKEAVTAETLSTKVSAMVKQNDKDKLQVYIAGDGRANYQPVMDAMNILQKAGVEKVSLISQPEKGKQ
>NZ_AP014940.1|WP_074862841.1|1306458_1307241_+|protein-TolQ
MTSSLIALLATTVQALPEEATQAVTQGAAAAGQAAAEFSLLDLVIKASLPVQFIMALLVVASLTSWFIIFRKWKVIRRAKAEADHFEERFWSGAELSKLYAGTTERARNIGGLEAIFEAGFREFNRVRQRRGVDARAQIESAQRAMRATGSREVDGLEHNLELLANIGSTSPYIGLVGTVFGIMVTMHSLVSASKQVGIADVAPGISEALLATAMGLFVAIPAVWAYNRFATGVERLAVRYDAFSEEFSSILQRQAHLDE
>NZ_AP014940.1|WP_096376992.1|1305768_1306224_+|tol-pal-system-associated-acyl-CoA-thioesterase
MSAISANSAANPGLFSWPTRVYWEDTDAGGLVYHAQYLAFMERARSEWVRALGYGQEGLRLEHGLVFVVAGMQIGFLKPGRLDDELQVTVRLVRCRRASLIFVQQVMRGEERLIEAEVKIASVDARQLRPCPIPPALYAQLQAQEAPEPGG
>NZ_AP014940.1|WP_074862836.1|1304678_1305719_+|Holliday-junction-branch-migration-DNA-helicase-RuvB
MNDQRIIGSGATREDDAIEASIRPKRLDEYLGQQPVREQLKIYIEAAKGRGEALDHVLIFGPPGLGKTTLSHVIANELGVNLRQTSGPVIEKAGDLAALLTNLQPHDVLFVDEIHRLSPLVEEVLYPAMEDYQIDIMIGEGPAARSIKLDLPPFTLIGATTRAGLLTAPLRDRFGIVQRLEFYNAEELTKIVRRSAQILGIACEAEGAGEIARRSRGTPRIANRLLRRVRDYAQVRANGHIDRAVADAAMAMLKVDPEGFDDLDRRLLKTIIESFDGGPVGVESLAAALSEERGTLEDVIEPFLIQQGYLIRTARGRMASSRAYRHFGLDPRDRPGERAIDSGDLF
>NZ_AP014940.1|WP_145960227.1|1313165_1315322_-|catalase/peroxidase-HPI
MAGPAPTPSQSPAKPMSNHDWWPRTLDLSALRQHEAQSNPYGADYDYAKEFATLDLDAVKADIRKTLTTSQPWWPADYGHYGPFFIRMAWHSAGTYRVGDGRGGSDGGEQRFDPLNSWPDNVSLDKARRLVWPIKQKYGRKLSWGDLMVLSGNVALEDMGFKTIGFAGGRVDAWQPDVVFWGPETKMMADQRRDAKGNLKGPLAATQMGLIYVNPEGPNGNHDPISAAADIRRAFGNMAMNDEETLALIAGGHTFGKAHGAHKPDKCVGAEPSAAGIEQQGLGWHNKCGKGNAEDTVSSGLEGAWSANPIKFTTQYLDNLLGFDWVKTKSPAGATQWIPTDVSAARLVPDAHIKGKTHAPIMFTTDIAIKEDPGFRKIADRWHENPQEFADAFARAWFKLTHRDLGPQARYLGKDVPHQTFEWQDPLPKAAAAPLSEADQRKLKAQLLASGLTAPQLVRTAWASASTFRGTDMRGGANGARLRLQPQRGWAVNDPAELAQVLSKLAAVQSAFAQGGKQVSMADLIVLGGNAGIEQAAAQAGYRVAVPFAPGRVDATQEQTDAASFAYLEPKADGFRNYYGPGAELDPAAALVDKADALDLTVPEMTVLVGGLRVLGANAGRSTAGVFTATPGKLDNAFFVNLLSMDTVWSKSAAPGLFEGKDRASGAAKWTATPVDLAFGSNSELRAVAEVYASDDAKQKFVDDFVRAWAKVMNADRS
>NZ_AP014940.1|WP_172437152.1|1315462_1315885_-|c-type-cytochrome
MATIANIAAIPFFAALLAAMFAMFPAASPATAASAEPAPSAQSGKKHFIRCAACHSTDAADRSATGPHLNGIVGRTAASLPHFAYTSALRAQDFKWSEPKLDAFLKSPHSTHPGMCLTFNGLAKAEDRAALIAYLKDPAG
>NZ_AP014940.1|WP_145959976.1|1316003_1316207_+|hypothetical-protein
MKAIDWPYEEADSGVIEVKTAGCVSIIFLSLSQLLLGGDASAEACVYARMRTRAHAAGVRPRLRSLG
>NZ_AP014940.1|WP_074862860.1|1317004_1317703_+|7-cyano-7-deazaguanine-synthase-QueC
MKKAVVLVSGGMDSAVVAAIAREQGFLVHALSVRYGQRHTSELDAAARIAESIGAAAHKTVSVDLRSIGGSALTDESIQVPLDDDGHAIGQDAAKDAIPVTYVPARNTIMLSIALGWAEVLGANDIFCGVNAVDYSGYPDCRPEFVEAFERLANLATKAGVEGAGLRVVAPLQFLSKADIVREGVRLGVDFGQTVSCYKADDAGRACGHCDACRLRAEGFHAAGVADPTRYV
>NZ_AP014940.1|WP_074862862.1|1318315_1318864_-|C39-family-peptidase
MKIKNKLSTAALLALAAIGTASAGVLSVPLYKQEHSNWCWAASASMILSYHGRSVAQCSMANYSFGINYACGNNTFYWNSYANQGNWNYDVDDAMNYFWGSQRFYQQNGALSQASLKARIDANKPFIMSWRWSSGGAHDVVVTGYSGNYVYFNDPWDGSYYRTYAATVSASDRKWEDVLVQY
>NZ_AP014940.1|WP_145959977.1|1318893_1319667_-|hypothetical-protein
MMKVGYMRGALWAPAVALGLCAAALPASAQNVGAGAIAGAGQGLASRVALRDQSSLGLRAAAEQGLRTMMLEMSRGHAAGAKLPEGFPLAAATYGELATLTLGAGFEVNTVDPAALMYANAAADLSRIARSTDTWKFVILSAGKPVGLLDMNRVGGRWTAVGAGASALAADLVAAAPATGDGSFRFVRIYQATSDLIEVRGAGDRSRFVPMPSARRSLALSASAARTTAGAEQTLDSQHLLPALQAAVRGNLQRGQR
>NZ_AP014940.1|WP_172437153.1|1320019_1320580_+|sigma-70-family-RNA-polymerase-sigma-factor
MGEITVLLGHARGGDGAAWDRVVHLLYADLKRLARRASAGSGGQDVTALVHDCYLRLDRGGADGIESRAHFLSVAAMAMRQLLINHARDRIAGKRGGQHAHTTLGKADLDAARAAYCEAEEMVMIDAALKRLGDADARLVRVLECRLFAGLSEEETALALGLPLRSAQRLWQQARERLRTLLDQAA
>NZ_AP014940.1|WP_096377002.1|1320590_1322888_+|serine/threonine-protein-kinase
MSLRDRLLEPQGPLRGALFGELLRSRFGACELQPGERIGAWRIVRELGRGGMGLVFLAERDDGEFEQRVALKLLPDAATSPDSEALFRRERQFLAGLSHPNIARLVDGGHTDDGHLWFAMEYVEGPPIDRHASVHALDERARVALLLPALEAVEFAHARLLIHRDIKPGNVLVDARGQARLLDFGIAGLAQDGDPAAAFTPDFASPEQCSARPVGTASDVWQLGRLLDTVLRADTDAPPSRDLQAIVAEAMREAPEQRYPTVVALKNELLRYLQRRPVRARRGGPAYRLRRLAQRHPFGTAGSALAALALIALAAAFAVQSAAEQRRLLQARDETAAINRFLSEDILGASDPFEGAGDGRPIAEQLEDGVQRAQARFRDHPAVAGRIVLALGKSLLARGRYAAAATAADRAAVLLGGVADPRDAADAELLRATVDMYRGLPQRAQPRLERLQERYPYRPGGASPLEWHIQVARGWNAMLLSRFGECVAIYTELLARPGAVGDGDLGDAYNSLSLCQVAIGAAEQGLRSGERAERHAAAANGPHSGNAAIARIRIAVALSALGRHDQATARFRREVDALIGLVGENHGTTATYMDHLGLLYLCAGDNERAAQWTGRGLRARQQVFGPQHPWTVGVQAQYVVALLRSGRIEAARRIVAEVERMQGEVDEPGSQVAIHRGLGEWYLREGRNDEAIRHYRAARELASRPGMAYRWNLHAIDAGLGLALSRAGQSAQAREAYLRYGGSAAYDSRCVGGPRMEADLDRLRY
>NZ_AP014940.1|WP_145959979.1|1323733_1324186_+|hypothetical-protein
MRWQQVMQIEAQKQEAADRLAVKAKLDREQAIDFGRQLDSLTAFYETVITLLLGALAVVTALAVWTIKVVSKSQAEETARAAVIEILGGHDDFRQRLAKEVEVQLEFALDVVREQFASGGVPEDSVVTNPQARKEKGPKPHVVLRTRNPK
>NZ_AP014940.1|WP_096377003.1|1324212_1324737_+|ImmA/IrrE-family-metallo-endopeptidase
MAVVKRRPAPAVVAVELKSLDQVRHLMAESGLGGVPVDVASVAALLGMHLQYEQMSEEMSGYLENRAGRWVIGVNSLHAGVRQRFTIAHEVAHYVLHRDQQGSFRDVIFMRRSMNANAMEKQADRFAAELLMPESQVVSDIRGGLLNVHALAARYNVSALAMKYRLQNLGYAVS

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Crispr_ID: NZ_AP014940_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_4

1444593-1444743

Orphan

Consensus_repeat	Method
CCTGTAGGAGCGGCGCAAGCCGCGACCGCGCCGCCACGCCGCCCGGCGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP014940_4

>merge|NZ_AP014940|4|1444593-1444743|CRISPRCasFinder
CCTGTAGGAGCGGCGCAAGCCGCGACCGCGCCGCCACGCCGCCCGGCGCCACCGCGATCGAGCCGCGTTCCCCCTGCGGACCGCACGAAACCGCCCGCAGCCCCTGTAGGAGCGGCGCAAGCCGCGACCGCGCCGCCACGCCGCCCGGCGC

>NZ_AP014940|4|4|1444593-1444743|CRISPRCasFinder
CCTGTAGGAGCGGCGCAAGCCGCGACCGCGCCGCCACGCCGCCCGGCGC	CACCGCGATCGAGCCGCGTTCCCCCTGCGGACCGCACGAAACCGCCCGCAGCC
CCTGTAGGAGCGGCGCAAGCCGCGACCGCGCCGCCACGCCGCCCGGCGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_096377083.1\|1443964_1444495_+\|adenine-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|235028
NZ_AP014940.1\|WP_096377086.1\|1448176_1448827_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096377081.1\|1442449_1442719_+\|DUF2007-domain-containing-protein	unknown	unknown	gnl\|CDD\|378182
NZ_AP014940.1\|WP_145959987.1\|1451682_1453200_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_172437157.1\|1435061_1436909_+\|DUF1302-domain-containing-protein	unknown	unknown	gnl\|CDD\|377751
NZ_AP014940.1\|WP_074863048.1\|1448823_1449771_-\|DNA-binding-transcriptional-regulator-OxyR	unknown	unknown	gnl\|CDD\|182999
NZ_AP014940.1\|WP_096377080.1\|1439767_1440343_-\|nucleoside-deaminase	unknown	unknown	gnl\|CDD\|238612
NZ_AP014940.1\|WP_096377076.1\|1433505_1434840_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340927
NZ_AP014940.1\|WP_096377078.1\|1437530_1438220_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|235334
NZ_AP014940.1\|WP_096377089.1\|1453249_1454863_-\|discoidin-domain-containing-protein	unknown	unknown	gnl\|CDD\|366285
NZ_AP014940.1\|WP_096377079.1\|1438397_1439468_-\|23S-rRNA-(cytidine(2498)-2'-O)-methyltransferase-RlmM	unknown	unknown	gnl\|CDD\|236971
NZ_AP014940.1\|WP_096383151.1\|1446718_1447369_+\|peptide-methionine-(S)-S-oxide-reductase-MsrA	unknown	unknown	gnl\|CDD\|234604
NZ_AP014940.1\|WP_096377085.1\|1447430_1448003_-\|DJ-1/PfpI-family-protein	unknown	unknown	gnl\|CDD\|153234
NZ_AP014940.1\|WP_096377075.1\|1433174_1433486_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096377084.1\|1444811_1446485_-\|peptide-N(4)-(N-acetyl-beta--glucosaminyl)asparagine-amidase	unknown	unknown	gnl\|CDD\|371971
NZ_AP014940.1\|WP_096377082.1\|1442957_1443902_+\|DMT-family-transporter	unknown	unknown	gnl\|CDD\|273359
NZ_AP014940.1\|WP_096377087.1\|1450870_1451398_+\|carboxymuconolactone-decarboxylase-family-protein	unknown	unknown	gnl\|CDD\|129859
NZ_AP014940.1\|WP_096377090.1\|1455588_1457460_-\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|276809
NZ_AP014940.1\|WP_074863051.1\|1449936_1450476_+\|peroxiredoxin	unknown	unknown	gnl\|CDD\|239313
NZ_AP014940.1\|WP_172437158.1\|1440353_1442129_-\|glutamine--tRNA-ligase/YqeY-domain-fusion-protein	unknown	unknown	gnl\|CDD\|235424

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_096377083.1\|1443964_1444495_+\|adenine-phosphoribosyltransferase	gnl\|CDD\|235028	PRK02304, PRK02304, adenine phosphoribosyltransferase; Provisional.	4.23788e-83
NZ_AP014940.1\|WP_096377090.1\|1455588_1457460_-\|tetratricopeptide-repeat-protein	gnl\|CDD\|276809	sd00006, TPR, Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes.	1.48648e-13
NZ_AP014940.1\|WP_096377081.1\|1442449_1442719_+\|DUF2007-domain-containing-protein	gnl\|CDD\|378182	pfam09413, DUF2007, Putative prokaryotic signal transducing protein. This is a family of putative prokaryotic signal transducing proteins of Pii-type.	1.61182e-08
NZ_AP014940.1\|WP_172437157.1\|1435061_1436909_+\|DUF1302-domain-containing-protein	gnl\|CDD\|377751	pfam06980, DUF1302, Protein of unknown function (DUF1302). This family contains a number of hypothetical bacterial proteins of unknown function that are approximately 600 residues long. Most family members seem to be from Pseudomonas.	1.09482e-160
NZ_AP014940.1\|WP_074863048.1\|1448823_1449771_-\|DNA-binding-transcriptional-regulator-OxyR	gnl\|CDD\|182999	PRK11151, PRK11151, DNA-binding transcriptional regulator OxyR; Provisional.	4.83032e-110
NZ_AP014940.1\|WP_096377080.1\|1439767_1440343_-\|nucleoside-deaminase	gnl\|CDD\|238612	cd01285, nucleoside_deaminase, Nucleoside deaminases include adenosine, guanine and cytosine deaminases. These enzymes are Zn dependent and catalyze the deamination of nucleosides. The zinc ion in the active site plays a central role in the proposed catalytic mechanism, activating a water molecule to form a hydroxide ion that performs a nucleophilic attack on the substrate. The functional enzyme is a homodimer. Cytosine deaminase catalyzes the deamination of cytosine to uracil and ammonia and is a member of the pyrimidine salvage pathway. Cytosine deaminase is found in bacteria and fungi but is not present in mammals; for this reason, the enzyme is currently of interest for antimicrobial drug design and gene therapy applications against tumors. Some members of this family are tRNA-specific adenosine deaminases that generate inosine at the first position of their anticodon (position 34) of specific tRNAs; this modification is thought to enlarge the codon recognition capacity during protein synthesis. Other members of the family are guanine deaminases which deaminate guanine to xanthine as part of the utilization of guanine as a nitrogen source.	7.30012e-30
NZ_AP014940.1\|WP_096377076.1\|1433505_1434840_-\|MFS-transporter	gnl\|CDD\|340927	cd17369, MFS_ShiA_like, Shikimate transporter and similar proteins of the Major Facilitator Superfamily. This subfamily is composed of Escherichia coli shikimate transporter (ShiA), inner membrane metabolite transport protein YhjE, and other putative metabolite transporters. ShiA is involved in the uptake of shikimate, an aromatic compound involved in siderophore biosynthesis. It has been suggested that YhjE may mediate the uptake of osmoprotectants. The ShiA-like subfamily belongs to the Metazoan Synaptic Vesicle Glycoprotein 2 (SV2) and related small molecule transporter family (SV2-like) of the Major Facilitator Superfamily (MFS) of membrane transport proteins. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	8.96306e-88
NZ_AP014940.1\|WP_096377078.1\|1437530_1438220_-\|hypothetical-protein	gnl\|CDD\|235334	PRK05035, PRK05035, electron transport complex protein RnfC; Provisional.	0.000611892
NZ_AP014940.1\|WP_096377089.1\|1453249_1454863_-\|discoidin-domain-containing-protein	gnl\|CDD\|366285	pfam00754, F5_F8_type_C, F5/8 type C domain. This domain is also known as the discoidin (DS) domain family.	1.34042e-16
NZ_AP014940.1\|WP_096377079.1\|1438397_1439468_-\|23S-rRNA-(cytidine(2498)-2'-O)-methyltransferase-RlmM	gnl\|CDD\|236971	PRK11760, PRK11760, putative 23S rRNA C2498 ribose 2'-O-ribose methyltransferase; Provisional.	0
NZ_AP014940.1\|WP_096383151.1\|1446718_1447369_+\|peptide-methionine-(S)-S-oxide-reductase-MsrA	gnl\|CDD\|234604	PRK00058, PRK00058, peptide-methionine (S)-S-oxide reductase MsrA.	2.31708e-145
NZ_AP014940.1\|WP_096377085.1\|1447430_1448003_-\|DJ-1/PfpI-family-protein	gnl\|CDD\|153234	cd03140, GATase1_PfpI_3, Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.	4.13998e-51
NZ_AP014940.1\|WP_096377084.1\|1444811_1446485_-\|peptide-N(4)-(N-acetyl-beta--glucosaminyl)asparagine-amidase	gnl\|CDD\|371971	pfam12222, PNGaseA, Peptide N-acetyl-beta-D-glucosaminyl asparaginase amidase A. This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 558 and 775 amino acids in length. There is a conserved TGG sequence motif. PNGase A is a protein which cleaves glycopeptides.	2.40676e-71
NZ_AP014940.1\|WP_096377082.1\|1442957_1443902_+\|DMT-family-transporter	gnl\|CDD\|273359	TIGR00950, Uncharacterized_inner_membrane_transporter_YicL, Carboxylate/Amino Acid/Amine Transporter. [Transport and binding proteins, Amino acids, peptides and amines].	8.40458e-09
NZ_AP014940.1\|WP_096377087.1\|1450870_1451398_+\|carboxymuconolactone-decarboxylase-family-protein	gnl\|CDD\|129859	TIGR00777, AhpD_protein., alkylhydroperoxidase, AhpD family. Members of this family are alkylhydroperoxidases, which catalyze the reduction of peroxides to their corresponding alcohols via oxidation of cysteine residues. In these alkylhydroperoxidases, the cysteines are located in a conserved -CXXC- motif located towards the COOH terminus. In Mycobacterium tuberculosis, two non-homologous alkylhydroperoxidases, AhpD and AhpC, are found in the same operon. [Cellular processes, Detoxification].	6.46982e-54
NZ_AP014940.1\|WP_074863051.1\|1449936_1450476_+\|peroxiredoxin	gnl\|CDD\|239313	cd03015, PRX_Typ2cys, Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant (TSA) proteins, which confer a protective role in cells through its peroxidase activity by reducing hydrogen peroxide, peroxynitrite, and organic hydroperoxides. The functional unit of typical 2-cys PRX is a homodimer. A unique intermolecular redox-active disulfide center is utilized for its activity. Upon reaction with peroxides, its peroxidatic cysteine is oxidized into a sulfenic acid intermediate which is resolved by bonding with the resolving cysteine from the other subunit of the homodimer. This intermolecular disulfide bond is then reduced by thioredoxin, tryparedoxin or AhpF. Typical 2-cys PRXs, like 1-cys PRXs, form decamers which are stabilized by reduction of the active site cysteine. Typical 2-cys PRX interacts through beta strands at one edge of the monomer (B-type interface) to form the functional homodimer, and uses an A-type interface (similar to the dimeric interface in atypical 2-cys PRX and PRX5) at the opposite end of the monomer to form the stable decameric (pentamer of dimers) structure.	1.45144e-84
NZ_AP014940.1\|WP_172437158.1\|1440353_1442129_-\|glutamine--tRNA-ligase/YqeY-domain-fusion-protein	gnl\|CDD\|235424	PRK05347, PRK05347, glutaminyl-tRNA synthetase; Provisional.	0

>NZ_AP014940.1|WP_096377083.1|1443964_1444495_+|adenine-phosphoribosyltransferase
MTDPLLPIQRLIRSVADFPKPGVTFRDVTPMLADAGGFARCIDALAEPWQGSGVQAVCGIESRGFIFGAALAQKLHAGFVPLRKPGKLPPPLVTVEYELEYGRDALQARSDALKPGERTLIVDDVLATGGTLAAARELVERLDAVLVGASVLIELPALGGRSRWSGEAPVHSLLRY
>NZ_AP014940.1|WP_096377082.1|1442957_1443902_+|DMT-family-transporter
MNAASSSTSPTASGNGPLLQMLLGASVISSSAVFVRWVEIGPGASAFWRMALAAAILLLLLGQPWRPGRLRAWRPAPRVLGLVMLSAVFMAFDLWMWHRSIVYVGVGLSTLLANFQVFVLAGAGALFLGERAGWKLWVGLSLGLVGLALLLAPGWEHMDARFRLGVFFGLAAALAYGGFLLAFRAAQARRGDTPNEALQWWLCVGCVLVLGATVPLGGENMWPQSAHDWLILTAYAAIAQVLGWLVIGRAMPLLPAGIVGLCLLLQPLLAYVWDVLIFHKQLGGLELLGIALSLAGIFLGLARGDQPLFSRKPR
>NZ_AP014940.1|WP_096377081.1|1442449_1442719_+|DUF2007-domain-containing-protein
MRVVYEAAHLIDAHLVRHALEDAGIPVFLRGEALVGGMGELPLFGAVQVCVPDPAWPQADAVVQALALGDPPAEPEPPAALSPPAWLPA
>NZ_AP014940.1|WP_172437158.1|1440353_1442129_-|glutamine--tRNA-ligase/YqeY-domain-fusion-protein
MPRRMSADPSRLAPETPTDAAPAQKQDFVRQIVRDDLASGKHQAVRTRFPPEPNGYLHIGHAKAICLDFGVASEFGGRCNLRFDDTNPAKEDPEYVEAIQEDVRWLGFEWAELRHASDYFEVFYLAAQKLIRQGDAFVCDLSAEEVRAYRGSLNEPGRNSPYRERSVEENLDLFARMRAGEFADGARTLRAKIDMASGNINLRDPALYRIKKVAHQNTGDAWPIYPMYDFAHSLSDSCEGITHSLCTLEFEDHRPLYDWCVARVDLPNSPDLLAPLLAKGYPNEAAIPRQIEFSRANLNYTVMSKRKLMVLVQEKLVDGWDDPRMPTLQGIRRRGYTPASLRLWAERLGVSKQNSVIDYSVLEGCLREDLDAAAARRMAVIDPLKLVIANLPDSHEESLHFANHPKDERFGSRQVPFSNQLWIEREDFEEVPPKGFKRLIPGGEVRLRGAGILRCDEVIKDEAGKIVELRGTLDPESRPGMAGADRKIKGTIHWVSARHAAQAQIRLYDRLFDVAAPDDDSDGKTYQDHLNPNSRRTVVGYVEPSAAQAAPEQAFQFERVGYFVADRYDHRSDAPVFNRSVTLRDTWASKE
>NZ_AP014940.1|WP_096377080.1|1439767_1440343_-|nucleoside-deaminase
MSTKIQNPLTRQVQLLLPDWIDGAVDRSRVYASDEDKVVLAIELSRRNVELRTGGPFGAVVFDGHDRVVGVGVNRVVPQNCSVAHAEMMAFMCAQTAVSQFRLNELGPMTLATSAQPCCMCYGASFWAGINNLLIGARSEDVMRLTEFDEGPLPADWIGELERRGIAVRRDLQREAACEVLRKYGESGVSY
>NZ_AP014940.1|WP_096377079.1|1438397_1439468_-|23S-rRNA-(cytidine(2498)-2'-O)-methyltransferase-RlmM
MTDSALFCLCRAGFEPELAAELSERAARAGHPGYARTQRNSGYVEFVLEDAAAASRALPWSSLIFARQKLVRLADLRGLDPSDRIAPMLAALDAVGGAGLNVSSFGELWVEHPDSDEGKPLAGLARSFGNALRPALRKAGWLSKHDDPSRPRLHVVFLAGDHAVLAMSEPLDSAPWPLGIPRLKMHPDAPSRSALKLEEALLTLLDPEERERRVRDNMQAADLGAAPGGWTWVLMRNGMKVTSVDNGPLRQALLDSGRVDHLRADGFTWQPKRTLDWMVCDMVESPARVAERMATWFRENWCRQAIFNLKLPMKKRWEETRICLEAFEHQAHRPLIVRARQLYHDREEITVFATPR
>NZ_AP014940.1|WP_096377078.1|1437530_1438220_-|hypothetical-protein
MRTHAIKRHSLLMLATVAALAASAASAQVPGKVQSKHDAVEKADVAAQDARQARDSASSAQAAATAAAQTRQQGAISERGAIAAQATAQQAQRAAEDARQASQQAKRASEDARSAQAAATAGSNPTGAAIEARAALSEARTANAVAADAGSVARAAAAATAEANQLPDRVIAPPSDGRSVDFAALDANGDGVISREESRAHGALSANFLAVDLDADGRISANEIAAWRR
>NZ_AP014940.1|WP_172437157.1|1435061_1436909_+|DUF1302-domain-containing-protein
MSTSILAALAAAPAAAADFELADGRVHGQWTTRVVAGTAVRTGKAQPHLLGKGYASDGRPKGGTGADTADDGNLNFGRGDAFSSLFKIVQSVDLKYRDVGLNLSARTWYDATLDRHEVRQGNVPNGFDPSAPLSDAGFSRSNKFSGFLWLNAYAYGHLKLDDDSALDVRVGKQAVKWGGGLFFSGVNQINPVDYTTLRRPGTDAASEAQIPVEMLWAKWTLDSKLSLEGFWQWNWRPSEYDPCGTFFSGSDLGIERGCAGIQSNAYYPLNSASSGAGPWLSDGFMQSMGAILPRDRDRYGSDRGQYGLSMRYRDEASGRGWGAYYLRINSRAPYLDATVIDPARTDPTLAPRLIAAGVPEVYAQLSARLSTIREIWEYPDDIRILGLSAQTRWRGWNLGAELSHTRGQPVQLNTADMFRALTSNGGPIGARNAALAPGAVLRGYDRVDKNQLMLNVQRSFAGVLGAKQATLAGEAMLSRADLPPLSQARYGRGFHWGFSPQGYGGACPPIQNPRGCVDQGFYTRNAWGYRLRAQLDYALGADWTVSPSLSFGHDVRGFAIDNQLVEDRRQLTLGVSAKYGSRYFASVSYTDYAGSAHYDPLADHDYASVAVGATF
>NZ_AP014940.1|WP_096377076.1|1433505_1434840_-|MFS-transporter
MNSPQSMNSPALAATPAGAAPLNRKDARTLLLSALGGALEFYDFVIFVFLTETLRKLFFPVGTPEWLGTLQVYGIFAAGYLVRPIGGVIMAHFGDRSGRKRMFTLSVFLMALPTLFIGLLPTYAQIGLAAPLLLLFLRIVQGIAIGGEVPGAWTFVAEHAPRGRVGFACASLSAGLTAGILIGSLISTAINTLLAPTQVLDWGWRVPFLIGGVFGFLAVYLRRWLSETPVFTAMRESRQLVQELPLKQVLREHRAGVVLSMLVTWLLTAAIVVIILMTPTIVQQKFGMAPAHAFLGNSLAAFCLTLSAVGGGWLVDRIGRGRALLIGSLGVLVSSFALYYDLNHGAHNFLLLYALAGVFVGVVGVIPAVMVAAFPAPVRFSGLSFSYNVAYAVFGAATPPLIGGYLAPHFGGMAPAYYVMAVALVGVAVSVYLLGPNQQRFHEQ
>NZ_AP014940.1|WP_096377075.1|1433174_1433486_+|hypothetical-protein
MRRDKSPTCFLASILAMFPNWVWAISRCPPEAGEKSKAFVILGFAILGVFVALGVLVRRAMLRLARDRPAWARTLLAMAAYVLMLGCWLLGVSIFWMGFVLTC
>NZ_AP014940.1|WP_096377084.1|1444811_1446485_-|peptide-N(4)-(N-acetyl-beta--glucosaminyl)asparagine-amidase
MSARPASRLNATAHRTAARLPALVLALLCAHAAPALAADEFGSDWDDPRTADPPVTRPATRSCTVEILDTAFADFDWHLGQIAPPAACPGPWSKVVLEMDGQVKGVQYDRLGHLEIGGVTVFSTSTPEPSRDGIGWHVEKDISGYAALLKSPQQVRMALGNVVNDTYTGVIYVQARVVFYNADRRHPAADSADAVAPLANARRDGGDLVGEYTLPANATRWSGEVYATGSGGGCEEFWYFTAPPEANYSCPAQHGPYREVQVLIDGRVAGIAMPYPHIYTGGWSNPFLWYVLPAPRAFNIEPIRYDLTPFIGLVNDGRAHEVRFRVANLPDGASGWTLQPNLQAWTDPRRGATGGRLLSYELTPLAARSTYTAKPDGTFQVDTRGGHRLRATGYVDTSKGREYTTVERIVGNTGLHRWGADENPDGINAQWNDTQTVRRLGRGLPTVSTLAQRFGFDGAISVTPSGSAQRIVTTMKIFDHADWLQTPGLGQPAAAQVKRNTFEGEAGWNYGVPRPERHATGHSTQRHRSYGTQGCYDHEISQRNGFIDTDRYRCGAP
>NZ_AP014940.1|WP_096383151.1|1446718_1447369_+|peptide-methionine-(S)-S-oxide-reductase-MsrA
MPGIGAFKQRMPQREDALPGRATPMPLHNAHYLSGAKLRDAYPGLARVQFGLGCFWGAERKFWSLPGVAVTAVGYSGGYTPNPTYREVCSGQTGHAETVLVVYDPAKIGFDDLLKVFWESHDPTQGMRQGNDTGSQYRSAIYCEDEGQYRAALSSRDAFQAKLREAGFGEITTEITAPPAPEFYYAEDDHQQYLAKNPAGYCGLGGTGVSCPIGAL
>NZ_AP014940.1|WP_096377085.1|1447430_1448003_-|DJ-1/PfpI-family-protein
MTRRIVLLMIDRPADWEYGPLVGAAHAWFGIDVVSASIDAAPLTTMGGLSLQPQRRLQELAADDADLWVVPGSPLWDEAPAPAPIVHALRERAARGGAIAGICGGTRALAAAGLLNARAHTSNEPAYLDAVPGYSGQAHYREQACVSADGIVTAPGTSPVSFAEACLLRVLPEQAEGIAQMRAMFAREFA
>NZ_AP014940.1|WP_096377086.1|1448176_1448827_-|hypothetical-protein
MIEIRRDWLAAALALSAIGWWYSPLSPRAPYFPAVAPGDTPRCPPPPLVAAGAEPLQTAVPDGLAPFRLKPGTLTPLAGFSLDARVLSRRDYRSDRLADFAPTDLAVGWGRLSEDAVLARMSFRQEVRFLSYYWPERPPLPIPEIGRSSANLHIIPADAAVAQALKRARAGERVRVDGWLVRIDARDGWQAVSSLSREDQGAGACEIVYACAIASH
>NZ_AP014940.1|WP_074863048.1|1448823_1449771_-|DNA-binding-transcriptional-regulator-OxyR
MNLRDLKYLVALADHKHFGRAAAASFVSQPTLSTQIKKLEDELGVSLVERAPRRVMLTPVGRDIAERARKVIADVEQMSEIARRSQDPEAGTVRLGLFPTLGPYLLPHVVPNLRKRFPRLELLLVEEKTDQILARLRDGRLDAGLLALPIHDDQLHVEPLFDEPFILAVPQQHPMAARDTLDLHDLDDQHLLLLEEGHCLRDQALDVCRLAGADERDGFRATSLETLRQMVAAGVGITLLPTLAVQPPVPNSPDIRLLRFNGAAPHRQIGMLWRRSSAMSEFLMQLADELRKLPPALLQPPGNVAGKRKQAPQPR
>NZ_AP014940.1|WP_074863051.1|1449936_1450476_+|peroxiredoxin
MLSIGEKFPKFKVKATVGIDNLDTAFADIDNDTYKGKWLLVFFYPKDFTFVCPTEIKGFGDLNQQFLDRDCQVLAASTDSEFVHLAWRKDHKDLRDLPFPMLADIKKDLTSALGILTDDGVAQRATFLVDPDGIIRFVYVTDGSVGRNPQEVLRVLDALQTDELCPCNWNQGENTLKVA
>NZ_AP014940.1|WP_096377087.1|1450870_1451398_+|carboxymuconolactone-decarboxylase-family-protein
MSLTDLRNALPDYAKDLKLNLDSVLSDAGSQGLDAKQIRAIALSCAIASRYKPLTQAVEAFAAEKLSAEEIAGAKAAAAVMGMNNIYYRATHLIQNEEYGQLRAGLRMNIMANPGIDKMTFELASLAVSAINGCGACMDSHEKVLRKHEISAQGVQSALKIAAVVHAVAVVLEQA
>NZ_AP014940.1|WP_145959987.1|1451682_1453200_+|hypothetical-protein
MRDPLRVAAKPDEGSVVVSLTNNTGEVNQMDVIELEEMSRLDKNGQGRFYVMNRVGGPLSRDTSLFAARLPAGRYRFRILRDMQPQNLQGSIYLPLNLHQIEGIGEFTVEAGAHADLGRLVITAVNTMVAVGRSREVVANRALIERHAPAYVELSSAPPKGGWIRAAPPDDGDVESFALARPQGATGFSELSTGEVIGGSRMGTVLLRETDGQWRKFARTGTLDAIAWTLPYEIDGHIAVVAGDLDTLALVGRDGSVRQVDTGDLPHGNLFFVDRSADGAQWIVGVSDDRQGALYVSSKLDGGRWTRMRGDTTGFSVWSGQRSVWAWRRPGGIGFASSQTPRIACYDYAERQWSERDTPGRRKLFALSPGVGDALGVLTTPGGGLVGIFASSFYSLDCGAAWAETRSPYKVKVMPPLALASGRLLEGGGVFRDTGLYASRVGSDLWTKLGVQVNFNENVWALPKAGLLAVTRGADGFEVIQHSSDEGASWTVEMSSFDLRRGASR
>NZ_AP014940.1|WP_096377089.1|1453249_1454863_-|discoidin-domain-containing-protein
MPKPTPHSTASARSRRRCCASALALSLAALAAPAVGAESAIFGGGPFYSGGQTVINDLKASGFTTVFLWSIHIEDNGDLVYNDIPIVKNGAYIGGDADWPARLASLKTAPTSVKRVEVSIGAWGVPDFERMAKLANGTAAGCGTTIVCGTGSGSILYRNFQALKTVTGADAVNFDDESYYNVADTTTFGNMLVGLGYKITFAPYTNQTFWKGVKDNLGASVDRIYLQVYDGGAGNNPATWNTAMGMTVMPGLWTKHGSGCSAGDSPASVESRMAGWKTSAGINGGFLWLYDDIQKCWAQGTSAQYAAAINNALSGNTAPVANFGVTVNGLTASFSDSSSDADGSIASRSWNFGDGSSSTATNPPHTYASAGNYSVSLTVTDNGGASNTKTSTVSVGAGNVNLALNKPTTSSAACNSNESGAKAVNGSVSGGTTDKFCSLASPAWLQVDLGSAQTVSSFTVKHAGAGGEQASWNSKAFTIQTSTNGSTWSTPVSATANTGNTSTHAITATSARYIKLNVTTPTQNGDPATRIYEFEVR
>NZ_AP014940.1|WP_096377090.1|1455588_1457460_-|tetratricopeptide-repeat-protein
MTLAADVTAPIAATLRLRPAGADGAAPAGAPDRRFAIDADFRHGGTWAGVAELAELAWRELGESGRDDLIDAHNPELHMALARHRERIALKYACLTETAHDAERTRNFPLDRAYRLVHGLVGLMLDWKRALAPQQRWRVVAFGYDHAEHLAARFFAELARRGAAHGIEVIVHSALDAQALAQRAPGLHAQAASDAGAAPSAPAALDDAGYAALQPRLERGEPLAWEIHAPALIAYHRARGEDALAARASLRALCLSNHYGYYHESASFAEAVLAHFDDMVGDDEDARWNYIGNIFQGLVSAGRQEFALELILTRAEPHLRRRELRAKMHYLLSMIHLRYARKPDLALAEHYILLAAQDIAAARGAIDDADQTFLRVFIDNGLAFLRVRQGRARDALALCQEGYALLTRELGDDRHALHRSVLQYNTAQVYVMLDRAEDALAHYRKSIEMDPYYSEYYNESGNLLQRQGRFEEALALYELAVRYSAPYPEVHFNRGVCQSQTGDWEAALASFALSLELNPQQPEIHQIRAEIHEQSGDADAALADYDAAIALAADSVAARVNRAVLHYGRGDYARALADMDRAIALDPDNPEHYENRAEIHKSMRREELYRHDLDRAEACRAAA

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Crispr_ID: NZ_AP014940_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_5

1574811-1574916

Orphan

Consensus_repeat	Method
CGGCGGAAGCCGGAATCCAACCGCAGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP014940_5

>merge|NZ_AP014940|5|1574811-1574916|CRISPRCasFinder
CGGCGGAAGCCGGAATCCAACCGCAGCGACATAGCTCCGCCGCAACGTCCGAAGCCACGCAACCCCCAGCCCGTTATCCCGGCGGAAGCCGGAATCCAACCGCAGC

>NZ_AP014940|5|5|1574811-1574916|CRISPRCasFinder
CGGCGGAAGCCGGAATCCAACCGCAGC	GACATAGCTCCGCCGCAACGTCCGAAGCCACGCAACCCCCAGCCCGTTATCC
CGGCGGAAGCCGGAATCCAACCGCAGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_096383172.1\|1577478_1578570_-\|pyrroloquinoline-quinone-biosynthesis-protein-PqqE	unknown	unknown	gnl\|CDD\|235397
NZ_AP014940.1\|WP_057948535.1\|1569154_1569547_+\|30S-ribosomal-protein-S11	unknown	unknown	gnl\|CDD\|180007
NZ_AP014940.1\|WP_074872153.1\|1566735_1567173_+\|50S-ribosomal-protein-L15	unknown	unknown	gnl\|CDD\|235523
NZ_AP014940.1\|WP_083383010.1\|1580685_1580769_-\|pyrroloquinoline-quinone-precursor-peptide-PqqA	unknown	unknown	gnl\|CDD\|178960
NZ_AP014940.1\|WP_096377141.1\|1572895_1574287_+\|3-deoxy-7-phosphoheptulonate-synthase-class-II	unknown	unknown	gnl\|CDD\|366662
NZ_AP014940.1\|WP_074872160.1\|1569561_1570191_+\|30S-ribosomal-protein-S4	unknown	unknown	gnl\|CDD\|235411
NZ_AP014940.1\|WP_074872172.1\|1578601_1578898_-\|pyrroloquinoline-quinone-biosynthesis-peptide-chaperone-PqqD	unknown	unknown	gnl\|CDD\|274818
NZ_AP014940.1\|WP_096377146.1\|1585156_1586362_+\|pyridoxal-phosphate-dependent-aminotransferase	unknown	unknown	gnl\|CDD\|235596
NZ_AP014940.1\|WP_074872162.1\|1570349_1571348_+\|DNA-directed-RNA-polymerase-subunit-alpha	unknown	unknown	gnl\|CDD\|235359
NZ_AP014940.1\|WP_074872164.1\|1571565_1571940_+\|50S-ribosomal-protein-L17	unknown	unknown	gnl\|CDD\|235522
NZ_AP014940.1\|WP_074872181.1\|1584199_1584706_+\|peptidylprolyl-isomerase	unknown	unknown	gnl\|CDD\|223725
NZ_AP014940.1\|WP_074872176.1\|1581000_1581474_-\|DUF2127-domain-containing-protein	unknown	unknown	gnl\|CDD\|378298
NZ_AP014940.1\|WP_096377140.1\|1572303_1572813_+\|disulfide-bond-formation-protein-B	unknown	unknown	gnl\|CDD\|235294
NZ_AP014940.1\|WP_096377143.1\|1575383_1577039_-\|amidase	unknown	unknown	gnl\|CDD\|236161
NZ_AP014940.1\|WP_096377142.1\|1574291_1574762_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_074872158.1\|1568784_1569141_+\|30S-ribosomal-protein-S13	unknown	unknown	gnl\|CDD\|235358
NZ_AP014940.1\|WP_096377145.1\|1579691_1580621_-\|pyrroloquinoline-quinone-biosynthesis-protein-PqqB	unknown	unknown	gnl\|CDD\|235361
NZ_AP014940.1\|WP_074872178.1\|1581903_1583733_-\|translational-GTPase-TypA	unknown	unknown	gnl\|CDD\|224138
NZ_AP014940.1\|WP_096377144.1\|1578894_1579695_-\|pyrroloquinoline-quinone-synthase-PqqC	unknown	unknown	gnl\|CDD\|235353
NZ_AP014940.1\|WP_074872155.1\|1567180_1568554_+\|preprotein-translocase-subunit-SecY	unknown	unknown	gnl\|CDD\|236412

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_096383172.1\|1577478_1578570_-\|pyrroloquinoline-quinone-biosynthesis-protein-PqqE	gnl\|CDD\|235397	PRK05301, PRK05301, pyrroloquinoline quinone biosynthesis protein PqqE; Provisional.	0
NZ_AP014940.1\|WP_057948535.1\|1569154_1569547_+\|30S-ribosomal-protein-S11	gnl\|CDD\|180007	PRK05309, PRK05309, 30S ribosomal protein S11; Validated.	8.39965e-82
NZ_AP014940.1\|WP_074872153.1\|1566735_1567173_+\|50S-ribosomal-protein-L15	gnl\|CDD\|235523	PRK05592, rplO, 50S ribosomal protein L15; Reviewed.	3.61815e-65
NZ_AP014940.1\|WP_083383010.1\|1580685_1580769_-\|pyrroloquinoline-quinone-precursor-peptide-PqqA	gnl\|CDD\|178960	PRK00284, pqqA, pyrroloquinoline quinone precursor peptide PqqA.	2.47505e-05
NZ_AP014940.1\|WP_096377143.1\|1575383_1577039_-\|amidase	gnl\|CDD\|236161	PRK08137, PRK08137, amidase; Provisional.	0
NZ_AP014940.1\|WP_074872160.1\|1569561_1570191_+\|30S-ribosomal-protein-S4	gnl\|CDD\|235411	PRK05327, rpsD, 30S ribosomal protein S4; Validated.	5.01517e-122
NZ_AP014940.1\|WP_074872172.1\|1578601_1578898_-\|pyrroloquinoline-quinone-biosynthesis-peptide-chaperone-PqqD	gnl\|CDD\|274818	TIGR03859, PQQ_PqqD, coenzyme PQQ biosynthesis protein PqqD. This model identifies PqqD, a protein involved in the final steps of the biosynthesis of pyrroloquinoline quinone, coenzyme PQQ. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other].	1.12799e-20
NZ_AP014940.1\|WP_096377146.1\|1585156_1586362_+\|pyridoxal-phosphate-dependent-aminotransferase	gnl\|CDD\|235596	PRK05764, PRK05764, aspartate aminotransferase; Provisional.	7.45811e-137
NZ_AP014940.1\|WP_074872162.1\|1570349_1571348_+\|DNA-directed-RNA-polymerase-subunit-alpha	gnl\|CDD\|235359	PRK05182, PRK05182, DNA-directed RNA polymerase subunit alpha; Provisional.	3.49522e-178
NZ_AP014940.1\|WP_074872155.1\|1567180_1568554_+\|preprotein-translocase-subunit-SecY	gnl\|CDD\|236412	PRK09204, secY, preprotein translocase subunit SecY; Reviewed.	0
NZ_AP014940.1\|WP_074872181.1\|1584199_1584706_+\|peptidylprolyl-isomerase	gnl\|CDD\|223725	COG0652, PpiB, Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family [Posttranslational modification, protein turnover, chaperones].	6.51268e-70
NZ_AP014940.1\|WP_074872176.1\|1581000_1581474_-\|DUF2127-domain-containing-protein	gnl\|CDD\|378298	pfam09900, DUF2127, Predicted membrane protein (DUF2127). This domain, found in various hypothetical prokaryotic and archaeal proteins, has no known function.	1.8583e-29
NZ_AP014940.1\|WP_096377140.1\|1572303_1572813_+\|disulfide-bond-formation-protein-B	gnl\|CDD\|235294	PRK04388, PRK04388, disulfide bond formation protein B; Provisional.	7.16025e-69
NZ_AP014940.1\|WP_074872164.1\|1571565_1571940_+\|50S-ribosomal-protein-L17	gnl\|CDD\|235522	PRK05591, rplQ, 50S ribosomal protein L17; Validated.	2.67899e-66
NZ_AP014940.1\|WP_096377141.1\|1572895_1574287_+\|3-deoxy-7-phosphoheptulonate-synthase-class-II	gnl\|CDD\|366662	pfam01474, DAHP_synth_2, Class-II DAHP synthetase family. Members of this family are aldolase enzymes that catalyze the first step of the shikimate pathway.	0
NZ_AP014940.1\|WP_074872158.1\|1568784_1569141_+\|30S-ribosomal-protein-S13	gnl\|CDD\|235358	PRK05179, rpsM, 30S ribosomal protein S13; Validated.	2.52883e-69
NZ_AP014940.1\|WP_096377145.1\|1579691_1580621_-\|pyrroloquinoline-quinone-biosynthesis-protein-PqqB	gnl\|CDD\|235361	PRK05184, PRK05184, pyrroloquinoline quinone biosynthesis protein PqqB; Provisional.	9.31094e-165
NZ_AP014940.1\|WP_074872178.1\|1581903_1583733_-\|translational-GTPase-TypA	gnl\|CDD\|224138	COG1217, TypA, Predicted membrane GTPase involved in stress response [Signal transduction mechanisms].	0
NZ_AP014940.1\|WP_096377144.1\|1578894_1579695_-\|pyrroloquinoline-quinone-synthase-PqqC	gnl\|CDD\|235353	PRK05157, PRK05157, pyrroloquinoline quinone biosynthesis protein PqqC; Provisional.	7.84134e-143

>NZ_AP014940.1|WP_096377142.1|1574291_1574762_+|hypothetical-protein
MNRTDAVAAPWRRNPALIAAGALSALAAFAHLGCIVFGAPWYRALGAGEGMARAAEAGDPTPALITLPIAAVLALWSLYAFSGAGLVRRLPLLRTALCAITAVYLLRGLALPPVMAEFPGRSAAFWWWSSGICLGIGLVHLVGLIRTWPRLRSRKA
>NZ_AP014940.1|WP_096377141.1|1572895_1574287_+|3-deoxy-7-phosphoheptulonate-synthase-class-II
MSASDRSNLRAVNLPADWSPTSWRERTALQLPTYPDQAELESALAELRHLPPLVTSWEILSLKQQLAEAQEGKRFLLQGGDCAESFDSCTSDVISNRLKVLLQMSLVLVHGMRKPVVRVGRFAGQYAKPRSADSETIDGVTLPSYRGDMVNGPAFTEAARKPDPRRMIKAHARSSMTMNFVRALIDGGFADLHHPEYWNLSWVGHSPLADEYRRMVNAIGDAVRFMETLSGSEVHNLNRVDFYTSHEALLLPYEESLTRQVPRHWGHFNLSTHYPWIGMRTAAVDGAHAEYFRGIRNPIALKVGPSVTPDQMLRTIDLLNPEDEPGRLTFIHRMGATAIADKLPPLLEAMRRDGRRVLWVCDPMHGNTESTSNGYKTRRFRNIRAEIEQSFELHAAAGTRLGGVHLELTGEDVTECLGGARELTESDLERAYRSTVDPRLNYEQALEVAMLIVRKQAQIAAPA
>NZ_AP014940.1|WP_096377140.1|1572303_1572813_+|disulfide-bond-formation-protein-B
MNPFKASFRIQFLLGFLACAGLLAYAVYLQFYQHLEPCPLCIFQRVAFAALGLMFLLGAIHGPGKPLGQRIWGVLALIAAGAGIAVAGNHVRLQHLPPDQVPACGPGLDYMMGAMPIGGVIRKVMTGSGECANVDWTFLGLAMPAWSLICFVVLAAWAAYAAFRARSSK
>NZ_AP014940.1|WP_074872164.1|1571565_1571940_+|50S-ribosomal-protein-L17
MRHQKAGRKFSRTSAHRDAMFTNMAASLIKHGLIRTTLPKAKELRRVAEPLITLAKVDGVANRRLAFSRLRDKEAVGTLFTTLGPRYATRPGGYLRILKCGFRAGDNAPMAYVELVDRPEAATE
>NZ_AP014940.1|WP_074872162.1|1570349_1571348_+|DNA-directed-RNA-polymerase-subunit-alpha
MTVTANQVLRPRGPQIERLNGNRAKVVIEPLERGYGHTLGNALRRVLLSSIPGFAITEVEIDGVLHEYTTVEGLEEDVLEVLLNLKDVAIRMHTGESSTLSLAKQGPGIVTAGDIKTDHNVEILNTDHVICHLTKDTAINMRLKIERGFGYQPAASRRRPDEETRAIGRLMLDASFSPVRRVAYAVEAARVEQRTDLDKLVLDIETNGTIDAEEAVRTAADILTDQLSVFGDFTHRDRGAQKPATSGIDPILLRPIDDLELTVRSANCLKAESIYYVGDLIQKTEVELLKTPNLGKKSLTEIKEVLAQRGLSLGMKLENWPPAGIASHGMMG
>NZ_AP014940.1|WP_074872160.1|1569561_1570191_+|30S-ribosomal-protein-S4
MARYIGPTCKLARREGADLGLKSSARALDSKCKLEQKPGQHGPTARKGKLSDYATQLREKQKVKRIYGLLERQFRNYYKKASTKKGNTGENLLQFLETRLDNVVYRMGFAVTRPAARQLVSHRGVTVNGKSVNLPSYQVKAGDIIALSERAQKQLRVQESLTVSSQMDLSPSWVEVDSKKFSGVFKAVPDRADLPADINEALIVELYSK
>NZ_AP014940.1|WP_057948535.1|1569154_1569547_+|30S-ribosomal-protein-S11
MAKPAAVKTKKKIKRVVTDGIAHVHASFNNTIITITDRQGNALSWATSGGAGFRGSRKSTPFAAQVAAEKAGRAALDYGVKSLEVRIKGPGPGRESAVRSLNNVGYKIINIIDVTPIPHNGCRPPKKRRV
>NZ_AP014940.1|WP_074872158.1|1568784_1569141_+|30S-ribosomal-protein-S13
MARIAGVNLPAQKHVWVGLQSIYGIGRTRSKQICDTAGVTSTTKIRDLSEPEVERLRAEVGKFVVEGDLRREIGIAIKRLMDLGCYRGLRHRRGLPLRGQRTRTNARTRKGPRKAIKK
>NZ_AP014940.1|WP_074872155.1|1567180_1568554_+|preprotein-translocase-subunit-SecY
MARSGNAMAGIGGGLGKFTELRQRLLFVIGALIVYRIGSYIPVPGINPEAMVKFMETKQGTIVDMFNMFSGGALHRFSLFALNVMPYISASIIVQLLVQIVPSLKAIQKEGESGRRKINQWSRMGAIPLAVFQAWGIAAGLQSSVAPDGVPVVYAPGMGFILTAVIALTAGTMFLMWLGEQITERGVGNGVSLIIFAGIVAGLPAAVLHMFEQIRNGDMSAIAAIVVILLVFGFTYLVVFVERGQRRITVNYARRQGGRNAYMNQASFLPLKLNMSGVIPAIFASSIVMFPATAATWFAQSNSGSGFSGFLQRLSQWLAPGEPVHMILYAGLIIGFAFFYTALVFNSQETADNLKKSGALIPGIRPGKATADYVDGVLTRLTAAGAIYLVIVCLLPEVMRTQLGTSFYFGGTSLLIVVVVVMDFIAQIQAHLMSHQYESLLKKANLKGGSRGGLARG
>NZ_AP014940.1|WP_074872153.1|1566735_1567173_+|50S-ribosomal-protein-L15
MRLNTLKPADGARQERTRVGRGIGSGLGKTAGRGHKGSFARSGKGKIKAGFEGGQMPMQRRLPKIGFRSKLAKDTAEVLLYQLDKLEAGEIDFAALKAAKLVPSTAKQAKIVKKGELTKKFVLKGVLATAGAKAAIEAAGGKIEE
>NZ_AP014940.1|WP_096377143.1|1575383_1577039_-|amidase
MPALSPAPRPIALACLAAFAAALAGCAGSPAPRPPQPIAASAAQAPRDFVPGDPLRIAEADLASLAARMAGGELSSARLTQAYLDRIAALDDAGPQLNAVIELNPNALNEARALDEERKAGRTRGPLHGIPVLIKDNIDAVPMVNSAGSLALAAHRPKQDAPLVAALRQAGAVILGKTNLSEWANFRSDRSISGWSGRGGLTRNPYALDRSACGSSSGTGAAVAASLAAVGVGTETDGSILCPAAMNGLVGFKPSVGLVSRTGIIPISHSQDTAGPMARSVADAAQLLNALAAADAGGDSAAQAAAGKRAQNFLAALDADALHGARLGLLRDTGIKLHPEQDAALQRTLKALRDAGATVVDVRMPNAGKWGAAEFEAMLYEFKDGLQRYLQSSDAPVKTLDELIAFNRANAAREMPFFGQELFEQAAKKGPLTDAAYRKAAAQARALAGAQGIDALMKKHRLAALIAPATTPAFMVDPVNGDAFGGASWGAAAVAGYPSLTVPMGEAQGLPVGLVFMGRRWDDAKLLSLGYAYEQITQARTAPKYRVTLSP
>NZ_AP014940.1|WP_096383172.1|1577478_1578570_-|pyrroloquinoline-quinone-biosynthesis-protein-PqqE
MSASPAPPLAVLLELTHRCPLACPYCSNPLQLVGLRQELDTAQWQRVLEQAAELGVLQAHFSGGEPTLRKDLAELLAHARAHGLYCNLITSGVGLSRERLIELQNAGLDHLQLSLQDSRADGADRIAGYQGAHARKLALARWCGELDLSLTLNAVIHRHNAERVGEMIELALELGAGRLEVAHTQYYGWGLKNRAALLPTRPQFDAVSAVVADARERLRGRLTIDYVTPDYYARRPKPCMGGWARRFLNITPEGKVLPCHAAETIEGLRFDSVLERGLDEIWRDSDAFNRYRGTDWMPEPCRGCEHRERDWGGCRCQALALSGRADTLDPVCEKSPDHAGLRALTERESQAPAPEFVYRRPGR
>NZ_AP014940.1|WP_074872172.1|1578601_1578898_-|pyrroloquinoline-quinone-biosynthesis-peptide-chaperone-PqqD
MSAAIDSGSVMRFPVGVRLQHDRTRERWVLLAPERVIELDDIAHAVLTHVDGRSDVEAIVAALARDYGADPGEIYGDVIDLFSTLLEKRMLAFAPQLT
>NZ_AP014940.1|WP_096377144.1|1578894_1579695_-|pyrroloquinoline-quinone-synthase-PqqC
MNAAAAPAAAPAPNARDAALAPNELEARLRAIGAERYHDKHPFHVLLHSGRLDRGQVQAWALNRFEYQRCIPLKDAALLARIEDPQLRRVWRQRIVDHDGERDGDGGIARWLHLTDALGLPRELVESGRALLPATRFAVQAYIHFVRERSLLEAIASSLTELFAPKIIGQRVAGMLANYDFVSKDALAYFDSRLHQAPQDADFALDYVKRHALSREQQESVLAALRFKCDVLWSMLDALHLAYVEPRLIPPGAFRPQEFFPQEPRP
>NZ_AP014940.1|WP_096377145.1|1579691_1580621_-|pyrroloquinoline-quinone-biosynthesis-protein-PqqB
MRILVLGAAAGGGFPQWNCNTPGSRRAWHEHDGAKRRSQASIAVSADGERWLLINASPDFRQQVLALPPLWPQRGLRHSPIEAVLLSSGEIDHIAGLLSMRERQRFDLWASARVHELLALNPIFDALHPDYVARKPLALETPVDIDGVDAPLGLRVTAFAVPGKVPLFMESRSETLQGNDDDTVGLEISDGRERFYYIPGCAALTAPLRERLRGAALVFFDGTLWRDDEMQRAGVGSKTGARMGHMSIAGGNGEDDAGTLAAFADLAVRRKLFIHLNTTNPVLDETSPERAHVRAQGWEVAEDGMELTL
>NZ_AP014940.1|WP_083383010.1|1580685_1580769_-|pyrroloquinoline-quinone-precursor-peptide-PqqA
MKTWSKPQILEVPCGCEINSYSSGDLF
>NZ_AP014940.1|WP_074872176.1|1581000_1581474_-|DUF2127-domain-containing-protein
MNPADPHYNADPKAHPGLHAIAMVEAVKGLLALSAASGLELLGPTPLQRWIELLIRRFHLDPEHGSMAWLAHSISPGSVHLAAGIVFAYAALHLFEAWGLWKAKAWASWLGCVGAALYLPFDIFAMVRHPGWLASAVLIINVIVVWVLARDILKRRR
>NZ_AP014940.1|WP_074872178.1|1581903_1583733_-|translational-GTPase-TypA
MSIERLRNIAIVAHVDHGKTTLVDCLLKQSGTLSERTVLAERAMDSNDQEKERGITILAKNTAITWQGNRINIVDTPGHADFGGEVERVLSMVDSVLILVDAMDGPMPQTRFVTQKAFAMGFKPIVVVNKIDRPGARPDWVIDQVFDLFDKLGATNEQLDFPIVYASALHGYASLDDAARSGDMTPLYEAIMKHVPPPEVDLDGPFQMRISQLDYSNFVGLIGIGRIQRGKVRRNMPVSVVDRHGKKRQGKVLQVLGFMGLERLETEEAEAGDIVAISGVADLSISDTVCALDAPEALPALTVDEPTISMTFQVNNSPFAGNKDLSGGKFLTSRQLRERLVRETLHNVALKVEEGSDPDKFLVSGRGELHLSVLIENMRREGFELAVSRPEVIIKEIDGKLMEPVEQLVVDIEEQHQGGVMEKLGTRKAQLKDMVSDGKGRVRLDYMIPARGLIGFQNEFRTLTQGSGLLFHVFDHYGPKEQGAIAKRINGVMIANAPGTTPAYSLGPLQDRGRLFAAEGDNVYEGQLVGIHSKDNDLTVNAIKTKPLTNMRASGKDDAIQLSPAIKYTLEQALDFIEDDELVEVTPKEIRLRKKFLTESDRKRASRAA
>NZ_AP014940.1|WP_074872181.1|1584199_1584706_+|peptidylprolyl-isomerase
MSLIATFDTSRGPIRVELAAEKAPLTVANFVNLAQRGFYDGLSFHRVIPNFMIQGGCPKGTGTGGPGYRFEDETRNGLGHERGVLSMANAGPGTNGSQFFITHIVCDWLDGKHTVFGKVLEGQQIVDTVQQGDKINSVKIEGDTAAVLAAKAERVAEWNKVLDAEARP
>NZ_AP014940.1|WP_096377146.1|1585156_1586362_+|pyridoxal-phosphate-dependent-aminotransferase
MPQLARRIGRAKPSAIMQVAEKAKRLKAEGRDIISFSIGVPNFLPGDHVYAAVREALAKDSGQYGSNRGADALLDAFIEHMGKIGLTGYGRVNVATGIGAKHVIYNIAEALLDEGDTIAFPTPYWTSYLDIAEIVNAKIDLLPCPASQDYKLTPAQLDAALAKKPKVFLFNNPSNPTGMVYSKDEIDALAAVVAKYPDTWIITDDIYNRMVFDGLGYHNFVHARPELRDRVIFIDSLSKTYGMPGWRVGFMAGPEVIAQAVTTMNSNHITNVPEIVTAAAVAALSGPQDVPTAKCAEFQAKRDRVMAVMNAIPGVICPRPQGAFYVFPDISVAFGKTHQPSGIKIGNDMDFCSALLETKGVACVPGSAFGEPNALRISYTCPTPQLAPGLQRFQEFFAELV

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Crispr_ID: NZ_AP014940_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_6

2736854-2736998

Orphan

Consensus_repeat	Method
CCCTGTAGGAGCTGCGCAAGCTGCGACCGCGAATCCTCAGCTACG	CRISPRCasFinder

1 spacers

csa3

The CRISPR arrays of NZ_AP014940_6

>merge|NZ_AP014940|6|2736854-2736998|CRISPRCasFinder
CCCTGTAGGAGCTGCGCAAGCTGCGACCGCGAATCCTCAGCTACGGCGTAGCTGTCGTCGTAGTTGCATTTGCGGCCACCGCTTCGTAGCTGCGATAGCCCCCTGTAGGAGCTGCGCAAGCTGCGACCGCGAATCCTCAGCTACG

>NZ_AP014940|6|6|2736854-2736998|CRISPRCasFinder
CCCTGTAGGAGCTGCGCAAGCTGCGACCGCGAATCCTCAGCTACG	GCGTAGCTGTCGTCGTAGTTGCATTTGCGGCCACCGCTTCGTAGCTGCGATAGCC
CCCTGTAGGAGCTGCGCAAGCTGCGACCGCGAATCCTCAGCTACG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_074870322.1\|2728340_2729282_-\|ABC-transporter-permease	unknown	unknown	unknown
NZ_AP014940.1\|WP_096377932.1\|2735710_2735986_+\|SlyX-family-protein	unknown	unknown	gnl\|CDD\|179141
NZ_AP014940.1\|WP_096377928.1\|2731335_2731935_+\|glutathione-peroxidase	unknown	unknown	gnl\|CDD\|223463
NZ_AP014940.1\|WP_096377926.1\|2729362_2730247_-\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224054
NZ_AP014940.1\|WP_096377957.1\|2747172_2748291_-\|homocysteine-S-methyltransferase-family-protein	unknown	unknown	gnl\|CDD\|236539
NZ_AP014940.1\|WP_096377941.1\|2738167_2738947_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|223377
NZ_AP014940.1\|WP_096377938.1\|2737079_2737940_-\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|223669
NZ_AP014940.1\|WP_096377951.1\|2741808_2743290_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|235906
NZ_AP014940.1\|WP_096377927.1\|2730636_2731155_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_172437217.1\|2733248_2734073_+\|FKBP-type-peptidyl-prolyl-cis-trans-isomerase	unknown	unknown	gnl\|CDD\|223619
NZ_AP014940.1\|WP_096377949.1\|2740758_2741589_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379079
NZ_AP014940.1\|WP_172437218.1\|2739848_2740658_+\|right-handed-parallel-beta-helix-repeat-containing-protein	unknown	unknown	gnl\|CDD\|379079
NZ_AP014940.1\|WP_074870006.1\|2743488_2744211_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096377944.1\|2739084_2739633_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|366102
NZ_AP014940.1\|WP_074870017.1\|2748301_2749270_-\|metalloregulator-ArsR/SmtB-family-transcription-factor	csa3	COG0640_csa3_CAS-I-A	gnl\|CDD\|369777
NZ_AP014940.1\|WP_096377931.1\|2734374_2735718_+\|UDP-glucose/GDP-mannose-dehydrogenase-family-protein	unknown	unknown	gnl\|CDD\|223936
NZ_AP014940.1\|WP_074869953.1\|2730243_2730633_-\|GntR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224639
NZ_AP014940.1\|WP_096377935.1\|2735996_2736740_+\|DUF2058-family-protein	unknown	unknown	gnl\|CDD\|225664
NZ_AP014940.1\|WP_096377954.1\|2744269_2747029_-\|methionine-synthase	unknown	unknown	gnl\|CDD\|236539
NZ_AP014940.1\|WP_096377929.1\|2732177_2733122_+\|FKBP-type-peptidyl-prolyl-cis-trans-isomerase	unknown	unknown	gnl\|CDD\|223619

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_096377941.1\|2738167_2738947_-\|SDR-family-oxidoreductase	gnl\|CDD\|223377	COG0300, DltE, Short-chain dehydrogenases of various substrate specificities [General function prediction only].	6.74002e-86
NZ_AP014940.1\|WP_096377932.1\|2735710_2735986_+\|SlyX-family-protein	gnl\|CDD\|179141	PRK00846, PRK00846, hypothetical protein; Provisional.	7.06454e-17
NZ_AP014940.1\|WP_096377928.1\|2731335_2731935_+\|glutathione-peroxidase	gnl\|CDD\|223463	COG0386, BtuE, Glutathione peroxidase [Posttranslational modification, protein turnover, chaperones].	2.10061e-76
NZ_AP014940.1\|WP_096377926.1\|2729362_2730247_-\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224054	COG1131, CcmA, ABC-type multidrug transport system, ATPase component [Defense mechanisms].	7.67767e-60
NZ_AP014940.1\|WP_096377957.1\|2747172_2748291_-\|homocysteine-S-methyltransferase-family-protein	gnl\|CDD\|236539	PRK09490, metH, B12-dependent methionine synthase; Provisional.	0
NZ_AP014940.1\|WP_096377938.1\|2737079_2737940_-\|alpha/beta-hydrolase	gnl\|CDD\|223669	COG0596, MhpC, Predicted hydrolases or acyltransferases (alpha/beta hydrolase superfamily) [General function prediction only].	1.26212e-07
NZ_AP014940.1\|WP_096377951.1\|2741808_2743290_-\|hypothetical-protein	gnl\|CDD\|235906	PRK07003, PRK07003, DNA polymerase III subunit gamma/tau.	8.14925e-09
NZ_AP014940.1\|WP_172437217.1\|2733248_2734073_+\|FKBP-type-peptidyl-prolyl-cis-trans-isomerase	gnl\|CDD\|223619	COG0545, FkpA, FKBP-type peptidyl-prolyl cis-trans isomerases 1 [Posttranslational modification, protein turnover, chaperones].	5.37649e-70
NZ_AP014940.1\|WP_096377949.1\|2740758_2741589_+\|hypothetical-protein	gnl\|CDD\|379079	pfam13229, Beta_helix, Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases.	0.000345671
NZ_AP014940.1\|WP_172437218.1\|2739848_2740658_+\|right-handed-parallel-beta-helix-repeat-containing-protein	gnl\|CDD\|379079	pfam13229, Beta_helix, Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases.	2.81293e-06
NZ_AP014940.1\|WP_096377954.1\|2744269_2747029_-\|methionine-synthase	gnl\|CDD\|236539	PRK09490, metH, B12-dependent methionine synthase; Provisional.	0
NZ_AP014940.1\|WP_096377944.1\|2739084_2739633_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|366102	pfam00440, TetR_N, Bacterial regulatory proteins, tetR family.	1.2469e-10
NZ_AP014940.1\|WP_074870017.1\|2748301_2749270_-\|metalloregulator-ArsR/SmtB-family-transcription-factor	gnl\|CDD\|369777	pfam08241, Methyltransf_11, Methyltransferase domain. Members of this family are SAM dependent methyltransferases.	5.99222e-25
NZ_AP014940.1\|WP_096377931.1\|2734374_2735718_+\|UDP-glucose/GDP-mannose-dehydrogenase-family-protein	gnl\|CDD\|223936	COG1004, Ugd, Predicted UDP-glucose 6-dehydrogenase [Cell envelope biogenesis, outer membrane].	0
NZ_AP014940.1\|WP_074869953.1\|2730243_2730633_-\|GntR-family-transcriptional-regulator	gnl\|CDD\|224639	COG1725, COG1725, Predicted transcriptional regulators [Transcription].	1.86258e-30
NZ_AP014940.1\|WP_096377935.1\|2735996_2736740_+\|DUF2058-family-protein	gnl\|CDD\|225664	COG3122, COG3122, Uncharacterized protein conserved in bacteria [Function unknown].	1.94452e-43
NZ_AP014940.1\|WP_096377929.1\|2732177_2733122_+\|FKBP-type-peptidyl-prolyl-cis-trans-isomerase	gnl\|CDD\|223619	COG0545, FkpA, FKBP-type peptidyl-prolyl cis-trans isomerases 1 [Posttranslational modification, protein turnover, chaperones].	1.67778e-65

>NZ_AP014940.1|WP_096377935.1|2735996_2736740_+|DUF2058-family-protein
MSDSLRDQLLGLGFKPAPKPERPERKGEDRRGGKPGGRSDGKPEGRPHARADGPARGDARPGAGKPGAGAKPGAPGARPGQGRPGGGKPGERGRGRPGAGGRAPTREDIDLAKAYAIRAQREKDERIAAEKAKQEEARLRREARAKLAELLKDQALNVADADIARHFPYGGKIKRVYVTAEQLKQLNAGELGVLQQEGRYLLVSAAMLAQAEAIFAPAVALKVDPNAPAQDDPYADPMYQVPDDLVW
>NZ_AP014940.1|WP_096377932.1|2735710_2735986_+|SlyX-family-protein
MPEPTPVSSDLGQSVERSAVEQRLVDLETRVAFQEHALTELSDALAAARSEESRNALLLLRALDEIKHLRAAMAASPLTGDAGNEPPPPHY
>NZ_AP014940.1|WP_096377931.1|2734374_2735718_+|UDP-glucose/GDP-mannose-dehydrogenase-family-protein
MRVTIFGTGYVGLVTGTCLADVGHDVVCVDIDQAKVEGLNRGVIPIYEPGLESMVKANHASGRLHFTTDAAGAIAHGDLIFIAVGTPPDEDGSADLKYVLAVAQTIGRHIERPVIVVNKSTVPVGTADKVQATIAAELAARGAQVAFDIASNPEFLKEGDAVNDCMRPDRIVIGAANPLAVEKLKRLYAPFNRNHERIVVMDVRSAELTKYAANAMLATKISFMNEIANIAEKVGADIEMVRQGIGSDPRIGWHFIYPGAGYGGSCFPKDVQALARTAQQNGYEARLLDAVESVNDSQKGHLFELIQRHYGGDVRGKTFAVWGLAFKPNTDDMREASSRRLLAQLWEAGAKVRAYDPEASEEAQRIFGERDDLVLCDSARAALADADALVVVTEWKQFRSPDFVRVRQALADAVIFDGRNLYHPDEVEAADLAYYGIGRGRSIHIDA
>NZ_AP014940.1|WP_172437217.1|2733248_2734073_+|FKBP-type-peptidyl-prolyl-cis-trans-isomerase
MRNTALAIAVGSMALFAAGCDQAGKPAGDKAAAESKSGDKAGEAKKDVKVLGGMKTEKEQNSYLIGMDMGRSLELLKDDIDLAVLQKAMQASMKGEKTALTDEEAMQIRQRLQETVRAKQVEKMVAMAKKNQEDGEKFLAANGKKAGVVTTASGLQYQIVTEGKGAKPKASDTVRVHYKGTLLDGKEFDSSYARNEPAVFPLGAVVPGWQEGIALMPVGSKFKLWIPAKLGYGEQGTPGGPIGPNATLVFDVELLDIVKADGPESAAMGTTPKH
>NZ_AP014940.1|WP_096377929.1|2732177_2733122_+|FKBP-type-peptidyl-prolyl-cis-trans-isomerase
MKPFVRGAAVLMTTAALFAGAASAQDKSVLANEREKISYAIGMDVASSLKPVGPDLDAAAFEKAVKNVFDGGKPLITQDEARTVDAALRARIASREGKPAQGTPPGTPPPAVDKSKVGLMIGSYMVGPALQQIKSEIELPVLVQAVRTSLGGGQTLLNEGDARTVLTNFSERMQAKTKAEAAAAGEKNLKEGKAFLEENKKVKGVFATGSGLQYMILRQGSGERPKPTDKVSVNYKGTLLSGKTFDSSYDRGQPAEFPVNGVIQGWQEGLAMMPVGSKFKFWIPSELAYGPNGAPPSIGPNAVLTFEVELLDIL
>NZ_AP014940.1|WP_096377928.1|2731335_2731935_+|glutathione-peroxidase
MPATASPQPRRAARAALALGLILAVGAAAAAGGLLDRSFRPLAGKQPVDLAKTYAGDVVLVVNTASKCGFTPQFEALEGLHAKYKARGFAVLGFPSGDFKAQEFEDEKQIQEFCTLTYGVKFPMFEKVHVVGEQATPLYKDLAKAAGEAPKWNFHKYLIGRDGKLIASYGSKTTPDDPAVVAAIERALAAPAPKPVAAR
>NZ_AP014940.1|WP_096377927.1|2730636_2731155_-|hypothetical-protein
MNRKLHNSISALMAAGGALVLGLVVALPLPAPDSPPAPALTQFAADAPATRPIEVDLGAVKARISFDRDFLERARSRSGDVAGAVRKIEQRAQQLENTERAAELTTIAGALAGDVADLAALANAVAPASFSPSSNAAAESAGAAEPKRKAGSAARRSRSNLVMPYFSFLSRG
>NZ_AP014940.1|WP_074869953.1|2730243_2730633_-|GntR-family-transcriptional-regulator
MTAIQWSDGAPIYRQLKERVVAMMLDGVLKPGDALPSVRQVAAEYQLNPITVSRAYQELADEALVEKRRGLGMYVTEEAAKKLLLNERDRFLREEWPLVLERIARLGLRAEELLGGDAAGEGTHKADAP
>NZ_AP014940.1|WP_096377926.1|2729362_2730247_-|ABC-transporter-ATP-binding-protein
MTNATHIDPGQVVRARGLRKIYRNKAALDGADFDIPAGRIVGLIGPNGAGKTTALKAVLGLTQFDGELSVLGLDPRSQRDALMREVCFIADVAVLPRWLRVREAIEFVAGVHPRFDRAKCERFLHGTQLKPDLRVREMSKGMIVQLHLALVMAIDARLLVLDEPTLGLDILYRKQFYQRLLEDYFDENKTIVVTTHQVEEIEHILTDVMFIRDGKIVLDCPMENLGERFVEVLVDRDKAEHARTLGPLDERALPFGKTVMLFDGVAAAQLDGLGETRTPGLADLFVATMKGTYA
>NZ_AP014940.1|WP_074870322.1|2728340_2729282_-|ABC-transporter-permease
MLLKREFWEHRGGFLWGPLIAGAVAVIFTVLGVIGGSVLFNKYAVRDHDGINLEMTGDMARAGQIGDAALAGGLGIVCLVFVFVVFFYALGSLYDERKDRSILFWKSLPISDTQAVLSKLAWALLLAPLLAAAIGLAVGLVMWTLAWLAAVLNGFSGAGAIFTQAHPFRLLGELALSVPVYSLWALPTVGWLMLCSAWARAVPFVWAVVIPLLACVFVSFLDVMPGIEIPHRAIWYTVALRGLLSVVPGTWFLHDSFSEDAQQAAMKGTDALNQLDSASSLQVLATADLWIGAAIGAAMIFAAIHLRRWRDEG
>NZ_AP014940.1|WP_096377938.1|2737079_2737940_-|alpha/beta-hydrolase
MQDLLLFSHANGFPAPVYRLMLEALSARYRIVRPERIGHDPRYPVTLDWPHLIEELVQRTQAAAGDARRIFLVGHSLGGYLSLLASHRLAGTALAARVAGVVMLDSPLIAGWRARLVQLGRRTGLDNLVMPTRATLQRRRHWPDRDAVRAHFLAKPAFARWDARVLEDYVEHGTRAGADGARELSFEREIEYRIYRSLPTTSLSGLTAQLRTPVGFLAGTRSRELRNAGDAATRRLVGDRWAWIEGSHLFPMERPLDTAQAIEAMLERLAPAAAETLAEPLRPTGT
>NZ_AP014940.1|WP_096377941.1|2738167_2738947_-|SDR-family-oxidoreductase
MSTLPTVVITGASTGIGAVYADRFARRGHDLILVARDLARLQALAERLRADYGVAAEPLKADLADPAQLAGLERLLRDDARIGVLVNNAGATLPGGFLEQTPEQTAQLIALNVTAPTRLAAAIAPRLAAAGSGAIVNLASVVGLAPEFGMSVYGATKAFVQYLSQSLQGEIGGKGVYVQAVLPAATRTEIWERSGRDVAQIPGVMEVDALVDAALAGFDRREAVTIPPLHDESLWQAADAARKAMLPHYSQSQPAPRYL
>NZ_AP014940.1|WP_096377944.1|2739084_2739633_+|helix-turn-helix-transcriptional-regulator
MKVSREQVGENRRRILDQAGRLFRERGFDAVSVAQVMKAAGLTHGAFYGHFQSKDELIAQTLAHVFAGSEVAAEPEAFLAGYLSSQHCADAAGGCPVAGLGAETLRQSPQARAAMTAGLREQLQRMSETAPGADAAARRREAIGRWSAMVGALTLARLSDDAALAEEILEQARSWIGERDAQ
>NZ_AP014940.1|WP_172437218.1|2739848_2740658_+|right-handed-parallel-beta-helix-repeat-containing-protein
MRIFMRTGLALAGLIGAGSALACDTVLDSQQRFIDQPGKYCLSADRDEPIAILADNVELDCRGRTLTWTPGNGNDGVGVHLRRGDKAIVRNCRLQGWSYGILVSERGNAQVLNNTVVDGGVGIAVQGSERPEDENARLIGNRIFYYGQGQGADSAIAVQHAAKPVLTNNLVAGFRGWSAILLDRAPDAQLTGNQLLDLNEGGSAAVRMEQSPRARLVHNTAMLRRGIDGRGLVGAVDATCIENVFINTVAPGFQQCSVRRYNVEQINND
>NZ_AP014940.1|WP_096377949.1|2740758_2741589_+|hypothetical-protein
MRHLANTGLALVGLLLSANALACDTILPPTQVGVHLPGKYCLSANRSLPIEIDGADIELDCRSRSLASAQPGNSDTGIRVRGGDKVVVRNCRIEGFAVGIFLEARSGAQLLNNTVLRAQFTPIVARGEYFQGGPIDPQIEPVRIVGNRVIGYGQGGTTNPGAALIVQGLPRAAISNNVVAGFSGPTGLELVESPDAQLTGNQFLDFSRGDRLLRLRNSPRARIVHNTIMSRQPTVFEGLSGATDATCVENVFINTVRSGFADCAVARYNVEQQSQM
>NZ_AP014940.1|WP_096377951.1|2741808_2743290_-|hypothetical-protein
MPFQLYRTDNRPPDTIANDGFQARAPMSADTARAFVQRSLVDPNTDLNLPTAAQGGVMAGYLRTHSNLVGLSSLYQEIRRETSASTLHVSTSPSDGTGGIRSAHLYQIDMPASRLYAWQERGSGLSARPTEVTSFADAHPSNNAYGIPATRPVLLTDTNDLRTATMFAISSPSGDGEVAFLTGIPSQWINNSRTLPGGAWQAMPAQAQGQGAPATTAPTPIAPTSIASSSTAPGASAPLPPVSGSSFPPASSSSTAPSPAVPPQQASHQASSSHAPNVQGTPSAASSSSPEVEGRRPPPVPPRPLSMQTHPYQDAGHANHNLYEQARDGLQRLKPLLPANERTLAAAALADAAQAATPPLRSIDHVTEGRDGRLFAVNGGLHSPTARLAYADPAQVQAQAQVAADHTAGRGAPAQGAANPAAPPQATPGQVATPQLAQPQAPLQAQQPPAQQQQQQQQAQQPAQQEGRVRALTAMFETQNQDQGQNQGGPRQR
>NZ_AP014940.1|WP_074870006.1|2743488_2744211_-|hypothetical-protein
MSEILLPEDLADAESSDPRGNQAFLEKHAAPGRIGLCGGRDFINKLIRKAQSPLTEDGHRSLWSHAFVFSERRVDGQWWVIESDLDLRYRQIRLGVQENRVARYYDAEAFPNIAVLDFGLSPEQVLQVQKAGLDLLAGLSSYSISELLGTMMAMHSRRLRKRGNLLAKDGALFCSALVQHCYLAAGVEFLPGVPGKNIAPHDIDESPLPHATHRILRDLGVSTVREIGHSLRERLASSLD
>NZ_AP014940.1|WP_096377954.1|2744269_2747029_-|methionine-synthase
MTSALPRQTRLSGLEPLQITPESNFVNVGERTNVTGSAQFKKLILEGRLDEAVVVARQQVENGAQVIDVNMDEGLLDSQQAMVEFLNLIAAEPDIARVPVMVDSSKWNVIEAGLKCLQGKGIVNSISMKEGEDEFLRQARLVRRYGAAVVVMAFDEVGQADTIERKVDICSRAYKLLTEQVGFPPEDIIFDPNVFAVATGIEEHNDYAVAFIEATREIKRRFPYSHISGGVSNVSFSFRGNEPVRQAIHVVFLYHAIKAGMDMGIVNAGALPLYDDLETDLRERVEDVVLNRRSDATERLLEIADRFKGKKGEKKVEDLRWRDKPVRERLSHALVHGIDQWIEEDTEVARAQSTRPLDVIEGPLMSGMNVVGDLFGAGKMFLPQVVKSARVMKKAVAYLLPYIEAEKLRTGDVGKSNGKIVMATVKGDVHDIGKNIVGVVLACNNFDVVDLGVMVPAQTILDRARAENADLIGLSGLITPSLEEMSHVAREMQRQGFTMPLLIGGATTSRAHTALKIDPHYDAPTIWVKDASRAVGVAQSLISIELREPFVAANASDYAEIRQRHRQRGDGKRLVSLEKARGQRYAGHWDEYVPPTPKTPGVYAFDDYPLDELVEYIDWTPFFNTWELAGRYPAILTDEIVGKQATELYRDARAMLKKIVAEKWIGAKAVFGLWPANAVGDDVDVDPSIALDAVVLPDNGLVQPQRVAGGLRETTRLHFLRQQVDKPADRPDFCLADFIAPKDSGRQDWIGAFAVTAGLGIEPHVARFEADHDDYNAIMLKALADRFAEALAERLHQRVRKEFWGYAGDETLDNDALIDEGYRGVRPAPGYPACPEHSEKRTLFALLDAPAHSGLELTESFAMYPAAAVSGYYFSHPDSQYFVVGRVSKEQVEDYARRKGVSLVQAERWLASNLDYDPE
>NZ_AP014940.1|WP_096377957.1|2747172_2748291_-|homocysteine-S-methyltransferase-family-protein
MKPLPWLHPERAQALLRGLSERILIIDGAMGTMIQQHSLTEADYRGERFAEGFDRLYSPPAREHDGEHVHGEGCGCSRDQRGNNDLLTLTRPEIIAGIHREYLQAGADLVETNTFNSTTISLEDYGLEHLARELNFEGAKLARGVCDEIEALDPSRPRYVIGVLGPTSRTASLSPDVNRPGYRAISFDQLRAAYREAADGLIDGGADVLMVETIFDTLNAKAALFAVEEAFDARGARLPVMISGTITDASGRTLSGQTAEAFWYSVRHVQPTAIGLNCALGAKDLRVHVDVLAQIADSHVSTHPNAGLPNAFGGYDETPEDMAAVLGEFARAGLLNLVGGCCGTSPAHIAAIAAAVQGVPPRQPLQLIDAAA
>NZ_AP014940.1|WP_074870017.1|2748301_2749270_-|metalloregulator-ArsR/SmtB-family-transcription-factor
MDLEGWSSRLKVFADATRVRLLALLEGEELTVAELSAITRLAQPRVSTHLSKLKEAGLVRDRRAGVSAYYRFDDGALDQAQRALWQTLSTGSDDPLLRQDAERVAAVLAMRASDQNWADSVAGDMERHYSPGRTWEALARSALPLLQPGDVLDIASGDGVLAELLAPHSHRYICLDASTKVVAAASERLRKLRNVEVREGDMHALPFPAETFDLVVLMHALTYAEQPAQAVAEAARVLRPGGRLLLTSLARHEHRGAVEAFGHVNLGFSEKDLQKFAAKAGFDIVSCETVTRERRPPHFEVIALMARKPQPEPAAARKPAKK

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Crispr_ID: NZ_AP014940_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_7

3309694-3309767

Orphan

Consensus_repeat	Method
ACCAGGCCGAGCGGACCGTTCCA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP014940_7

>merge|NZ_AP014940|7|3309694-3309767|CRISPRCasFinder
ACCAGGCCGAGCGGACCGTTCCAGCGGCCGGAGCCGTCGTTGTTGATCGTCACCAGGCCGAGCGGCCCGTTCCA

>NZ_AP014940|7|7|3309694-3309767|CRISPRCasFinder
ACCAGGCCGAGCGGACCGTTCCA	GCGGCCGGAGCCGTCGTTGTTGATCGTC
ACCAGGCCGAGCGGCCCGTTCCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_096378671.1\|3317069_3317513_-\|DUF4287-domain-containing-protein	unknown	unknown	gnl\|CDD\|379478
NZ_AP014940.1\|WP_096378667.1\|3312410_3312833_+\|Rrf2-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|236820
NZ_AP014940.1\|WP_096378662.1\|3305917_3308101_-\|glycoside-hydrolase-family-3-C-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|185053
NZ_AP014940.1\|WP_096378655.1\|3292429_3294985_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|227112
NZ_AP014940.1\|WP_096378657.1\|3296306_3296990_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|197666
NZ_AP014940.1\|WP_172437375.1\|3303387_3305517_-\|TonB-dependent-siderophore-receptor	unknown	unknown	gnl\|CDD\|227114
NZ_AP014940.1\|WP_172437249.1\|3317649_3318447_-\|DUF4198-domain-containing-protein	unknown	unknown	gnl\|CDD\|378467
NZ_AP014940.1\|WP_096378656.1\|3294990_3296292_+\|cytochrome-c-peroxidase	unknown	unknown	gnl\|CDD\|224771
NZ_AP014940.1\|WP_096378658.1\|3296980_3297886_-\|sterol-desaturase-family-protein	unknown	unknown	gnl\|CDD\|225546
NZ_AP014940.1\|WP_096378668.1\|3313009_3314209_-\|cellulase-family-glycosylhydrolase	unknown	unknown	gnl\|CDD\|365907
NZ_AP014940.1\|WP_096378669.1\|3315489_3316413_+\|glycerophosphodiester-phosphodiesterase	unknown	unknown	gnl\|CDD\|176522
NZ_AP014940.1\|WP_096378659.1\|3298262_3299957_+\|malate-dehydrogenase-(quinone)	unknown	unknown	gnl\|CDD\|179979
NZ_AP014940.1\|WP_172437248.1\|3300489_3302295_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224055
NZ_AP014940.1\|WP_145960074.1\|3308753_3309143_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096378670.1\|3316470_3317025_+\|DUF308-domain-containing-protein	unknown	unknown	gnl\|CDD\|225786
NZ_AP014940.1\|WP_074868562.1\|3314425_3315196_+\|DNA/RNA-non-specific-endonuclease	unknown	unknown	gnl\|CDD\|366523
NZ_AP014940.1\|WP_096378666.1\|3311915_3312284_-\|group-III-truncated-hemoglobin	unknown	unknown	gnl\|CDD\|381257
NZ_AP014940.1\|WP_096378661.1\|3302420_3303350_+\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293825
NZ_AP014940.1\|WP_096378665.1\|3310644_3311871_-\|NO-inducible-flavohemoprotein	unknown	unknown	gnl\|CDD\|237337
NZ_AP014940.1\|WP_172437250.1\|3318497_3318992_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_096378671.1\|3317069_3317513_-\|DUF4287-domain-containing-protein	gnl\|CDD\|379478	pfam14117, DUF4287, Domain of unknown function (DUF4287). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 70 and 180 amino acids in length.	4.26277e-21
NZ_AP014940.1\|WP_096378667.1\|3312410_3312833_+\|Rrf2-family-transcriptional-regulator	gnl\|CDD\|236820	PRK11014, PRK11014, HTH-type transcriptional repressor NsrR.	1.69876e-46
NZ_AP014940.1\|WP_096378662.1\|3305917_3308101_-\|glycoside-hydrolase-family-3-C-terminal-domain-containing-protein	gnl\|CDD\|185053	PRK15098, PRK15098, beta-glucosidase BglX.	0
NZ_AP014940.1\|WP_096378661.1\|3302420_3303350_+\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293825	cd07739, metallo-hydrolase-like_MBL-fold, uncharacterized subgroup of the MBL-fold_metallo-hydrolase superfamily; MBL-fold metallo hydrolase domain. Members of the MBL-fold metallohydrolase superfamily are mainly hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.	1.773e-105
NZ_AP014940.1\|WP_096378657.1\|3296306_3296990_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|197666	smart00342, HTH_ARAC, helix_turn_helix, arabinose operon control protein.	4.52988e-12
NZ_AP014940.1\|WP_172437249.1\|3317649_3318447_-\|DUF4198-domain-containing-protein	gnl\|CDD\|378467	pfam10670, DUF4198, Domain of unknown function (DUF4198). This family was previously missannotated in Pfam as NikM.	4.03156e-28
NZ_AP014940.1\|WP_096378656.1\|3294990_3296292_+\|cytochrome-c-peroxidase	gnl\|CDD\|224771	COG1858, MauG, Cytochrome c peroxidase [Inorganic ion transport and metabolism].	2.07362e-72
NZ_AP014940.1\|WP_096378658.1\|3296980_3297886_-\|sterol-desaturase-family-protein	gnl\|CDD\|225546	COG3000, ERG3, Sterol desaturase [Lipid metabolism].	8.70722e-38
NZ_AP014940.1\|WP_096378668.1\|3313009_3314209_-\|cellulase-family-glycosylhydrolase	gnl\|CDD\|365907	pfam00150, Cellulase, Cellulase (glycosyl hydrolase family 5).	3.17954e-11
NZ_AP014940.1\|WP_096378669.1\|3315489_3316413_+\|glycerophosphodiester-phosphodiesterase	gnl\|CDD\|176522	cd08580, GDPD_Rv2277c_like, Glycerophosphodiester phosphodiesterase domain of uncharacterized bacterial protein Rv2277c and similar proteins. This subfamily corresponds to the glycerophosphodiester phosphodiesterase domain (GDPD) present in uncharacterized bacterial protein Rv2277c and similar proteins. Members in this subfamily are bacterial homologous of mammalian GDE4, a transmembrane protein whose cellular function has not yet been elucidated.	1.21938e-113
NZ_AP014940.1\|WP_096378659.1\|3298262_3299957_+\|malate-dehydrogenase-(quinone)	gnl\|CDD\|179979	PRK05257, PRK05257, malate:quinone oxidoreductase; Validated.	0
NZ_AP014940.1\|WP_172437248.1\|3300489_3302295_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224055	COG1132, MdlB, ABC-type multidrug transport system, ATPase and permease components [Defense mechanisms].	1.97976e-158
NZ_AP014940.1\|WP_096378655.1\|3292429_3294985_+\|TonB-dependent-receptor	gnl\|CDD\|227112	COG4771, FepA, Outer membrane receptor for ferrienterochelin and colicins [Inorganic ion transport and metabolism].	9.45235e-09
NZ_AP014940.1\|WP_096378670.1\|3316470_3317025_+\|DUF308-domain-containing-protein	gnl\|CDD\|225786	COG3247, HdeD, Uncharacterized conserved protein [Function unknown].	4.86227e-12
NZ_AP014940.1\|WP_074868562.1\|3314425_3315196_+\|DNA/RNA-non-specific-endonuclease	gnl\|CDD\|366523	pfam01223, Endonuclease_NS, DNA/RNA non-specific endonuclease.	7.45197e-38
NZ_AP014940.1\|WP_096378666.1\|3311915_3312284_-\|group-III-truncated-hemoglobin	gnl\|CDD\|381257	cd08916, TrHb3_P, Truncated hemoglobins (TrHbs, 2/2Hb, 2/2 globins); group 3 (P). The M- and S families exhibit the canonical secondary structure of hemoglobins, a 3-over-3 alpha-helical sandwich structure (3/3 Mb-fold), built by eight alpha-helical segments. Truncated hemoglobins (TrHbs, 2/2Hb, or 2/2 globins) or the T family globins adopt a 2-on-2 alpha-helical sandwich structure, resulting from extensive and complex modifications of the canonical 3-on-3 alpha-helical sandwich that are distributed throughout the whole protein molecule. They are classified into three main groups based on their structural properties and named after Mycobacterium sp. genes glbN, glbO, and glbP: TrHb1s (N), TrHb2s (O) and TrHb3s (P). TrHb3s include Campylobacter jejuni Ctb, encoded by Cj0465c, which may play a role in moderating O2 flux within C. jejuni.	1.58307e-39
NZ_AP014940.1\|WP_172437375.1\|3303387_3305517_-\|TonB-dependent-siderophore-receptor	gnl\|CDD\|227114	COG4773, FhuE, Outer membrane receptor for ferric coprogen and ferric-rhodotorulic acid [Inorganic ion transport and metabolism].	0
NZ_AP014940.1\|WP_096378665.1\|3310644_3311871_-\|NO-inducible-flavohemoprotein	gnl\|CDD\|237337	PRK13289, PRK13289, NO-inducible flavohemoprotein.	0

>NZ_AP014940.1|WP_145960074.1|3308753_3309143_-|hypothetical-protein
MRAASATILGLGLTLPMSGLANDFSLGLDVDRVPTAQLSLPACNAAIARGAAALGYATRVNRDQKTLITHVSGPPQDGRALIAYCIAAGTYTAWVVQAFDYSGPNLTEPQRIATRVSGEIRKAIKPAAK
>NZ_AP014940.1|WP_096378662.1|3305917_3308101_-|glycoside-hydrolase-family-3-C-terminal-domain-containing-protein
MTGRVDIEALIDRMTLEEKIGQLSILADSIRPFAFDVNPDSFQWGPDRTREMIRAGQVGALFNGVGAKEGRELQRIAVEQSRLGIPILLGADVIHGMRTVFPIPLGEAASFEPELAERTARAAAVEATREGLHWTFAPVVDIARDQRWGRVAETTGEDTVLACAFARARVRGFQGPDLTADDSLLATPKHFAAYGAVSAGLDYNTVDLSPQTLFDVHLPPFKAAIEAGALTVMSSFNDINGVPATANRELLTGVLREQWGFEGFVVSDYTSDFELIAHGYAADEKHAAELSIGAGLDMSMQSGVFMDHLAALVGEGKVSVQAIDTAVRRILTVKARMGLFDNPYRSLNEAPPGPAPYLAAHDELAREAARRSVVMLKNDGDVLPLRKSGQRIALIGPFARDRANLAGCWNIFGDPSREVDLETGLRAALADGDALEVVEGCDFESAIDGGIDAAVAAARGADAVLLALGEPSVFSGEAQSRTQIVLPAAQLALAEAVLAAGTPVIVLLRCGRALALGPLQRADAVLVTWFLGSQTGHAVADLVFGEHSPGGRLPVSFPHDSGQQPYYYNHPATGRPYVPGGLEAFRTRWRETDHTALYPFGHGLTYGRIEYGAATLDAPALAWDGELRARVRITNVGERAAEEVVQLYVRDRVASRVRPVRELKRFAKIALAPGESREVEFALSRADLEFRGVDNRAVAEPGLFDLWLAPSATAGEAVQFELLAAQG
>NZ_AP014940.1|WP_172437375.1|3303387_3305517_-|TonB-dependent-siderophore-receptor
MAGVLAWSAPILAVAQTAAPARDSAAAAADPTELDRVEVVANQLGTVTEGSGSYTPGSIATATRLVLTPRQTPQSISVIGRQEMDDFGLTGIDDVMRVTPGISIVTYDSERTEYYARGFAIQNFQYDGIPMQRDSAFSAGNTLSDTAIYDRIEVLKGATGLLTGIGDPGATINLIRKKPTREFKGQATLGAGSWDEYRGEVDVSGPLSEDGRVRGRAVAVRQDRHGYSERYQRSTEVFYGIVEADLTPDTLLTLGADSQDSDPRGSSWGGIPLLDADGQFYRVPRSFNNGADWSRWRQYTRTGFATLEHRFGDGWVAKLQLNHQVNGYDAALGAAAAGHPDPRDGSGVSLWLGQYVGKTLANAADAYVSGHFQWFGRKHELVFGASASRKRWTNVGYFAPPDYPTDVPDYRQWNGAIPEPAWQRGFDNDQTTRESGVYLVGRFDLADPFKLILGSRIANYKTDGIDESGVVVPYAGAVYDLNTYLSVYASYSTIFKPQVEQDERGRALDPREGENYELGLKGEFFEGRLNASAAAFRLNQDNYPVPSGGKTPTGGDAYRALQGVRTEGYELELSGQLRPGWQIQGGYAHKVARQRGAKVSTLEPEDQFSAHTSYRFDGALDGLTVGGGARWQSSSFGPVGAPGGGTVEHRTQPYWLLDAMLAYRFDEHFSAAFNLDNLLDKRYYTIFDVYSTYTWGEPRSVRASVTYRF
>NZ_AP014940.1|WP_096378661.1|3302420_3303350_+|MBL-fold-metallo-hydrolase
MSATPALRLSLAFGLVAAFAAFAAQSAPAKAAAPLRIEVYNPGENGVFPVSSELVVGEREVLLIDAQFQRSDAQALVEKIRATGKTLRTVYISQSDPDYYFGLDTIRAAFPDARILATPQTVAAIRESMQGKLAYWGPILKDNAPRQLIVPEALQGDTLSLEGRTLKIQGLRGPDPARTYLWIPSLKTVAGGVVVSSGGHVFMADTQTPASRQGWLKTLRGIQALKPARVIPGHYLGPEPKGLDAVKFTAAYIARFEREAARAADSAQLIAAMQAAYPKLGEASSLELSAKVIKGEMPWPAPAPDAVKP
>NZ_AP014940.1|WP_172437248.1|3300489_3302295_+|ABC-transporter-ATP-binding-protein
MSRTHPSDEPANKPASSSRDLWRLIRTGRPSPVALSIAALAAIASVAGTLWFPVQTKQMIDGFGHGQIDVWAMVGLVAILAAAALLNAASAYLLARVGYQLVARLRQSLIDKLLRLPVSSFDRESSGERVSRVVRDCESISELIARQAVNLLTGVLLLAGSIVVLLLLDVRLTLALIGSIGAAFAIMIPIAFLLDGLSRRIQDRTARFSGILTHIFQEIRLVKAFTAEPRERERSRGEIDGLMRLGLRVARVNVLLEPLMSLAMTLAIIVILVYGAARVAAGEITVGTLTAFILYIFNVATPLMQLTHFTAELQKAKGASARIAAILLEDEEQTRPGTAERLPGQVLEFHDVSFAYDGRDAAVLRGIDLRFEPGRTVALVGTSGSGKTTLLSLIERFYEPSGGRILYGGRPIGEFDLRQWRGSIGYVAQSAPVMPGSVRDNIAYGLDGEFDDEQLRSAARRAGALEFIEKMPQGFDTQLIEQGNNLSGGQRQRIAIARMFLRDPDILILDEATSALDSETEHQVKLALDELMRGRTNIIVAHRLSTVMHADRICFLDAGRISGMGSHVELLATHPHYARLVERQFRHPAESEPASELALAT
>NZ_AP014940.1|WP_096378659.1|3298262_3299957_+|malate-dehydrogenase-(quinone)
MKKFRKVLLLLIVVAAVGGVVFLYWPLYQRSVPAAQNDQPVDVVLVGAGIMSVTLATYLQELQPDWKLQIYERRDGVAEESSDGWNNAGTGHSGFAELNYTPQLADGSVETKRAVEIAEQFEISRQFWSHQVREGRLGTPSDFINPTPHMSFVWGEDNIDYLRKRREALVKNPLFYGMQFSDDAAQIKQWAPLLMEGRDPKQHVAATYMPLGTDVNFGVITRQLTQGLQRSPNFALNLGHEVTALRRNADKTWNVTVKDLKSGQESTVKSRFVFIGAGGAALKLLQLSGIPEADDYAGFPVGGQFLAFTAPAIADRHRVKAYGMAETGSPPMSVPHLDARKLDGKPVILFGPFALYSTKFLKHGSWFDLYSSVNHDNVGEMLSVGTENLDLVKYLMSQAQLNDNDRHAELLKYFPTAKRSDWTLVTAGQRVQVIKRDPVKGPVLQFGTEIVIDKDRSIAALLGASPGASTSPPIMLDLMAKAFPQQVAAGWGEKLRQIVPSYGRKLNDSPALTNEIRRMTSQTLQLPYLEVPVAGAQPAQTPQPAPTPAPAKDARNQSPELQAM
>NZ_AP014940.1|WP_096378658.1|3296980_3297886_-|sterol-desaturase-family-protein
MSAWFQRLYAPAFFFGFILAALYAVEGLGLRPHWALPPLLALSLAVSFASERALPYRREWNRGPGERGRDAIHFVVNEGLNLAGLALLPLAAAWRPWPALWPQSWPLALQLAVAIVLADLGLTLAHYASHRWPLLWRFHAVHHSVTRMYGFNGLMKHPLHQAIEAAAGVGPLIALGLPLEATCVLAFAIAIQLQLQHSNVDMRIGPLRHVFAWAPVHRLHHLRYGRAGDVNFALFFSVWDRLLGTAAQAPGYRVGSQDLGIGSHPDYPRDYAGQLLEPFRTRPAQAEPALPPALRAALAQD
>NZ_AP014940.1|WP_096378657.1|3296306_3296990_+|helix-turn-helix-domain-containing-protein
MPALPMPPWTGTLRIHEEFALAWAAPGDTAPHRHYCHQIVRAAHGVATATIDGELLREPVLAIASQREHRLQADERPCFLLFAEPSSFQLQALAEAITAAPAQADAIALAAARCRRPQTLDPRVAHCLQRIDGLLAEKIHAASLAAGVRLSLSQLERLCGAQLNLSVRRLVLWRRLRLAATEALRERSLTVAAHAAGFADSAHLSRAFRRFFGVRGSDLVRAMRLQS
>NZ_AP014940.1|WP_096378656.1|3294990_3296292_+|cytochrome-c-peroxidase
MRTPRRWANLAVAAASALAFAIVFAGLLWASATAAQSAPQREQEPEPTPDPVADPVAAPTDKPVAQAAASRVAASASAPVAVDLDECRRRLDAGGAQIDRDCLRRVYALPIGQWPRPLTDPGARWSELAPLPKQAPYPPDNPPSPAKTALGKRLFEDPRLSGSGQIACASCHDSELGWGDGRSVPFGHDRQRGRRNALPVAMSGFAAHLFWDGRASSLEAQVLHPLTDPREMAARPAAVLRRLRSQADYRRAYADAFGSPGIDLARTSQALASFQRSLVPRFNRFDRFLEGSRNALDDRQLWGLHLFRTRARCMNCHSGATLSDDGFHNLGLHFYGRALQDLGRYEVTGDRADAGKFKTPSLRNVAKTGPWMHNGRFATLRGVVNLYNAGMPRPRPTPQQIGDPLFPQPDPLLHPLDLHRTELEAITAFLETL
>NZ_AP014940.1|WP_096378655.1|3292429_3294985_+|TonB-dependent-receptor
MNRLTLAIGLALSAGSLRAAETPQAPVAAVAPAAAPDAAAPAPSIYTYDPLKVIGQRLFPYQEGMSLDRRYIDEQIRGNGDIGTLLRINPSVQFDDTATTSRNMGEIRPADISINGGLYYQNAFALDGASFNNDTAPGGSTLAASIIDVPSHSQGIALDASQIGTLTVYDSNVPASYGGFSGGVVEAESRRARDAFSGSVVARMQRSVWNETHIVAPAVQNFEQSSTESLQPRYDKYQLRASLEGRTRNGLGLSGTVSRLRSVIPLRGYTAGRNSPTDENEKEQVRENTSASLRADWSDGDGLEISASVNYAPTDERYFIVNAKNGYYDLKQGGPVASARVNYQRGDWTWRNTLSYSDLDSSRRSQTDYWKSWARSSEMDWGVTTLSAEGSWGNIDQRNRNLGYKLVLEREPLRLGRGEHRLQFGLEYRDRNAEYHRLNDHYSYLTPAATLTCTAANGGVDRDGCSLAPVDATGSGVIKGRGQYFTRRNLYREGAFSVDNREWAVFAQDDLRLGRWSLRPGVRVDGDSLMGRTTVAPRLAASWDVFGDRDTLLTAGVNRYYGRNIFAYKLREGRERLQLEQRRGADLIWRDVRVSPADYRFDRLRVPYGDELALGWNQRWAGLDLSLKYVRRDNRDEVLRQTIVNTDDSGFYDTRVNRYDNRGRSRSQTYTASLAPAQPLRWGPAVTTAEAAFDYTDVRRNYTDYETVYSETFETWVRYQGKLMRTWELPATSFNRPWTARLATQTRWEAAGLLWSNFLRYRSGYRGKRTVGNESYQGEAIAVIEEVAYPATWTWDSAVEWTLRLPRDQQAYARVEAQNLTNRANLISSATTATTVYEPGRSYWLELGYRF
>NZ_AP014940.1|WP_096378665.1|3310644_3311871_-|NO-inducible-flavohemoprotein
MTTALNEAAAAVVRATVPALAAHGHAVTTAMYRRLFRDERIAALFNHANQGGDNAQAHALAGAILAYAQHIDDLPALSGALERIAQKHVGYHILPEHYPFVAGALLGAIEETLGEAATPQVLAAWGEAYWFLADLLQRREAELRGELAQVVGGWSGWREFVVAAKRAENASSDAAIVSFELRPADGGAVIAHRPGQYLTLRYPVPGQGAVKRNYSISCGPNREAYRITVKREAHGHGGSRHLHDVMKLGDRIELTPPAGDFFLPDAPPRPVVLLSGGVGLTPMVSMLEAIAARHPDLDTHYVHGTADGASHAMAAHVRALAQAHGRIRVSTFYAEPTADGAARGEPHRTGLIETDWLRANVPLLDADIYLCGPRPFLRALVPALARAGVAGERVHYEFFGPSDEQLAA
>NZ_AP014940.1|WP_096378666.1|3311915_3312284_-|group-III-truncated-hemoglobin
MRSSHDLDEAALAALVRRFYAAVREDDRLGPVFAAAIDDWDAHERRLIDFWTSLMLGSGRYRGNPAQMHLRHAGRIQPELFAHWLALWRRCSEHTLPPAQAAAVQARAGRIAEHLQRLLAQA
>NZ_AP014940.1|WP_096378667.1|3312410_3312833_+|Rrf2-family-transcriptional-regulator
MKLSLYTDYSLRVLIHLGTHPGELASIAQIAQAYGISHSHLTKVVQDLGAAGYIETVRGRNGGIRLGRAPAKIGLGEVVRHTEAHFELVDCSGCLIAPACGLPPILAEATRAFFAVLDGYTVADLLGKQRALQRLFAVGG
>NZ_AP014940.1|WP_096378668.1|3313009_3314209_-|cellulase-family-glycosylhydrolase
MRRLSLSVLALALALNAPRPAAAADLIGFWDAPRHGGNSFNRLPPDAAYFAALRGYGASWVRLSYDKWKPEGRDFLIGDADDYQRLAPADLKTLKAALARADAAGLKIVVAPLSLPYSRWAQNNGGRFDDRLWQDRKHWEAAARFWRDLARELKDQPGIAAYNLINEPAPEKQAGLSEYASAQQRRDWYAAQRGGARDLPAFYQHIVRAIREVDPDTPIMLDAGWYASAGGFDYWPAPLADAKTLYSVHMYEPYQVTSAPNLKRAKPYVYPGPAPYGGREQTWNRERVAAHLAQAFDWAKTHQVPATRLVAGEFGCVRQLNDCARYLDDVLAALDRAGAHWAFYAFREDAWDAMDYELGKGKVDWRYWEAMEQGKPDPVSRKATPVFEPIRKRLSAGRE
>NZ_AP014940.1|WP_074868562.1|3314425_3315196_+|DNA/RNA-non-specific-endonuclease
MKFAACLAAVGLALAAPAAFAAACTSAHNEQYPSGRKPVLSNADLNEQTLSICYQDYNLYASKVTGTNLWSAQHLTRAKVIGAESINRIDSNFFSETGFPTKHASYTNSGYDRGHMMPAGDASTTPAQKETFSVANIVPQAPKLNRGTWARIESLVRTVAKEWDEAYIVTGPDFDDMNTTIASGAVVVPSQTWKAVYVPSAKVAGAYWCVNSDASSCSLISLNELKRRAFVDPFPSLGTALRAQTSADWTDILVLP
>NZ_AP014940.1|WP_096378669.1|3315489_3316413_+|glycerophosphodiester-phosphodiesterase
MKLHTHLLAAALAAAVLPAATACASSRPLIVAHRAGTADYPENTLLAIRGALANRAQALWLSVQLSADGVPVLYRPQDLATLTDARGLVSQYTAAQLAGFNAGYLFPNPDPAAPNPYPYRDRPQPLPSLDSALQLIAGRVPVMLDLKTAPDQRLVDAVAAVLERRQAWNNVQFYSTESGFDPMLARHPKARRFETRDATRGRLLQVALEQRCEPPAAPVWTAFELRRRLEVEETFTLGVGATTIPAATLWTPQSVACFRERSAAVGILVIGVNSSDDYRRAAMLGADAVLVDSPAAARRWSLSARRP
>NZ_AP014940.1|WP_096378670.1|3316470_3317025_+|DUF308-domain-containing-protein
MNAPLIAHFARHWWVLLVYGLIGLGFGVACFVAPAASVVALVWSFGLMALLEGALSAVALFSGPSALGKGWLALYALASLAFGALALVRPLAIADALILLLGLWLVVGGVLRVFWSVALRKAIDHEWFLALSGLLVLALGALLLLYPRVALVGVVWWIGLGALVFGLLQVFVALRVRRLSRLRV
>NZ_AP014940.1|WP_096378671.1|3317069_3317513_-|DUF4287-domain-containing-protein
MATASKAKTPAAKPAAKTASKTASKKVASKKVASEKPPAGKKTASAAPRSAPAKAAKKTAVPAKPLAAAKPAKSAVAPASADKVKGPASYFPSIEKTYGKPVAHWFAIIDALGARKHMDLVAELKSKHGLGHGHANALVAYRLAGKG
>NZ_AP014940.1|WP_172437249.1|3317649_3318447_-|DUF4198-domain-containing-protein
MSACAAPAAAHDFWIQPEPYRNDAAAATALTLQVGHGRDRQRSAIPARRIQRFEAVGGDGRRLDLRAQLHPDPHAPADARIAVPAGAWMLVLETDAGAQSRLPAPRFNDYLRAEGLTPALKQRRAQGRENADGAERYSRRSKALLRAGPAPAGVAALLAQPLGLPLEILLDADPQARAARLPVRVLWQGRPLPGALVKLTRLEDDAQPLDARRTDAAGRAEFAAPGAGAWLLNAIWTRPLPAGAEVDFETTFTSLSFDIVEAAPR
>NZ_AP014940.1|WP_172437250.1|3318497_3318992_-|hypothetical-protein
MSGAAWAPAVLCAALGLLLGFVPARVGRYAAMAFAAAWALVAGFSAATVALASMRYSTLACWIVAAAVAGALYAPTAVRERATWMLACVVGVCVAWASLASAACAPSPWSPVCLALALPAHWLAARGGGIAVRIGGAWLLAVALLMLVSTGSPALPGDLPDHLE

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Crispr_ID: NZ_AP014940_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_8

3665558-3665668

Orphan

Consensus_repeat	Method
GAGTTCGGCGGAGCTACGTCGCTGTGGTTGG	CRISPRCasFinder

1 spacers

csa3

The CRISPR arrays of NZ_AP014940_8

>merge|NZ_AP014940|8|3665558-3665668|CRISPRCasFinder
GAGTTCGGCGGAGCTACGTCGCTGTGGTTGGATTCCGGCTTTCGGCGGAATGACGGGCTGGGAGCTTCGGGTCTCCGGGTGAGTTCGGCGGAGCTACGTCGCTGCGGTTGG

>NZ_AP014940|8|8|3665558-3665668|CRISPRCasFinder
GAGTTCGGCGGAGCTACGTCGCTGTGGTTGG	ATTCCGGCTTTCGGCGGAATGACGGGCTGGGAGCTTCGGGTCTCCGGGT
GAGTTCGGCGGAGCTACGTCGCTGCGGTTGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_096378859.1\|3660382_3661231_+\|phosphatidylserine-decarboxylase	unknown	unknown	gnl\|CDD\|234591
NZ_AP014940.1\|WP_096378869.1\|3671247_3671664_+\|helix-turn-helix-transcriptional-regulator	csa3	COG0640_csa3_CAS-I-A	gnl\|CDD\|223713
NZ_AP014940.1\|WP_096378871.1\|3672912_3673902_-\|LLM-class-flavin-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|274646
NZ_AP014940.1\|WP_096378868.1\|3669708_3670524_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|375319
NZ_AP014940.1\|WP_096378862.1\|3663256_3664885_-\|transglycosylase-SLT-domain-containing-protein	unknown	unknown	gnl\|CDD\|381615
NZ_AP014940.1\|WP_096378858.1\|3659741_3660386_+\|SCO-family-protein	unknown	unknown	gnl\|CDD\|239266
NZ_AP014940.1\|WP_083382554.1\|3672370_3672808_+\|FKBP-type-peptidyl-prolyl-cis-trans-isomerase	unknown	unknown	gnl\|CDD\|223619
NZ_AP014940.1\|WP_145960088.1\|3652054_3654313_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225711
NZ_AP014940.1\|WP_096378867.1\|3669178_3669586_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096378860.1\|3661358_3662369_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096378870.1\|3671689_3672241_+\|SRPBCC-family-protein	unknown	unknown	gnl\|CDD\|176908
NZ_AP014940.1\|WP_096378857.1\|3656794_3657922_-\|chorismate-synthase	unknown	unknown	gnl\|CDD\|235438
NZ_AP014940.1\|WP_074866948.1\|3658666_3659596_-\|50S-ribosomal-protein-L3-N(5)-glutamine-methyltransferase	unknown	unknown	gnl\|CDD\|236988
NZ_AP014940.1\|WP_096378863.1\|3665960_3667496_+\|DUF853-family-protein	unknown	unknown	gnl\|CDD\|283518
NZ_AP014940.1\|WP_096378856.1\|3655791_3656802_-\|D-glycerate-dehydrogenase	unknown	unknown	gnl\|CDD\|240626
NZ_AP014940.1\|WP_096378855.1\|3654578_3655601_-\|aspartate-semialdehyde-dehydrogenase	unknown	unknown	gnl\|CDD\|237845
NZ_AP014940.1\|WP_096378865.1\|3668313_3668826_+\|transcription-elongation-factor-GreB	unknown	unknown	gnl\|CDD\|179345
NZ_AP014940.1\|WP_172437262.1\|3667629_3668127_+\|copper-resistance-protein-NlpE-N-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|377235
NZ_AP014940.1\|WP_096378872.1\|3674132_3674606_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096378861.1\|3662444_3663134_-\|lysoplasmalogenase	unknown	unknown	gnl\|CDD\|377946

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_096378859.1\|3660382_3661231_+\|phosphatidylserine-decarboxylase	gnl\|CDD\|234591	PRK00044, psd, phosphatidylserine decarboxylase; Reviewed.	1.20549e-167
NZ_AP014940.1\|WP_096378869.1\|3671247_3671664_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|223713	COG0640, ArsR, Predicted transcriptional regulators [Transcription].	2.06028e-16
NZ_AP014940.1\|WP_096378871.1\|3672912_3673902_-\|LLM-class-flavin-dependent-oxidoreductase	gnl\|CDD\|274646	TIGR03558, oxido_grp_1, luciferase family oxidoreductase, group 1. The Pfam domain family pfam00296 is named for luciferase-like monooxygenases, but the family also contains several coenzyme F420-dependent enzymes. This protein family represents a well-resolved clade within family pfam00296 and shows no restriction to coenzyme F420-positive species, unlike some other clades within pfam00296. [Unknown function, Enzymes of unknown specificity].	0
NZ_AP014940.1\|WP_096378868.1\|3669708_3670524_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|375319	pfam17765, MLTR_LBD, MmyB-like transcription regulator ligand binding domain. This domain is found in a family of actinobacterial transcription factors. The structure shows it has a PAS domain like fold and it is bound to Myristic acid.	2.91681e-22
NZ_AP014940.1\|WP_096378862.1\|3663256_3664885_-\|transglycosylase-SLT-domain-containing-protein	gnl\|CDD\|381615	cd16894, MltD-like, Membrane-bound lytic murein transglycosylase D and similar proteins. Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).	7.44896e-27
NZ_AP014940.1\|WP_096378858.1\|3659741_3660386_+\|SCO-family-protein	gnl\|CDD\|239266	cd02968, SCO, SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II.	4.47503e-47
NZ_AP014940.1\|WP_083382554.1\|3672370_3672808_+\|FKBP-type-peptidyl-prolyl-cis-trans-isomerase	gnl\|CDD\|223619	COG0545, FkpA, FKBP-type peptidyl-prolyl cis-trans isomerases 1 [Posttranslational modification, protein turnover, chaperones].	4.0834e-39
NZ_AP014940.1\|WP_145960088.1\|3652054_3654313_-\|hypothetical-protein	gnl\|CDD\|225711	COG3170, FimV, Tfp pilus assembly protein FimV [Cell motility and secretion / Intracellular trafficking and secretion].	8.46578e-26
NZ_AP014940.1\|WP_096378861.1\|3662444_3663134_-\|lysoplasmalogenase	gnl\|CDD\|377946	pfam07947, YhhN, YhhN family. The members of this family are similar to the hypothetical protein yhhN expressed by E. coli. Many are annotated as possible transmembrane proteins, and in fact they all have a high proportion of hydrophobic residues. A human member of this family, formerly known as TMEM86B, is a lysoplasmalogenase that catalyzes the hydrolysis of the vinyl ether bond of lysoplasmalogen. Putative conserved active site residues have been proposed for the YhhN family.	5.76543e-34
NZ_AP014940.1\|WP_096378870.1\|3671689_3672241_+\|SRPBCC-family-protein	gnl\|CDD\|176908	cd08899, SRPBCC_CalC_Aha1-like_6, Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and Aha1-like proteins. SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of a functionally uncharacterized subgroup of CalC- and Aha1-like proteins. This group shows similarity to the SRPBCC domains of Micromonospora echinospora CalC (a protein which confers resistance to enediynes) and human Aha1 (one of several co-chaperones which regulate the dimeric chaperone Hsp90), and belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands.	2.77096e-53
NZ_AP014940.1\|WP_096378857.1\|3656794_3657922_-\|chorismate-synthase	gnl\|CDD\|235438	PRK05382, PRK05382, chorismate synthase; Validated.	0
NZ_AP014940.1\|WP_074866948.1\|3658666_3659596_-\|50S-ribosomal-protein-L3-N(5)-glutamine-methyltransferase	gnl\|CDD\|236988	PRK11805, PRK11805, 50S ribosomal protein L3 N(5)-glutamine methyltransferase.	1.17203e-152
NZ_AP014940.1\|WP_096378863.1\|3665960_3667496_+\|DUF853-family-protein	gnl\|CDD\|283518	pfam05872, DUF853, Bacterial protein of unknown function (DUF853). This family consists of several bacterial proteins of unknown function. BMEI1370 is thought to be an ATPase.	0
NZ_AP014940.1\|WP_096378856.1\|3655791_3656802_-\|D-glycerate-dehydrogenase	gnl\|CDD\|240626	cd05301, GDH, D-glycerate dehydrogenase/hydroxypyruvate reductase (GDH). D-glycerate dehydrogenase (GDH, also known as hydroxypyruvate reductase, HPR) catalyzes the reversible reaction of (R)-glycerate + NAD+ to hydroxypyruvate + NADH + H+. In humans, HPR deficiency causes primary hyperoxaluria type 2, characterized by over-excretion of L-glycerate and oxalate in the urine, possibly due to an imbalance in competition with L-lactate dehydrogenase, another formate dehydrogenase (FDH)-like enzyme. GDH, like FDH and other members of the D-specific hydroxyacid dehydrogenase family that also includes L-alanine dehydrogenase and S-adenosylhomocysteine hydrolase, typically have a characteristic arrangement of 2 similar subdomains of the alpha/beta Rossmann-fold NAD+ binding form, despite often low sequence identity. The NAD+ binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain, which has a similar domain structure to the internal NAD binding domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD is bound, primarily to the C-terminal portion of the 2nd (internal) domain. Some related proteins have similar structural subdomain but with a tandem arrangement of the catalytic and NAD-binding subdomains in the linear sequence. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric.	1.69429e-146
NZ_AP014940.1\|WP_096378855.1\|3654578_3655601_-\|aspartate-semialdehyde-dehydrogenase	gnl\|CDD\|237845	PRK14874, PRK14874, aspartate-semialdehyde dehydrogenase; Provisional.	0
NZ_AP014940.1\|WP_096378865.1\|3668313_3668826_+\|transcription-elongation-factor-GreB	gnl\|CDD\|179345	PRK01885, greB, transcription elongation factor GreB; Reviewed.	3.58564e-82
NZ_AP014940.1\|WP_172437262.1\|3667629_3668127_+\|copper-resistance-protein-NlpE-N-terminal-domain-containing-protein	gnl\|CDD\|377235	pfam04170, NlpE, NlpE N-terminal domain. This family represents a bacterial outer membrane lipoprotein that is necessary for signalling by the Cpx pathway. This pathway responds to cell envelope disturbances and increases the expression of periplasmic protein folding and degradation factors. While the molecular function of the NlpE protein is unknown, it may be involved in detecting bacterial adhesion to abiotic surfaces. In Escherichia coli and Salmonella typhi, NlpE is also known to confer copper tolerance in copper-sensitive strains of Escherichia coli, and may be involved in copper efflux and delivery of copper to copper-dependent enzymes.	4.92491e-29

>NZ_AP014940.1|WP_096378862.1|3663256_3664885_-|transglycosylase-SLT-domain-containing-protein
MPAYSRSARAARALVGFRAAVAPLAAALALCSLSPQASALSKRDQAAVDALSQRMQSAEARYQSALVKIRNADPTGRQDSDAALEDMEDVIAACLKQKGCAPSTMLAGYKRLLKANADSVANTDEDAEDAGQLDSDGLAADVPEAARAAALLSDDGQRFVKMVQYNPAVQAGIRRWLTDLRGPLMQSYDNYQYMRQLMWPEFQRAGLPEALLFGIMAKESNGRVHSTSRVGAAGPLQFMFATGKRFGLGDDGSGFDTRYDPKQSAQAAAEYLNERLGQLNNSIEMSLAAYNGGEGRALRINNASGGRNFWDESVYNQFPAETRDYVPMVVAAAWLFLHPREYGLNFPKVDSKLAQLRLNRPSSIYELTICMGGSGSRDGYMRALRNLNPRYQADSYLSAGTTLNATTRMVSLYNRWCVQGKRADLARTLVASDANSAIVRTGPLTVLPASSTGEDGTVTYAGTSAAAVPTTVATGRPAPAPKPEPKKKAAPKDYKIQRGDTLTDVARKFSCDTRALAKANGLKAPRYAVKPGQRIKLSGCGD
>NZ_AP014940.1|WP_096378861.1|3662444_3663134_-|lysoplasmalogenase
MSQPTATYTRYVLSTRGWGAVVALSAALAIAGAYAPGAIWLHYLFKPATTLLIAAMVLREGAGADPRYRRAIFAGLLLSTAGDAFLMLPGDWFVFGLGSFLCAHLAYLVGLCRRARPFAAAWPFLAYAVVAAAVMSVLWPHLPNELRIPVIVYVAVLAAMAAQAAAVWRKRADAAGAAAAIGGACFVFSDATLAIDRFAAPFAAAQALVLVSYWAAQWWIGRSATLARD
>NZ_AP014940.1|WP_096378860.1|3661358_3662369_+|hypothetical-protein
MTRNGRLFVLAALALALAACGAKSESEQLADLRDGLTYTQYRRVSENGLPAALETYRFGAQFSDKAGIARSDLPELGPADLCIAHLLLAYGALGADKTTLALAETDIVEAQDCAAFDDLAAASLRSVAFQRLQWPQLAQAESERVWAAQGDGDFQKGPAGQMLALHLGLGYLAVSEKRWDRAQIHADALGQMLRAPWLGKIAGAGVAVQEGRPRDALISLKRLSADPSVPPELRKELTGFIAQVEAKGGDVDSFAFMPRLATSLAWDAVQAHGPEAMRAATRFADEQALKPVGESLQKGVGQASEAAGGWWRKLREAVSSSPAPEAPADGKAAPAG
>NZ_AP014940.1|WP_096378859.1|3660382_3661231_+|phosphatidylserine-decarboxylase
MSLVTTLTYVLPHRFLSGLARMLAYSDDPRVSRWLIDTVTEKFGVDLNEAANPDPRAYPTFNAFFTRALKPGARRAQGDARTLLMPADGRISQCGPIRAGEIFQAKGRSFTALELLGGDEAAAAPFRDGDYATVYLSPRDYHRVHMPWTGTLRETVHVPGRLFSVGPDAVRNVPRLFARNERLVCHFDTDFGPMALVMVGALLVSGVETVWSGIEIPAYGDRVTTKDYRGKGITLKRFEEMARFNYGSTVIVLLPPGAATLDAGLSAETAVRLGQPLARRTR
>NZ_AP014940.1|WP_096378858.1|3659741_3660386_+|SCO-family-protein
MFNRTNAIILVAALAAALGLWASQKYFGSAKRSHLPQTQAVRLFDPPRTLPAFSLRQSDGTQLIPGELKGHWTLVFLGFTHCPDVCPTTLAQMSVAQKAWESIPESTRPRVLFVSVDPERDSPDKIGEYAHGFHKDTLAATADVPALENFAKSLSMVFAKVPAPAGAPENQYSMDHSASMAVLDPQGRMAGLVRPPFEPNVIARDMAALTEASP
>NZ_AP014940.1|WP_074866948.1|3658666_3659596_-|50S-ribosomal-protein-L3-N(5)-glutamine-methyltransferase
MPASVSFEPLTLVDLIRYGASRFNAAGLSFGHSYDNALDEATQLVLHALHLPHDLSPVYGQGRVTTEEKDAVLALFQRRVDERIPAAYLTGEAWFAGLSFKSDARALVPRSPIAELIEAGFEPWLGGREVRRALDLCTGSGCIAIATGHYHPDWDVIGADINDAALSLAAENKERLLAGNVELRKSDLFQGLQGEVFDLIVTNPPYVTDDETDALPREYSFEPELGLRAGFDGLDLALKILRDAPQHLSEDGLLICEVGEAERALGELLPQLPLAWVEFKVGQMGIFVVERHDLVEHHDAIKRLADARA
>NZ_AP014940.1|WP_096378857.1|3656794_3657922_-|chorismate-synthase
MASNSFGTLLTVTTFGESHGPAIGCVVDGCPPGLELAPEEFRHDLERRATGRSRHTSQRRETDEIEILSGVYQGRTTGTPIALLIRNTDARSKDYGNIAEQFRPGHADYSYWQKYGHRDPRGGGRSSARETTMRVAAGVIAKKWLAQRYGVSVRGYMAQIGEVVPAGFDLDAVEGNPFFWPHAAQVDELERYMDALRKSGDSVGARVEVVADGVPPGWGEPIYGKLDGELAAALMSINAVKGVEIGDGFASVAQKGTQHRDELLPQGFASNHAGGILGGISTGQRLRCAAAFKPTSSLRLPGRSLDVHGNEVEVVTVGRHDPCVGVRATPICEAMVALVLMDQALRHRAQCGDVGTVTPRVPAQAEFGDAGAGDV
>NZ_AP014940.1|WP_096378856.1|3655791_3656802_-|D-glycerate-dehydrogenase
MSERPRVWVSQPLFDDIVARLGEHFEVETTAEVTQHAPDAVNAILRRMDGALVTLNDPIGAAQIEGASRLRAIANVGVGYNNLDVAALSAAGILASNTPDVLTETTADFGFALMMAAARRIGEAERWLREGHWQRWSFDSLLGADVHGATLGILGMGRIGQAIARRATGFGMRTLYHNRSRLPEAVEAECKASYVGFDELLARADHLILVLPYSPQAHHLIDAAALARMQPHATLTNIARGGIVDEDALCDALERGRLGAAGLDVYEGEPRLNPRLLAQRRVVLTPHIASGSLTTRRAMVALAVDNLIAALGCGPRAGDPPSPLNAAEAAAARAGR
>NZ_AP014940.1|WP_096378855.1|3654578_3655601_-|aspartate-semialdehyde-dehydrogenase
MNAKTSCNVAVVGATGAVGETMLKVLAERKFPIGKLHVLASERSAGEKIEFEGQTLVVQDLATFDPAGVDIALFSAGGSVSKEYAPKFAAAGAVVIDNSSAFRYQDDVPLVVSEVNPEALKNRPLGIVANPNCSTMQLMVALAPIHRKAKLERINIATYQSVSGTGKRAMEELGRQTAALLNFQEAEAEVYPVQIAFNVIPHGGDFTDNGYTTEEMKLVWETRKILGDDSIGVNATVVRVPVFYGHSEAVHIETRDKLSAADARALLEKAPGLVVVDEAKGGGYPTPVTHASGEDPVFVGRIREDISHPRGLSLWVVADNIRKGAATNAVQLAELVWNER
>NZ_AP014940.1|WP_145960088.1|3652054_3654313_-|hypothetical-protein
MRSGFARTALGLALALASSAACALGLGQIEVKSRAGQPLLAEIPVIASGPEELAQLRAGLASPETFQRIGLEPPQGIVTDLRFTLAVDANGKPIIRVTSTQPVQQPLLTFLIEVDWGQGRLTREYSALLDAPRTASAPMQPPIQAAAGAAPNTIERPLQAPLPFGAQPQQTDPLAVENAPPGYDPGNLGQAPALPPDAIAGQGEPLPQARPLPEAAPPAPAPRPNAGRIAREPRPQPAAAPAIPGDGEITVAQGQTLSGIAAQMGGAQSLNQTMIALLRANPEAFVGGNINRLRAGAVLRRPAGGEMASIDPREANELVRAQIQQWRQAPQRAVPQPLTVDADRVAKAPVAPAARASGRASDARLEIVPPGAERAQAGAQSGISAGGEGHMVREQVQQANETIAVREQELADLKSKVAELEKLSTDQQKLIAMKDSELAATQQRLAENQARADSGSPLPWLFGGLGLLALLAGGWVLSRREPKRPSFRAGSPVPVPFAAPAEPGPDPVETLRRKPEAAAVVDPVAQLLGQRDEPAAVDPDLYPVLDPGQGAIQDEPPAAAPRHTLDELAAAEPPVSRPLATDEPPAAPERVDPAAAPHWTAPVSEPKSQSRVPTWHSATAGRQPTREEQTLEQQLREPPALPAGSAAPVSAIPVAPIPVAPVAAAPVAAQAPSVEPVAVAQSSPQARPAAPSAASVGLERIELARAYLDLGDEGSARQLLGEVLINGDHAARQQAARLLRELEASGGDRAGA
>NZ_AP014940.1|WP_096378863.1|3665960_3667496_+|DUF853-family-protein
MAPTPGDTQNDILIGKAVTTPDSGQVFLHTKLGNRHGLVAGATGTGKTVTLMTLAEGFSRQGVPVFLADVKGDVAGLAVAGAANDKLQERLKEIGVADWTPQANPVVFWDLFGKLGHPVRTTVSEMGPTLLARILELNDTQSGVLDIVFKLADDRGLLLLDLEDLRALLGLVADERKDISTSYGLVSAQSIGAIQRSLLRLEQDGGDHFFGEPALELADLMRTTPNGHGVVNVLAADSLILKPRLYSSFLLWLLSELFEQLPEVGDLDRPKLVFVFDEAHLLFDDAPAALQQRVEQVVRIIRSKGVGVYFCSQFPDDIPDNILGQLGNRVQHALRAFTPRDQKAVRTAAETFVPNPALNVAEAISKLGTGEALVSTLQDKGVPMPVERTLVAPPRCRMGAITEAERAQVRAGSPIGGKYDTAVNRESAAEMLAKRADTAAEQAQAPPAKTREQDDQEEGGFGQAVKDAVFGTKRRQGMVETMAKQTARTVGTQVGRQILRGLLGGIFGGKR
>NZ_AP014940.1|WP_172437262.1|3667629_3668127_+|copper-resistance-protein-NlpE-N-terminal-domain-containing-protein
MNRKLLAFACLATLALSACNKPAEPAPAPADAPKAAEPAPAPEPAPAPAAEAAPAAFDAAAFAGTFSGTLPCADCSGIDTKLALKADGSYAIDESYQGKKDGQFKGDGTWTAEDNGKRVRLDPNSKSENDRLFEIVSKDEIRMLDTEGKKIDSQLDYSLKRAAGQ
>NZ_AP014940.1|WP_096378865.1|3668313_3668826_+|transcription-elongation-factor-GreB
MGRWRPPAEHSTALITREGHARLKHELDELWRLRRPEVVKALAAAAAEGDRSENAEYTYRKKQLAEIDRRVRYLSKRLPLLRVIESTPSDPQSVFFGAWVEVEDVASGELARYRIVGPDETDARLGHISIDSPLARAMLKRRVDDEFEAVLPGGPARFAIVEVAYAPPAG
>NZ_AP014940.1|WP_096378867.1|3669178_3669586_-|hypothetical-protein
MAIAAHRTHPALFLRRVVQADLAVSAAAGALQLAAAEPLARLTAIDAGFLRGSGLVLMAWVAFLGWTLSRRTIAAPLAWTLIAVNLAWVAASVLVWLEGAIAPNTLGTVYVLAQAAVVAVFADLQYFGLRRLRRG
>NZ_AP014940.1|WP_096378868.1|3669708_3670524_+|helix-turn-helix-domain-containing-protein
MNDSAPVGELLRQWRQRRRLTQFDLAEMAEISTRHVSFIETGRSLPSRAMLLRLADRLDVPLRERNALMTAAGLAPIYAERALDHPAMREAYAAVELVLYAHEPHPALAVDRHWNLIQHNRALAPMLAGVAEHLLAGPANVLRAALHPEGMAPSILNLGEWRAHILHRLRHQIETSRDPVLEALYAELEAYPAPADFDPAELTGAAHVAVPCRMRTPFGDLSFISTTTVFGTPMDVTLAELAIESFFPADAVTAQAMREFGASLAPSAAAG
>NZ_AP014940.1|WP_096378869.1|3671247_3671664_+|helix-turn-helix-transcriptional-regulator
MVDYHSQRLDALFQALADPTRRAMLRRLAEGERNVGELAGPFDMTLAAASKHIKALERAGLVRREVRGRIHVCRLDAEPLHGGFEWLRHYERFWNQRLDDLEALLRAEDQVVPAPPADAAPEPAPPPASRPQRRKPRP
>NZ_AP014940.1|WP_096378870.1|3671689_3672241_+|SRPBCC-family-protein
MNLSVNDAFGVLTAPDSVRIERVLPGPIERVWAYLTESDKRRRWLAAGDMDLRVGGAVELNFDNARLTHNDDPPPAKYANDCVNTMRGRITAIEPPHRLSYTWNEESGSKSEVTFLLSEQGDQVQLVVEHRHLSNRSGLVSVSGGWHAHLGLLIDVLAQREPEGFWRTHGRLDAEYERLIPQA
>NZ_AP014940.1|WP_083382554.1|3672370_3672808_+|FKBP-type-peptidyl-prolyl-cis-trans-isomerase
MTLAGCQRPSAQEEQAAAAPKVLHGRIDQFQAIDERVGTGAVAQSGQEVIVQYTGWFFDETAANKRGSKFDSSYDRNGRPFSFLLGAGRVIRGWDDGVAGMRVGGKRVLMIPSDLAYGKDGAGGGAIPPDASLVFEVELIGIEAR
>NZ_AP014940.1|WP_096378871.1|3672912_3673902_-|LLM-class-flavin-dependent-oxidoreductase
MLPYSVLDLAPVTEGSDTRQAFANSLDLARHAEALGYTRYWLAEHHNMPGIASAATAVLIGHLAGGTSTIRVGAGGIMLPNHAPLQVAEQFGTLASLYPGRIDLGLGRAPGTDHATARALRRYYDGADSFPQDVAELLHYFEPAQPQQAVRAVPGAGLEVPVWLLGSSLFSARLAAQLGLPFAFASHFAPDAMDQALSLYRRDFQPSARLQAPHAMLALNVVAASSSGEARRLFTTQQQAFVNLRRGRPGLIPPPIDDIESFWTPLEKAGVAQALACAVVGDPGEVAAGIAAFVERHRPDELMVTANIFEHGARLRSFELAAQALRSLA
>NZ_AP014940.1|WP_096378872.1|3674132_3674606_-|hypothetical-protein
MPDSPSAAVPAHWIADTQDIGRLVRAVYECISGPAGAARDWARFRYLMHPRALSLRTVVEADGSTRAVVFDVEQYIADVEPLFAQTDFFEVETDQRIERFGQIAHVWSKYDARPAPGSPVLLKRGANSIQVCREHGRWWVVCTVWDNEREGLAFELF

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Crispr_ID: NZ_AP014940_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_9

3670721-3670827

Orphan

Consensus_repeat	Method
CCGTCATTCCGGCGAAAGCCGGAATCCA	CRISPRCasFinder

1 spacers

csa3

The CRISPR arrays of NZ_AP014940_9

>merge|NZ_AP014940|9|3670721-3670827|CRISPRCasFinder
CCGTCATTCCGGCGAAAGCCGGAATCCAACCGCAGCGACGCGGCTCCGCCGTGATCTCCCGAAGCCTGCAACCCTCACGCCGTCATTCCGGCGAAAGCCGGAATCCA

>NZ_AP014940|9|9|3670721-3670827|CRISPRCasFinder
CCGTCATTCCGGCGAAAGCCGGAATCCA	ACCGCAGCGACGCGGCTCCGCCGTGATCTCCCGAAGCCTGCAACCCTCACG
CCGTCATTCCGGCGAAAGCCGGAATCCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_096378859.1\|3660382_3661231_+\|phosphatidylserine-decarboxylase	unknown	unknown	gnl\|CDD\|234591
NZ_AP014940.1\|WP_096378869.1\|3671247_3671664_+\|helix-turn-helix-transcriptional-regulator	csa3	COG0640_csa3_CAS-I-A	gnl\|CDD\|223713
NZ_AP014940.1\|WP_096378871.1\|3672912_3673902_-\|LLM-class-flavin-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|274646
NZ_AP014940.1\|WP_096378868.1\|3669708_3670524_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|375319
NZ_AP014940.1\|WP_096378862.1\|3663256_3664885_-\|transglycosylase-SLT-domain-containing-protein	unknown	unknown	gnl\|CDD\|381615
NZ_AP014940.1\|WP_096378858.1\|3659741_3660386_+\|SCO-family-protein	unknown	unknown	gnl\|CDD\|239266
NZ_AP014940.1\|WP_083382554.1\|3672370_3672808_+\|FKBP-type-peptidyl-prolyl-cis-trans-isomerase	unknown	unknown	gnl\|CDD\|223619
NZ_AP014940.1\|WP_096378860.1\|3661358_3662369_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096378870.1\|3671689_3672241_+\|SRPBCC-family-protein	unknown	unknown	gnl\|CDD\|176908
NZ_AP014940.1\|WP_096378873.1\|3675129_3681051_+\|alpha-2-macroglobulin	unknown	unknown	gnl\|CDD\|225248
NZ_AP014940.1\|WP_096378872.1\|3674132_3674606_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096378875.1\|3683820_3684501_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096378874.1\|3681061_3683440_+\|penicillin-binding-protein-1C	unknown	unknown	gnl\|CDD\|273954
NZ_AP014940.1\|WP_096378867.1\|3669178_3669586_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096378876.1\|3684721_3686053_-\|sorbosone-dehydrogenase-family-protein	unknown	unknown	gnl\|CDD\|225044
NZ_AP014940.1\|WP_096378863.1\|3665960_3667496_+\|DUF853-family-protein	unknown	unknown	gnl\|CDD\|283518
NZ_AP014940.1\|WP_172437262.1\|3667629_3668127_+\|copper-resistance-protein-NlpE-N-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|377235
NZ_AP014940.1\|WP_170849151.1\|3674662_3674815_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096378865.1\|3668313_3668826_+\|transcription-elongation-factor-GreB	unknown	unknown	gnl\|CDD\|179345
NZ_AP014940.1\|WP_096378861.1\|3662444_3663134_-\|lysoplasmalogenase	unknown	unknown	gnl\|CDD\|377946

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_096378859.1\|3660382_3661231_+\|phosphatidylserine-decarboxylase	gnl\|CDD\|234591	PRK00044, psd, phosphatidylserine decarboxylase; Reviewed.	1.20549e-167
NZ_AP014940.1\|WP_096378869.1\|3671247_3671664_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|223713	COG0640, ArsR, Predicted transcriptional regulators [Transcription].	2.06028e-16
NZ_AP014940.1\|WP_096378871.1\|3672912_3673902_-\|LLM-class-flavin-dependent-oxidoreductase	gnl\|CDD\|274646	TIGR03558, oxido_grp_1, luciferase family oxidoreductase, group 1. The Pfam domain family pfam00296 is named for luciferase-like monooxygenases, but the family also contains several coenzyme F420-dependent enzymes. This protein family represents a well-resolved clade within family pfam00296 and shows no restriction to coenzyme F420-positive species, unlike some other clades within pfam00296. [Unknown function, Enzymes of unknown specificity].	0
NZ_AP014940.1\|WP_096378868.1\|3669708_3670524_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|375319	pfam17765, MLTR_LBD, MmyB-like transcription regulator ligand binding domain. This domain is found in a family of actinobacterial transcription factors. The structure shows it has a PAS domain like fold and it is bound to Myristic acid.	2.91681e-22
NZ_AP014940.1\|WP_096378862.1\|3663256_3664885_-\|transglycosylase-SLT-domain-containing-protein	gnl\|CDD\|381615	cd16894, MltD-like, Membrane-bound lytic murein transglycosylase D and similar proteins. Lytic transglycosylases (LT) catalyze the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc). Membrane-bound lytic murein transglycosylase D protein (MltD) family members may have one or more small LysM domains, which may contribute to peptidoglycan binding. Unlike the similar "goose-type" lysozymes, LTs also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).	7.44896e-27
NZ_AP014940.1\|WP_096378858.1\|3659741_3660386_+\|SCO-family-protein	gnl\|CDD\|239266	cd02968, SCO, SCO (an acronym for Synthesis of Cytochrome c Oxidase) family; composed of proteins similar to Sco1, a membrane-anchored protein possessing a soluble domain with a TRX fold. Members of this family are required for the proper assembly of cytochrome c oxidase (COX). They contain a metal binding motif, typically CXXXC, which is located in a flexible loop. COX, the terminal enzyme in the respiratory chain, is imbedded in the inner mitochondrial membrane of all eukaryotes and in the plasma membrane of some prokaryotes. It is composed of two subunits, COX I and COX II. It has been proposed that Sco1 specifically delivers copper to the CuA site, a dinuclear copper center, of the COX II subunit. Mutations in human Sco1 and Sco2 cause fatal infantile hepatoencephalomyopathy and cardioencephalomyopathy, respectively. Both disorders are associated with severe COX deficiency in affected tissues. More recently, it has been argued that the redox sensitivity of the copper binding properties of Sco1 implies that it participates in signaling events rather than functioning as a chaperone that transfers copper to COX II.	4.47503e-47
NZ_AP014940.1\|WP_083382554.1\|3672370_3672808_+\|FKBP-type-peptidyl-prolyl-cis-trans-isomerase	gnl\|CDD\|223619	COG0545, FkpA, FKBP-type peptidyl-prolyl cis-trans isomerases 1 [Posttranslational modification, protein turnover, chaperones].	4.0834e-39
NZ_AP014940.1\|WP_096378870.1\|3671689_3672241_+\|SRPBCC-family-protein	gnl\|CDD\|176908	cd08899, SRPBCC_CalC_Aha1-like_6, Putative hydrophobic ligand-binding SRPBCC domain of an uncharacterized subgroup of CalC- and Aha1-like proteins. SRPBCC (START/RHO_alpha_C/PITP/Bet_v1/CoxG/CalC) domain of a functionally uncharacterized subgroup of CalC- and Aha1-like proteins. This group shows similarity to the SRPBCC domains of Micromonospora echinospora CalC (a protein which confers resistance to enediynes) and human Aha1 (one of several co-chaperones which regulate the dimeric chaperone Hsp90), and belongs to the SRPBCC domain superfamily of proteins that bind hydrophobic ligands. SRPBCC domains have a deep hydrophobic ligand-binding pocket and they bind diverse ligands.	2.77096e-53
NZ_AP014940.1\|WP_096378873.1\|3675129_3681051_+\|alpha-2-macroglobulin	gnl\|CDD\|225248	COG2373, COG2373, Large extracellular alpha-helical protein [General function prediction only].	0
NZ_AP014940.1\|WP_096378874.1\|3681061_3683440_+\|penicillin-binding-protein-1C	gnl\|CDD\|273954	TIGR02073, Includes:_Penicillin-insensitive_transglycosylase, penicillin-binding protein 1C. This subfamily of the penicillin binding proteins includes the member from E. coli designated penicillin-binding protein 1C. Members have both transglycosylase and transpeptidase domains and are involved in forming cross-links in the late stages of peptidoglycan biosynthesis. All members of this subfamily are presumed to have the same basic function. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan].	0
NZ_AP014940.1\|WP_096378863.1\|3665960_3667496_+\|DUF853-family-protein	gnl\|CDD\|283518	pfam05872, DUF853, Bacterial protein of unknown function (DUF853). This family consists of several bacterial proteins of unknown function. BMEI1370 is thought to be an ATPase.	0
NZ_AP014940.1\|WP_096378865.1\|3668313_3668826_+\|transcription-elongation-factor-GreB	gnl\|CDD\|179345	PRK01885, greB, transcription elongation factor GreB; Reviewed.	3.58564e-82
NZ_AP014940.1\|WP_172437262.1\|3667629_3668127_+\|copper-resistance-protein-NlpE-N-terminal-domain-containing-protein	gnl\|CDD\|377235	pfam04170, NlpE, NlpE N-terminal domain. This family represents a bacterial outer membrane lipoprotein that is necessary for signalling by the Cpx pathway. This pathway responds to cell envelope disturbances and increases the expression of periplasmic protein folding and degradation factors. While the molecular function of the NlpE protein is unknown, it may be involved in detecting bacterial adhesion to abiotic surfaces. In Escherichia coli and Salmonella typhi, NlpE is also known to confer copper tolerance in copper-sensitive strains of Escherichia coli, and may be involved in copper efflux and delivery of copper to copper-dependent enzymes.	4.92491e-29
NZ_AP014940.1\|WP_096378876.1\|3684721_3686053_-\|sorbosone-dehydrogenase-family-protein	gnl\|CDD\|225044	COG2133, COG2133, Glucose/sorbosone dehydrogenases [Carbohydrate transport and metabolism].	2.05307e-106
NZ_AP014940.1\|WP_096378861.1\|3662444_3663134_-\|lysoplasmalogenase	gnl\|CDD\|377946	pfam07947, YhhN, YhhN family. The members of this family are similar to the hypothetical protein yhhN expressed by E. coli. Many are annotated as possible transmembrane proteins, and in fact they all have a high proportion of hydrophobic residues. A human member of this family, formerly known as TMEM86B, is a lysoplasmalogenase that catalyzes the hydrolysis of the vinyl ether bond of lysoplasmalogen. Putative conserved active site residues have been proposed for the YhhN family.	5.76543e-34

>NZ_AP014940.1|WP_096378868.1|3669708_3670524_+|helix-turn-helix-domain-containing-protein
MNDSAPVGELLRQWRQRRRLTQFDLAEMAEISTRHVSFIETGRSLPSRAMLLRLADRLDVPLRERNALMTAAGLAPIYAERALDHPAMREAYAAVELVLYAHEPHPALAVDRHWNLIQHNRALAPMLAGVAEHLLAGPANVLRAALHPEGMAPSILNLGEWRAHILHRLRHQIETSRDPVLEALYAELEAYPAPADFDPAELTGAAHVAVPCRMRTPFGDLSFISTTTVFGTPMDVTLAELAIESFFPADAVTAQAMREFGASLAPSAAAG
>NZ_AP014940.1|WP_096378867.1|3669178_3669586_-|hypothetical-protein
MAIAAHRTHPALFLRRVVQADLAVSAAAGALQLAAAEPLARLTAIDAGFLRGSGLVLMAWVAFLGWTLSRRTIAAPLAWTLIAVNLAWVAASVLVWLEGAIAPNTLGTVYVLAQAAVVAVFADLQYFGLRRLRRG
>NZ_AP014940.1|WP_096378865.1|3668313_3668826_+|transcription-elongation-factor-GreB
MGRWRPPAEHSTALITREGHARLKHELDELWRLRRPEVVKALAAAAAEGDRSENAEYTYRKKQLAEIDRRVRYLSKRLPLLRVIESTPSDPQSVFFGAWVEVEDVASGELARYRIVGPDETDARLGHISIDSPLARAMLKRRVDDEFEAVLPGGPARFAIVEVAYAPPAG
>NZ_AP014940.1|WP_172437262.1|3667629_3668127_+|copper-resistance-protein-NlpE-N-terminal-domain-containing-protein
MNRKLLAFACLATLALSACNKPAEPAPAPADAPKAAEPAPAPEPAPAPAAEAAPAAFDAAAFAGTFSGTLPCADCSGIDTKLALKADGSYAIDESYQGKKDGQFKGDGTWTAEDNGKRVRLDPNSKSENDRLFEIVSKDEIRMLDTEGKKIDSQLDYSLKRAAGQ
>NZ_AP014940.1|WP_096378863.1|3665960_3667496_+|DUF853-family-protein
MAPTPGDTQNDILIGKAVTTPDSGQVFLHTKLGNRHGLVAGATGTGKTVTLMTLAEGFSRQGVPVFLADVKGDVAGLAVAGAANDKLQERLKEIGVADWTPQANPVVFWDLFGKLGHPVRTTVSEMGPTLLARILELNDTQSGVLDIVFKLADDRGLLLLDLEDLRALLGLVADERKDISTSYGLVSAQSIGAIQRSLLRLEQDGGDHFFGEPALELADLMRTTPNGHGVVNVLAADSLILKPRLYSSFLLWLLSELFEQLPEVGDLDRPKLVFVFDEAHLLFDDAPAALQQRVEQVVRIIRSKGVGVYFCSQFPDDIPDNILGQLGNRVQHALRAFTPRDQKAVRTAAETFVPNPALNVAEAISKLGTGEALVSTLQDKGVPMPVERTLVAPPRCRMGAITEAERAQVRAGSPIGGKYDTAVNRESAAEMLAKRADTAAEQAQAPPAKTREQDDQEEGGFGQAVKDAVFGTKRRQGMVETMAKQTARTVGTQVGRQILRGLLGGIFGGKR
>NZ_AP014940.1|WP_096378862.1|3663256_3664885_-|transglycosylase-SLT-domain-containing-protein
MPAYSRSARAARALVGFRAAVAPLAAALALCSLSPQASALSKRDQAAVDALSQRMQSAEARYQSALVKIRNADPTGRQDSDAALEDMEDVIAACLKQKGCAPSTMLAGYKRLLKANADSVANTDEDAEDAGQLDSDGLAADVPEAARAAALLSDDGQRFVKMVQYNPAVQAGIRRWLTDLRGPLMQSYDNYQYMRQLMWPEFQRAGLPEALLFGIMAKESNGRVHSTSRVGAAGPLQFMFATGKRFGLGDDGSGFDTRYDPKQSAQAAAEYLNERLGQLNNSIEMSLAAYNGGEGRALRINNASGGRNFWDESVYNQFPAETRDYVPMVVAAAWLFLHPREYGLNFPKVDSKLAQLRLNRPSSIYELTICMGGSGSRDGYMRALRNLNPRYQADSYLSAGTTLNATTRMVSLYNRWCVQGKRADLARTLVASDANSAIVRTGPLTVLPASSTGEDGTVTYAGTSAAAVPTTVATGRPAPAPKPEPKKKAAPKDYKIQRGDTLTDVARKFSCDTRALAKANGLKAPRYAVKPGQRIKLSGCGD
>NZ_AP014940.1|WP_096378861.1|3662444_3663134_-|lysoplasmalogenase
MSQPTATYTRYVLSTRGWGAVVALSAALAIAGAYAPGAIWLHYLFKPATTLLIAAMVLREGAGADPRYRRAIFAGLLLSTAGDAFLMLPGDWFVFGLGSFLCAHLAYLVGLCRRARPFAAAWPFLAYAVVAAAVMSVLWPHLPNELRIPVIVYVAVLAAMAAQAAAVWRKRADAAGAAAAIGGACFVFSDATLAIDRFAAPFAAAQALVLVSYWAAQWWIGRSATLARD
>NZ_AP014940.1|WP_096378860.1|3661358_3662369_+|hypothetical-protein
MTRNGRLFVLAALALALAACGAKSESEQLADLRDGLTYTQYRRVSENGLPAALETYRFGAQFSDKAGIARSDLPELGPADLCIAHLLLAYGALGADKTTLALAETDIVEAQDCAAFDDLAAASLRSVAFQRLQWPQLAQAESERVWAAQGDGDFQKGPAGQMLALHLGLGYLAVSEKRWDRAQIHADALGQMLRAPWLGKIAGAGVAVQEGRPRDALISLKRLSADPSVPPELRKELTGFIAQVEAKGGDVDSFAFMPRLATSLAWDAVQAHGPEAMRAATRFADEQALKPVGESLQKGVGQASEAAGGWWRKLREAVSSSPAPEAPADGKAAPAG
>NZ_AP014940.1|WP_096378859.1|3660382_3661231_+|phosphatidylserine-decarboxylase
MSLVTTLTYVLPHRFLSGLARMLAYSDDPRVSRWLIDTVTEKFGVDLNEAANPDPRAYPTFNAFFTRALKPGARRAQGDARTLLMPADGRISQCGPIRAGEIFQAKGRSFTALELLGGDEAAAAPFRDGDYATVYLSPRDYHRVHMPWTGTLRETVHVPGRLFSVGPDAVRNVPRLFARNERLVCHFDTDFGPMALVMVGALLVSGVETVWSGIEIPAYGDRVTTKDYRGKGITLKRFEEMARFNYGSTVIVLLPPGAATLDAGLSAETAVRLGQPLARRTR
>NZ_AP014940.1|WP_096378858.1|3659741_3660386_+|SCO-family-protein
MFNRTNAIILVAALAAALGLWASQKYFGSAKRSHLPQTQAVRLFDPPRTLPAFSLRQSDGTQLIPGELKGHWTLVFLGFTHCPDVCPTTLAQMSVAQKAWESIPESTRPRVLFVSVDPERDSPDKIGEYAHGFHKDTLAATADVPALENFAKSLSMVFAKVPAPAGAPENQYSMDHSASMAVLDPQGRMAGLVRPPFEPNVIARDMAALTEASP
>NZ_AP014940.1|WP_096378869.1|3671247_3671664_+|helix-turn-helix-transcriptional-regulator
MVDYHSQRLDALFQALADPTRRAMLRRLAEGERNVGELAGPFDMTLAAASKHIKALERAGLVRREVRGRIHVCRLDAEPLHGGFEWLRHYERFWNQRLDDLEALLRAEDQVVPAPPADAAPEPAPPPASRPQRRKPRP
>NZ_AP014940.1|WP_096378870.1|3671689_3672241_+|SRPBCC-family-protein
MNLSVNDAFGVLTAPDSVRIERVLPGPIERVWAYLTESDKRRRWLAAGDMDLRVGGAVELNFDNARLTHNDDPPPAKYANDCVNTMRGRITAIEPPHRLSYTWNEESGSKSEVTFLLSEQGDQVQLVVEHRHLSNRSGLVSVSGGWHAHLGLLIDVLAQREPEGFWRTHGRLDAEYERLIPQA
>NZ_AP014940.1|WP_083382554.1|3672370_3672808_+|FKBP-type-peptidyl-prolyl-cis-trans-isomerase
MTLAGCQRPSAQEEQAAAAPKVLHGRIDQFQAIDERVGTGAVAQSGQEVIVQYTGWFFDETAANKRGSKFDSSYDRNGRPFSFLLGAGRVIRGWDDGVAGMRVGGKRVLMIPSDLAYGKDGAGGGAIPPDASLVFEVELIGIEAR
>NZ_AP014940.1|WP_096378871.1|3672912_3673902_-|LLM-class-flavin-dependent-oxidoreductase
MLPYSVLDLAPVTEGSDTRQAFANSLDLARHAEALGYTRYWLAEHHNMPGIASAATAVLIGHLAGGTSTIRVGAGGIMLPNHAPLQVAEQFGTLASLYPGRIDLGLGRAPGTDHATARALRRYYDGADSFPQDVAELLHYFEPAQPQQAVRAVPGAGLEVPVWLLGSSLFSARLAAQLGLPFAFASHFAPDAMDQALSLYRRDFQPSARLQAPHAMLALNVVAASSSGEARRLFTTQQQAFVNLRRGRPGLIPPPIDDIESFWTPLEKAGVAQALACAVVGDPGEVAAGIAAFVERHRPDELMVTANIFEHGARLRSFELAAQALRSLA
>NZ_AP014940.1|WP_096378872.1|3674132_3674606_-|hypothetical-protein
MPDSPSAAVPAHWIADTQDIGRLVRAVYECISGPAGAARDWARFRYLMHPRALSLRTVVEADGSTRAVVFDVEQYIADVEPLFAQTDFFEVETDQRIERFGQIAHVWSKYDARPAPGSPVLLKRGANSIQVCREHGRWWVVCTVWDNEREGLAFELF
>NZ_AP014940.1|WP_170849151.1|3674662_3674815_-|hypothetical-protein
MDIVALLVVVAALWLAFKLVGFALRSAMWLLVLGGLYWLIAPLAGWPMPF
>NZ_AP014940.1|WP_096378873.1|3675129_3681051_+|alpha-2-macroglobulin
MQTTPSPSQPAPPAEAGASGRANAWTRATQAVFGQMAWTPPPWLAALIARIRQRPGLYLGSLLGLLVAAWLAHWLITRPKPVIPGALSVELHAPELTDYERKPPTVHRLSLTFSDSAAPLKQIGNAPVGVSLSPELKGAWTWEDDKTLVFVPATDWPVKTKYKVEIDPQTSVAPKVALQEHEFEFETAPFKAELSNSEFYQDPQDPALKKGVFELKFSHPVDEAQLQRRVVLALVDGGGSAQAAPKYTLTYDDSRLKAWVHSEPLKLPENGGTLTLDVAAGVVSALGGEGSPEKLSAQVKLPSLYSVNIDDVTTTLVENERFEPEQALVLSFNNAMRDTDVAGATRAWLLPAKDPRRPAKEQSGNRSWSTGDVDEAVLKAAAPLPLSPIPAEREYTAVHSFKFQAPPDRYVYVRVNKGLKAFGGFLLGRDHAVALRVPEYPKLLRFVGEGALLSLRGERRISVVSRNVPRARLEIARILPEQIQHLVVDNRGGYATPRMYNIDADSLVEREERRLTLPAEDPAKAHYEGVDLGAYLKPNRRGVFLLSLRTMSDSDAERPSEETLADDAGSEEDSRLVVLTDLGIAVKQGLDGRRDVFVQSLSNGTPVAGARVRAVARNGETLVEADTDASGRAQLPSLKGFKREKQPAMLTVSQGEDYSFLPIDDYQRKLDYSRFDIGGEPNDIEAGALNAFLFSDRGLYRPGDTVNIGMIVRAADWKRPLAGLPLEWEFTDPRGNVAKRQKLKLSEQGFESASFAPSESAPSGTWQVQLFLLGRDDQRTSIGSTSVQVREFAPDTMKVAVKLSADNPRGWIKPDQLSAVVSAENLFGTPAQQRKVEGTMVLRPYLPRFAQYPGYQFSDPQAAREGYDEALSDQTTDAQGQATFKLDLTKYERATYQLSFLARAFEPGSGRNVAAQTSALVSNNDFLVGIKAADSLDYIQRGAKRSLQLLSIGQDGEPKPVPGLRAVVVEKRYVSVLTKQDSGLYRYVSHERRYDLREQPLALAGGRQSVALQTDQPGDFVVEVRGSDGKVLNQIGYRVAGAANLSRSLERNAELGLTLSKPSYKPGETIEVSIRAPYPGAGLITIERDKVYAHAWFRADSTASVQKIVLPADFEGNGYVNVQFLRDPNSDEIYMSPLSFGVAPFAVDRSARTQPLSVSLPKVTKPGQTVNASITTEGKARVVLFAVDEGILQVARYRVGEPLDHFFRKKMLQVDTAQILDLLLPEFSRIVAGAAPGGDGEGGMAKHLNPFKRKTEKPAVWWSGIVDVDGRREFPFVLPDHFNGKVRVVAVAVTPQRIGIVQDEAIIRGDFVLTPTLPTHVAPGDEFDLPVGVANTIEGAKQASKVTVSLQLPPGLSLAGAAPAPVSIAPRSETTVRFRVRAGNALGALPVAIQAVSGTYNAKRRIELSLRPAIVARQDLIAGRADKRTVIQPLRAMFDQQATRRVSASVSPLVAVDGLSAYLADYPYQCSEQVLSGAFPALVLGAHPELGKVVAAGKGDPRQNVIDLLRARQNSEGGIGLWTATPDADDFVTGYAALYLIEARERGQAVPDDLLKSLNGYLEQRAADRSGNDLPALRHRALAVYLLVRQGRTASNLLSAVHEQIKRDQPKTWENDVAGLLIASSYQLLQQDKPARALATVALRRANAAATTVRTAYASYYDGGIDQAWTVYLLNRHFGAISRDQLKQTALERLLDPLRHDSYNTLSSALTVLALDAYASAQPQQPLPVLEAAGKDGKSRRIGAAAGLISRGDFAGGDVRLWVAPGGDAPAWYLVNQSGYDRSVPKAVQDKGLEVVRDYLDDAGKPVTSIKQGQEVTVRLRVRALGAPMRDNIAVVDLLPGGFETVMQYAAPAAAASQSSASEDECGEECGEGEEGDGDGQPSRDGPDPNAAPAQTLALPGSSFQPQHVEQREDRVILYGSIGGQASEFRYKVRANNSGNFVVPPAYAESMYERSVYAQGGPAGTLQVTAPTP
>NZ_AP014940.1|WP_096378874.1|3681061_3683440_+|penicillin-binding-protein-1C
MKVLSSLRRGLKRWRWALIVLIALAAALTVIRFYPRPGLADAIPLSTVVRDREGRLLRLALASDQRYRLWVPLDNISPQLVESVMLQEDAWFYWHPGFNPISLVRGAWSTYGSGEARVGGSTLTMQLARLRWRLQTRDIRGKLVQIARAAQLELCYSKREILEAYLNLAPYGGNIEGVGAASLIYYRKPAGELTLPESLALAVLPQAPSRRGKLAARDDDAYYIGAGLEAARARLYARWRERHPRDSAQDALLRLPLRLHSARELPYRAPHLVDRVLSERAWHPQSGPELTTTLDLRMQRLLEERVGNYLRRGRERGLRNASAMLIDTRDMGVRALVGSADYFDASIQGQVNGSAAKRSPGSTLKPFIYALALDQGVLHPQTVLRDVPSAFGPYTPENFDGRFMGPVTATDALVRSRNIPAVYVASQLKQPSFYDFLRQAGVSRMASRDHYGLALVLGGGEVTMEELARMYAMLGNDGRLRALRWRDSDPAEDGARLLSAEAAFITRDMLQQNPRPDAGSQSSSRPLPVAWKTGTSWAFRDAWSAGLVGPYVLVVWLGNFDGSSNPALIGVEAAAPLFFDIVDGLQAARVDLAEPVRQWPLNLKRVEICRASGDLPNAWCPQRGVTWFIPGKSPIRISTVHRAVIVDSASGKPVCGRFDPATMRQEVYEFWPSDLAQVFAQAGIPRRRPPAGHDCGGAQDWLGSAPSITSPFRATRYTMRLSHPEQLSLSLAATVDADVSRLYWFVGNTFIGSAEAGKALAWAPDRTGQFRLSVVDDHGRSDQREIEVAVVQ
>NZ_AP014940.1|WP_096378875.1|3683820_3684501_+|hypothetical-protein
MLRPIIACFALAALAGAAGAATPQPPASSAPQPPSASPTQAQDIAFDHVRGCWIRREEPDGRATALLRLLPPPEHPGWLNGQISRPEGDDPDRRLHLWFSRDGRTAVLASQPLADPTRAPAGGKPETQIRPLAKTYPPGRAPGSSQSLVLMPQPRIEFVRVPTVTALTADWPADAFNADYVAGAAATGTRRLRVQASPERLTLTLLAGSGQARDLTLFDGRRDGCD
>NZ_AP014940.1|WP_096378876.1|3684721_3686053_-|sorbosone-dehydrogenase-family-protein
MSAASRSERLRWIALAPLALALAACGERAKLQVADGTGPAPQLPAPNPTMIPTVDIATAVGWPAGAKPTPAPGLAVNAFAQGLDHPRWLYVLPNGDVLVAESNAPQSEHKPSGIKAWFAARFMKKAGAAVPSADRISLLRDADGDGVAETRTIFLQGLHSPFGMTLIGDRLYVANADAVWRFAYRPGETAIAGAGEKVTELPAGINHHWTKNLIADASGSKLYVTVGSNSNVGENGMAAEEGRAAIWQLDPASGEKRLFATGLRNPNGLAWEPATGKLWTAVNERDEIGSDLVPDYITSVEDGAFYGWPYSYYGQHVDERVQPPRPDLVAKARAPDYALGPHTASLGIAFAQGAKLPAQYAQGLFVGQHGSWNRKPKSGYKVIFVPFADGKPAGAPQDVLSGFLDAREQAQGRPVDVRIDARGALLVSDDVGNTVWRVTAAGG

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Crispr_ID: NZ_AP014940_10

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_10

4235710-4235812

Orphan

Consensus_repeat	Method
CGTCATTCCGGCGAAAGCCGGAA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP014940_10

>merge|NZ_AP014940|10|4235710-4235812|CRISPRCasFinder
CGTCATTCCGGCGAAAGCCGGAATCCAACCGAAGCGACGCAGCTCCGCCGTAACCTCCCGAAGCCTCACAACCCCCAGCTCGTCATTCCGGCGAAAGCCGGAA

>NZ_AP014940|10|10|4235710-4235812|CRISPRCasFinder
CGTCATTCCGGCGAAAGCCGGAA	TCCAACCGAAGCGACGCAGCTCCGCCGTAACCTCCCGAAGCCTCACAACCCCCAGCT
CGTCATTCCGGCGAAAGCCGGAA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_096379254.1\|4245017_4245812_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096379249.1\|4237312_4238581_-\|multidrug-effflux-MFS-transporter	unknown	unknown	gnl\|CDD\|340878
NZ_AP014940.1\|WP_096379250.1\|4238577_4239033_-\|VOC-family-protein	unknown	unknown	gnl\|CDD\|319916
NZ_AP014940.1\|WP_096379245.1\|4230175_4231693_-\|DNA-binding-protein	unknown	unknown	gnl\|CDD\|226699
NZ_AP014940.1\|WP_139174664.1\|4229825_4230179_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096383612.1\|4226010_4226445_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_083382326.1\|4226548_4227025_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|376346
NZ_AP014940.1\|WP_096379248.1\|4236152_4237067_-\|siderophore-interacting-protein	unknown	unknown	gnl\|CDD\|99790
NZ_AP014940.1\|WP_074863511.1\|4232474_4233155_-\|VWA-domain-containing-protein	unknown	unknown	gnl\|CDD\|226696
NZ_AP014940.1\|WP_096379247.1\|4233369_4235460_+\|phospholipase-C,-phosphocholine-specific	unknown	unknown	gnl\|CDD\|274561
NZ_AP014940.1\|WP_096379243.1\|4222586_4225910_+\|winged-helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|226233
NZ_AP014940.1\|WP_096379251.1\|4239555_4242414_+\|aminomethyl-transferring-glycine-dehydrogenase	unknown	unknown	gnl\|CDD\|235432
NZ_AP014940.1\|WP_096379255.1\|4245827_4246961_+\|type-IV-secretion-system-protein	unknown	unknown	gnl\|CDD\|377390
NZ_AP014940.1\|WP_172437285.1\|4246963_4247467_+\|DUF4189-domain-containing-protein	unknown	unknown	gnl\|CDD\|372741
NZ_AP014940.1\|WP_096379246.1\|4231704_4232463_-\|protein-phosphatase-2C-domain-containing-protein	unknown	unknown	gnl\|CDD\|379325
NZ_AP014940.1\|WP_096383615.1\|4247522_4248101_+\|type-IV-secretion-system-protein	unknown	unknown	gnl\|CDD\|377390
NZ_AP014940.1\|WP_096379252.1\|4242693_4243164_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096379244.1\|4227066_4227450_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096379253.1\|4243421_4244438_+\|GGDEF-domain-containing-protein	unknown	unknown	gnl\|CDD\|143635
NZ_AP014940.1\|WP_074863503.1\|4227935_4229366_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_096379255.1\|4245827_4246961_+\|type-IV-secretion-system-protein	gnl\|CDD\|377390	pfam04610, TrbL, TrbL/VirB6 plasmid conjugal transfer protein.	2.82586e-20
NZ_AP014940.1\|WP_096379250.1\|4238577_4239033_-\|VOC-family-protein	gnl\|CDD\|319916	cd07253, GLOD5, Human glyoxalase domain-containing protein 5 and similar proteins. Uncharacterized subfamily of VOC family contains human glyoxalase domain-containing protein 5 and similar proteins. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.	4.83316e-33
NZ_AP014940.1\|WP_096379245.1\|4230175_4231693_-\|DNA-binding-protein	gnl\|CDD\|226699	COG4248, COG4248, Uncharacterized protein with protein kinase and helix-hairpin-helix DNA-binding domains [General function prediction only].	2.24592e-24
NZ_AP014940.1\|WP_074863511.1\|4232474_4233155_-\|VWA-domain-containing-protein	gnl\|CDD\|226696	COG4245, TerY, Uncharacterized protein encoded in toxicity protection region of plasmid R478, contains von Willebrand factor (vWF) domain [General function prediction only].	1.93593e-51
NZ_AP014940.1\|WP_096379249.1\|4237312_4238581_-\|multidrug-effflux-MFS-transporter	gnl\|CDD\|340878	cd17320, MFS_MdfA_MDR_like, Multidrug transporter MdfA and similar multidrug resistance (MDR) transporters of the Major Facilitator Superfamily. This family is composed of bacterial multidrug resistance (MDR) transporters including several proteins from Escherichia coli such as MdfA (also called chloramphenicol resistance pump Cmr), EmrD, MdtM, MdtL, bicyclomycin resistance protein (also called sulfonamide resistance protein), and the uncharacterized inner membrane transport protein YdhC. EmrD is a proton-dependent secondary transporter, first identified as an efflux pump for uncouplers of oxidative phosphorylation. It expels a range of drug molecules and amphipathic compounds across the inner membrane of E. coli. Similarly, MdfA is a secondary multidrug transporter that exports a broad spectrum of structurally and electrically dissimilar toxic compounds. These MDR transporters are drug/H+ antiporters (DHA) belonging to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.01549e-102
NZ_AP014940.1\|WP_083382326.1\|4226548_4227025_-\|hypothetical-protein	gnl\|CDD\|376346	pfam00545, Ribonuclease, ribonuclease. This enzyme hydrolyzes RNA and oligoribonucleotides.	2.58435e-08
NZ_AP014940.1\|WP_096379253.1\|4243421_4244438_+\|GGDEF-domain-containing-protein	gnl\|CDD\|143635	cd01949, GGDEF, Diguanylate-cyclase (DGC) or GGDEF domain. Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.	1.40203e-53
NZ_AP014940.1\|WP_096379248.1\|4236152_4237067_-\|siderophore-interacting-protein	gnl\|CDD\|99790	cd06193, siderophore_interacting, Siderophore interacting proteins share the domain structure of the ferredoxin reductase like family. Siderophores are produced in various bacteria (and some plants) to extract iron from hosts. Binding constants are high, so iron can be pilfered from transferrin and lactoferrin for bacterial uptake, contributing to pathogen virulence. Ferredoxin reductase (FNR), an FAD and NAD(P) binding protein, was intially identified as a chloroplast reductase activity, catalyzing the electron transfer from reduced iron-sulfur protein ferredoxin to NADP+ as the final step in the electron transport mechanism of photosystem I. FNR transfers electrons from reduced ferredoxin to FAD (forming FADH2 via a semiquinone intermediate) and then transfers a hydride ion to convert NADP+ to NADPH. FNR has since been shown to utilize a variety of electron acceptors and donors and has a variety of physiological functions including nitrogen assimilation, dinitrogen fixation, steroid hydroxylation, fatty acid metabolism, oxygenase activity, and methane assimilation in a variety of organisms. FNR has an NAD(P)-binding sub-domain of the alpha/beta class and a discrete (usually N-terminal) flavin sub-domain which vary in orientation with respect to the NAD(P) binding domain. The N-terminal moeity may contain a flavin prosthetic group (as in flavoenzymes) or use flavin as a substrate. Because flavins such as FAD can exist in oxidized, semiquinone (one-electron reduced), or fully reduced hydroquinone forms, FNR can interact with one and two electron carriers. FNR has a strong preference for NADP(H) vs NAD(H).	1.16475e-72
NZ_AP014940.1\|WP_096379243.1\|4222586_4225910_+\|winged-helix-turn-helix-domain-containing-protein	gnl\|CDD\|226233	COG3710, CadC, DNA-binding winged-HTH domains [Transcription].	2.77231e-22
NZ_AP014940.1\|WP_096379251.1\|4239555_4242414_+\|aminomethyl-transferring-glycine-dehydrogenase	gnl\|CDD\|235432	PRK05367, PRK05367, aminomethyl-transferring glycine dehydrogenase.	0
NZ_AP014940.1\|WP_172437285.1\|4246963_4247467_+\|DUF4189-domain-containing-protein	gnl\|CDD\|372741	pfam13827, DUF4189, Domain of unknown function (DUF4189). This domain of unknown function contains six well-conserved cysteine residues.	1.47589e-17
NZ_AP014940.1\|WP_096379246.1\|4231704_4232463_-\|protein-phosphatase-2C-domain-containing-protein	gnl\|CDD\|379325	pfam13672, PP2C_2, Protein phosphatase 2C. Protein phosphatase 2C is a Mn++ or Mg++ dependent protein serine/threonine phosphatase.	4.93159e-34
NZ_AP014940.1\|WP_096383615.1\|4247522_4248101_+\|type-IV-secretion-system-protein	gnl\|CDD\|377390	pfam04610, TrbL, TrbL/VirB6 plasmid conjugal transfer protein.	5.48049e-06
NZ_AP014940.1\|WP_096379247.1\|4233369_4235460_+\|phospholipase-C,-phosphocholine-specific	gnl\|CDD\|274561	TIGR03396, PC_PLC, phospholipase C, phosphocholine-specific, Pseudomonas-type. Members of this protein family are bacterial, phosphatidylcholine-hydrolyzing phospholipase C enzymes, with a characteristic domain architecture as found in hemolytyic (PlcH) and nonhemolytic (PlcN) secreted enzymes of Pseudomonas aeruginosa. PlcH hydrolyzes phosphatidylcholine to diacylglycerol and phosphocholine, but unlike PlcN can also hydrolyze sphingomyelin to ceramide ((N-acylsphingosine)) and phosphocholine. Members of this family share the twin-arginine signal sequence for Sec-independent transport across the plasma membrane. PlcH is secreted as a heterodimer with a small chaperone, PlcR, encoded immediately downstream. [Cellular processes, Pathogenesis].	0

>NZ_AP014940.1|WP_096379247.1|4233369_4235460_+|phospholipase-C,-phosphocholine-specific
MTDQHDPSRRGFLRGAAGATAAGLALNLFPPSIQKALAIPAARVTGTLHDVQHVVILMQENRSFDHYFGAMRGVRGFGDRFPIPLPGGKPVWRQSDARGREIQPWHIDTKTTSAQRIAGTPHTWPDAQAAWNHGKMDQWLPAKTERSMGHYVEADIPFQYALANAFTLCDAYHCSQLTGTNPNRLFLWTGSNNPAADRGGPAIVNTFDDSGPASEGYFWTTYPERLERAGVSWKLYQDMDDNFSDNPLEGFRQFRAAAPGSALAEKALKTWTLEDLASDVRSGKLPQVSWLVAPAKYSEHPGPSAPIWGADYTARVLDALTADPAVWARTVLIVNFDENDGFFDHVPPPAPPSLDAQRKPLGGSTVDLRGEHHFARSGPSHGTSADPAIYYDRPYGLGPRVPMYVISPWSRGGWINSQVFDHTSVIRFLEKRFGVSEPNISPWRRAVCGDLTSAFNFENPNHEPIPTLPYTGDADRIVAEQSKLPAPKPPATPSAARQEPGIKPSRALPYDLHVGERFDRDARSLRLNFGNSGRAAAVFHVYDLLDPEAIPRRYTVEPGRSLNGDWALRSGGARAYALQVFGPNGFFREFRGSLHGANPGATTIPDLRLRHRKLILALRNPGRKPLRLELADQYGLYAPRLERLGAGSLRYRPVRLDESCQWYDFVLIDANDPEYYRRIAGRVETGAHGVTDPGLI
>NZ_AP014940.1|WP_074863511.1|4232474_4233155_-|VWA-domain-containing-protein
MNQTAIPDVALVDNTEQRTPLVLVLDCSGSMTGAPMDQLNEGLKLLEEELKSDVIAAKRVRVLVVRYGGFDQAELAGDWCDAMDFTAPVLEAAGTTPTGRAIDLALGEVENEKQRFKAAGVAYTRPWLFLMSDGAPTDAWEAAAQRARDAETANKVAIFPIAVGQGDERIMSQFSSKGPGGVKRLQGLQFRELFLWLSASMQVVSQSRPGGAAQLPSTDTWSSVPT
>NZ_AP014940.1|WP_096379246.1|4231704_4232463_-|protein-phosphatase-2C-domain-containing-protein
MGWRIYAASAVGSSHLDKGIPCQDACAFHVSGDVLAAVVCDGAGSAAHSDIGARLIADGLARALGERLADEPQLLDAPRETFFEAAAEAVAQARASVVERAQADGRALGDYAATVVGYAGDAQRGWFLHIGDGIGVAEAADADEDAVVSLPANGEYANETWFVTGESWREQLRVLEVPAPTARLALMSDGAMPFAMTRGNAALYAPFIDPVARYLASVDEAEGSRALHGTLADPRTHGITSDDKTLLIALRA
>NZ_AP014940.1|WP_096379245.1|4230175_4231693_-|DNA-binding-protein
MSSLTTGSAIVIGSRRSRLGPLIKSGGAGSVYLLADDPHSVAKIYHARVDPPSYTDRIEAMLQLRPKLPDQYESGKRYVQIAWPDASVRDEQGRFVGFTMPALDVQSTNEVEQILQERQARAAGLPVGLGHKVTLAANLASVLAALHAQHHYVVDLKPVNLRFYRASLYIALLDCDGFSIQGRGGRFHAPQFTPDYLAPEYQIRALDEAGEETQDRFALAVVIFQLLNFGIHPYSGRPAYDRVPTDVPGRIRERCYAYSQRGNPMMAPNPVSGHALMPRGLRDLFDRAFGEEPARRPSSAEWSETLRAYAQPSRGLIVICDRNREHQHYAGEPCAACVRHDLLNATARKAASRPRPAPRAAAAIATARAQPQTLGWWRSARTAAKPTSAPASTAQPRLRVARPQPPPQWNPYYAPPQVPAAPAPSRSGWRARLPGRVRALAALAAPLAFGWLMQHAQGYYASLRAAAATPLDRWTNSILLTFLGMAFIAVCYVFLVAIPRRLSRS
>NZ_AP014940.1|WP_139174664.1|4229825_4230179_-|hypothetical-protein
MRWRRSNQRYRWNMHVPTRFALVKALVLAFFTILVLAPLTAWMFSLPMWAMDVFGYLLGSGQKEPGARWFGAGVVAAGVPCLAVVGWRAWRERDLDAGIMAAVAAVAWLVIAVAQLR
>NZ_AP014940.1|WP_074863503.1|4227935_4229366_+|hypothetical-protein
MSAYEPPYSHVGEASTPTLESPDEEVGPLSQFRHGAQDRRLLELARLDAGLAANADFDDKPWGLLYRALVDSIGLSPDDFQLAYPSAPWDWPCPQEGFIHAAQYDFCATAPQWSAIGAYVSSGDTVHQAYQQFLNTALAQTDYRSLRQHLNDADDALTTATNQYTLATTSAASAYAAQVEDNQPSFTQWLGSARGHGHQTRIVAAQVAMNRAQAHYAALVAQCQSPELGQAQRRCGDERFHVRLSDLNLIRMPKVPDWRLAQSSDDWVAQVEAGRGPAGVTLGFSNREAPYDFAQTWAGRRGRIRQLFWQVRINGRWERIDEFEFDNKLELSLDFQAVDTIAIRPGEWFDGDFARSMIDGPFMPGYSAFGGDSVETRGQPVFGERGFFGLIKSGLCVGYRPSFAIRTTTSTFRRFVDPFKAATALRIGPFVFEAEGGSLAAGWKADPATQTFTGATTSRSPLILGATVAELPNAAG
>NZ_AP014940.1|WP_096379244.1|4227066_4227450_-|hypothetical-protein
MNVQLVKWSLAAALLCAAAPALAGDPPACKTAPPEALVRDFNICVHAADPTKACLKYRLNARVYDNAQGLLPPLGGIGAQYWRASPALLGSPQGLVYNVAVGAKGKPVAKRYFTDDSFKSFCQVAGK
>NZ_AP014940.1|WP_083382326.1|4226548_4227025_-|hypothetical-protein
MPGRVRRSTAGDRPAVAAAIAAAVPLPRSIAMNLATRAVSALSLCLVAAAASAAAPPACGSLPPDIRDAKRDMSVCITMANPLADCGRMGLDVQIFSNNEGRLPAAGRGQLYWEGKIRAATGAAGQRRLVYLVTDGTKKVINARYYSPDHYVTFCSTN
>NZ_AP014940.1|WP_096383612.1|4226010_4226445_+|hypothetical-protein
MRKIELTVAHVGFGGNAGKGHYFYSFAPDVVTFQQPGGLWIEYAFEAQVPERFEIRNVLTSDAKDQIGPPVFDPSEKDPDYRRRVYLFNRNTESTLIFFTVLVRDRLSNYNDVELISCDPQVGNDPQIVPGAIKGEKPKKSKKG
>NZ_AP014940.1|WP_096379243.1|4222586_4225910_+|winged-helix-turn-helix-domain-containing-protein
MPQRVDRIKNLASVSQFRIGALLVQPDRLAIVRDGQSTALEPRMMEVLIALAERAGEVVSAEQLLIEIWRGTFYGDNPVHKTIAQLRRRLGDSSREPEFIETIRKRGYRLVAPVSFPDDYRSGLPRAAAWTQGSPYVGLRSFDQDHSGVFFGRSRATAELLATLREQIDNQRRFVLVAGASGCGKTSLLRAGVLPLLRQDGGFDGLHALASAYFDLGACRGGDLLARLAAALCAWSLDGRPVFLDGEAQWLEQQLRSAPEAVRARIDDAFARRTAPLAERAHLLLVVDHAEAAVAAPGIGDADRRDFGAALDALCSSPRVAAIAIARSDFYPALVEKVPGLAELKAGDGHIDLLTPRIGEIGQIIRAPAALAGLSFEEDPDSSLRLDDLLRDAAAEHPDSLPLLQHTLQALYERQGDGGLLRLATYRELGGLEGALAHRAEQVFAELPASAQASLERVLEALIVIRPDSDSVTGRRVPWSSLDGAAARELAEAFVRARLFVGELSGGEPGFGVAHEALLRQWPRAREWTRENRQLLQARERLQRAARRWAAEGRRNDHLLNPGRPLAEAREAARRLPDQLDADDLQFLHACERQQRRKQWLRAGAIGALCALALVATGLGLQAWQARREAEQRRDQAQTLVAFMLDDLAEQLRPLGNLKLLRSIANQSLSYLERMPETDMQPRELVSHARALRTVGEVLLDQGKFDDARVAFERAHAASARALDQEPQSLEALAESGTTAYWLGYHDYKQKKFDATRTHWQAYLHASERLVQRAPEDPRWRLELSYALNNLGTLAYSGQRLDEAGELFARSAAIKRQLLADKPDDSNLRYELVDSLSWLSSAQDARGLLAEAAQGYAAQTQMLRELVDSEPNADEWRRKLATSLLRSSVLALDRGQTEQAEREIAESVRMLKNLSEQQPDNQTWQRNLGHAYAHAGWVAAMAGARASALERLRAAQRTLAPIMQAKDRPPEWRLLDATVRLRLVQADPLASAEDADAAIADLQSLHEGAPADLPNRSSFARALAWRGERYAAAGETARARVDFQQVDRLLAQFAADTRDRVVLDAWSRAQVRLGARARAARQIAWLQRAGYRHPGFVALYETAPQPP
>NZ_AP014940.1|WP_096379248.1|4236152_4237067_-|siderophore-interacting-protein
MAQRNPFHLFDVSVRQRIELSPSMLRFVFAGESLAQARSFGPDQRIKIFFPNDAGELSVPRGEDWYARYRDQHPAQRAPMRTYTVRALRPQAAELDVDFVAHGDTGPASRWALQARPGDRVVLMAPHASQDDSGGVEWRPPADVRDVLLIADETALPAVAGILESLAAQPQPPKVRAYIEVPLRADAVDLHGPPDLRIHWLPRAERRDTDAADYGARLIEAIRAAQLAPAQTRTDAAEAELSEIDIDREILWEQAAVTASGFYAWIAGEAGAVMAIRRHLVGERGFAKSAISFMGYWRKGRVLE
>NZ_AP014940.1|WP_096379249.1|4237312_4238581_-|multidrug-effflux-MFS-transporter
MSHDAATVKPPIPIRRLALLLGGLAMFGPFSIDTIFPAFPAMGAELSADKLQMQQTISVYLVAYALMSIVHGPLSDAIGRRKVILGGLAVFTLASAACALADDLTSLLIFRAIQGLSAGVGLIVGRAVIRDLLHGDDAQRLMSQVMMIFGIAPAIAPVIGGWILGWSHWPAIFWFLVAFSVALWIAVALLLPETHPPQARLPLKPKRLLRDYFAICLNPRFQRLAAVGALNFGALFLYIASAPAFVLDILKLGERDFAWFFVPTIGGMVAGSFVSGRAAGKVSGDRLVDLGFACCALAIAVNLGYNLWTDVPQVPWAVVPMCIGAFGIALVFPIVTLSILDMYPHQRGSASSLQAFTGLVLNAVLAGVISPMLSDSALHLAVAASCLTAVAWLFWRWEAWVSRNPVSRVPEDAVVVEPQDSL
>NZ_AP014940.1|WP_096379250.1|4238577_4239033_-|VOC-family-protein
MAARPFRLLQLDHVVLRVRDSAAMAAFYCEVLGCSVERRQDEIGLIQLRAGDSLIDLVDVDGKIGRLGGAAPGEQGRNMDHLCLRADPFDRDAILAHLAAHGARVGEFGSRYGAEGEGPSQYLYDPEGNMVELKGPPDAPLDRAPADHAAR
>NZ_AP014940.1|WP_096379251.1|4239555_4242414_+|aminomethyl-transferring-glycine-dehydrogenase
MTHSTLRDLEHHDAFIERHIGPNDAEIGHMLGQVGYASLEALTDAIVPGSIKSPQPLALPQAISEVEALAKIRAIASKNQVLRSFIGRGYYGTHTPNVILRNILENPAWYTAYTPYQAEISQGRMEALINFQTMVADLTGMEIANASLLDEATAAAEAMTLAKRSAKSKSNTFFVSKNVHPQTLEVLRTRAEPLEIALQIGDDADAAGADVFGALLQYPDTFGGLGDYQAVADALHARGAILAVASDLLALVLLKSPGEFGADIVVGNTQRFGVPFGFGGPHAGFMACRDAYKRSMPGRLIGVSVDSDGKPAYRLTLQTREQHIRREKATSNICTAQVLLAVMASMYAVYHGPDGLTRIALRVHRQAAILAAALRQAGVKVADGFFDTLRIDGVDAAAIHAKARAAGINLREIDAASVGISLDETVARADLTALAGVFGAALDIDALDAATADAIPAALRRTSAFLQHPVFNTHHSEHELLRYMRSLADKDLAMDRTMIPLGSCTMKLNATAEMIPVTWPEFGNIHPLAPAEQAVGYKQLIDELEAMLVECTGYDAVSLQPNSGAQGEYAGLLAIRAYHRSRGEAHRDICLIPDSAHGTNPASAQMCGMTVVVTKTDANGNVDVEDIRRNAEKYSDRLAAIMMTYPSTHGVFEEEVVEICEIIHQHGGQVYTDGANMNALVGVAKPGKWGSDVSHLNLHKTFCIPHGGGGPGVGPCAVKSHLAPFLPKTVDGEGAVGMVSAASFGSASILPISWMYVTLMGTAGLRKATQVALLNANYIAKRLAPHYETLYTGRNGLVAHECILDLRPLKDATGISAEDVAKRLIDFGFHAPTLSFPVAGTLMVEPTESESQHELDRFIDAMIQIREEIRAVEDGRLDREDNPLKHAPHTATQVSGSEWTRAYPRELAAFPLPSLKLQKYWPPVSRVDNVYGDKNVMCACIPIDAYKEEVEA
>NZ_AP014940.1|WP_096379252.1|4242693_4243164_-|hypothetical-protein
MSYQDAPDAGATLQVSETLEAIRRRPERFLPADEPLALAIVSLLLETALRQGVAPLAVRAGEGFRAIGADRDWLWREQGGEPYVFDRLVPLPGPVQNSFRGEILLTAFAPFWAAVTQGQVVYRSSARFDDARVLQAAAGMGAFVVVVAETAQASTL
>NZ_AP014940.1|WP_096379253.1|4243421_4244438_+|GGDEF-domain-containing-protein
MNMQEPKLQAFSERLLKVIETQTEIARLGLDLGGVMDLVAHRAQGLTGAVGSVVELAEGEDMVYRAAAGIAESSLGMRLRRDASLSGHCVAEGRPLNCRDSETDERVDRAACRAVGLRSMIVVPLKHHDTVVGVLKVMSREPTAFDDDDLRVLDMMSGLIAAAMYHAAKYETNELFYQATHDALTGLPNRALFYDRLRHNLAQAHRESRRVGILNLDMDGLKPVNDQLGHRAGDAAIREFAARMKLSARTGDTVARVGGDEFAVILPRIEHREGAFAQAQRLAQALRFGFEFEQRPIALDASIGCAIYPDDGEELGELLEKADQAMYDVKRSKKTSRE
>NZ_AP014940.1|WP_096379254.1|4245017_4245812_+|hypothetical-protein
MKLAIRFAAILLGASLCTSAPAQSAWEVHDKHANDHLAEIEKRIGSDDNGNVNANLNKLAKIGNAKKSGDDAKEPEEKLDAKDPSVQVKKSMDERCPNPGGSAGAAQQQWQLCQEIVKTELAQYTYSMTMYELSRKRQERLQEIEQERGNLSVGEQGKLQDNSNKLLALLSRMEVDRQQSRAYMDAYTARLTYLRAVRDMLSNEILSGKDSGGPGGGGNLMPKKIVAAVAGMAAMKTALKAAESKRLCSPWIPLQDGENCTPRP
>NZ_AP014940.1|WP_096379255.1|4245827_4246961_+|type-IV-secretion-system-protein
MSLSWTTAAALAQLFDGLSAQFDSLGQWVFFKLIFDHLDHEIVVFRDNMMHRMTSVIGAIAATLATMWIVTQGYRIMTGQSREPMMSLLVSSLRVFLILTAATSATFVTGSIHTTLSHDLPRAIGNIVTDSDKDPAEVIDSGLTNMQLAMAAIDALPALDSPAIKDDKDRALLMTGIGVAGPAVIGGALLMMYKFAIALFIGFSPLFILSLMFERTKSMFARWLQYGLGTMFSMAVLSFTVTVAMKMVAAVAASFATQYLTMMALGAGDSPGVNTMALQQGGLGIFLTVLILSVPPMASSFFQGALGNFMHYSAFGANTAPTKPEAPGNSAPPQQPRLPDQNQGGRHDSQQKLPSYLPPQPQPQSPPDSASGEIRKR
>NZ_AP014940.1|WP_172437285.1|4246963_4247467_+|DUF4189-domain-containing-protein
MKTPIAKARMAALAAGLLFVSQTYACPPGTVPQQGIGWQGCAPAPGTSSSSATTDTSAAWADRWGAIAIDMTPGGVGIGSSSGMNRKRNAEKLALSACKRKGGARCEIEITYYNQCAAIVLGSQAFNSSSAASLEEAKRRGIDKCTQAGDKECTVYFSECSFPERIR
>NZ_AP014940.1|WP_096383615.1|4247522_4248101_+|type-IV-secretion-system-protein
MFERTKSMFARWLQYGLGTMFSMAVLSFTVTVAMKMVAAVAANFATQYLTMMALGAGDSPGVNTMALQQGGLGIFLTVLILSVPPMASSFFQGALGNFVPQSIFGANAAASRQESPGGHQSNRYQQGAPGGSANQQRMEQNQHTNQSIANASLGSGKRASEQTDVHAKDRSSPTDPPKDKIKNTENRRPEDS

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Crispr_ID: NZ_AP014940_11

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_11

4477366-4477472

Orphan

Consensus_repeat	Method
CCGTCATTCCGGCGAAAGCCAGAATCCA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP014940_11

>merge|NZ_AP014940|11|4477366-4477472|CRISPRCasFinder
CCGTCATTCCGGCGAAAGCCAGAATCCAAACGCAGCGACTTGGCTCTGCCGTGATTTCCCGAAGCCAGCAACCCCCACGCCGTCATTCCGGCGAAAGCCGGAATCCA

>NZ_AP014940|11|11|4477366-4477472|CRISPRCasFinder
CCGTCATTCCGGCGAAAGCCAGAATCCA	AACGCAGCGACTTGGCTCTGCCGTGATTTCCCGAAGCCAGCAACCCCCACG
CCGTCATTCCGGCGAAAGCCGGAATCCA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_096379472.1\|4474713_4476165_-\|bifunctional-2-methylcitrate-dehydratase/aconitate-hydratase	unknown	unknown	gnl\|CDD\|181845
NZ_AP014940.1\|WP_096383659.1\|4470851_4471367_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_172437296.1\|4490785_4493080_+\|NADPH-dependent-2,4-dienoyl-CoA-reductase	unknown	unknown	gnl\|CDD\|239240
NZ_AP014940.1\|WP_096379474.1\|4476370_4477162_+\|dioxygenase	unknown	unknown	gnl\|CDD\|153375
NZ_AP014940.1\|WP_096379480.1\|4482813_4484877_-\|elongation-factor-G	unknown	unknown	gnl\|CDD\|237186
NZ_AP014940.1\|WP_096379469.1\|4471850_4472930_-\|OmpA-family-protein	unknown	unknown	gnl\|CDD\|143586
NZ_AP014940.1\|WP_096379479.1\|4481729_4482746_+\|zinc-binding-alcohol-dehydrogenase-family-protein	unknown	unknown	gnl\|CDD\|176214
NZ_AP014940.1\|WP_096379485.1\|4494241_4494850_+\|glutathione-S-transferase-N-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|182533
NZ_AP014940.1\|WP_096379463.1\|4467554_4468088_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096379487.1\|4495043_4495553_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096379471.1\|4473363_4474443_-\|OmpA-family-protein	unknown	unknown	gnl\|CDD\|143586
NZ_AP014940.1\|WP_096379476.1\|4477971_4478886_-\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176114
NZ_AP014940.1\|WP_096379467.1\|4468774_4469302_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096379477.1\|4480356_4481601_+\|SGNH/GDSL-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|238868
NZ_AP014940.1\|WP_172437295.1\|4485460_4488268_-\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|274008
NZ_AP014940.1\|WP_172437294.1\|4478989_4480255_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|225371
NZ_AP014940.1\|WP_096379465.1\|4468170_4468695_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096379461.1\|4466902_4467433_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_074863946.1\|4493684_4494143_+\|cell-wall-hydrolase	unknown	unknown	gnl\|CDD\|377847
NZ_AP014940.1\|WP_096383657.1\|4469737_4470439_-\|rRNA-pseudouridine-synthase	unknown	unknown	gnl\|CDD\|224108

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_096379472.1\|4474713_4476165_-\|bifunctional-2-methylcitrate-dehydratase/aconitate-hydratase	gnl\|CDD\|181845	PRK09425, prpD, bifunctional 2-methylcitrate dehydratase/aconitate hydratase.	0
NZ_AP014940.1\|WP_096379476.1\|4477971_4478886_-\|LysR-family-transcriptional-regulator	gnl\|CDD\|176114	cd08422, PBP2_CrgA_like, The C-terminal substrate binding domain of LysR-type transcriptional regulator CrgA and its related homologs, contains the type 2 periplasmic binding domain. This CD includes the substrate binding domain of LysR-type transcriptional regulator (LTTR) CrgA and its related homologs. The LTTRs are acting as both auto-repressors and activators of target promoters, controlling operons involved in a wide variety of cellular processes such as amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to name a few. In contrast to the tetrameric form of other LTTRs, CrgA from Neisseria meningitides assembles into an octameric ring, which can bind up to four 63-bp DNA oligonucleotides. Phylogenetic cluster analysis further showed that the CrgA-like regulators form a subclass of the LTTRs that function as octamers. The CrgA is an auto-repressor of its own gene and activates the expression of the mdaB gene which coding for an NADPH-quinone reductase and that its action is increased by MBL (alpha-methylene-gamma-butyrolactone), an inducer of NADPH-quinone oxidoreductase. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	1.00489e-83
NZ_AP014940.1\|WP_096379474.1\|4476370_4477162_+\|dioxygenase	gnl\|CDD\|153375	cd07363, 45_DOPA_Dioxygenase, The Class III extradiol dioxygenase, 4,5-DOPA Dioxygenase, catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine. This subfamily is composed of plant 4,5-DOPA Dioxygenase, the uncharacterized Escherichia coli protein Jw3007, and similar proteins. 4,5-DOPA Dioxygenase catalyzes the incorporation of both atoms of molecular oxygen into 4,5-dihydroxy-phenylalanine (4,5-DOPA). The reaction results in the opening of the cyclic ring between carbons 4 and 5 and producing an unstable seco-DOPA that rearranges to betalamic acid. 4,5-DOPA Dioxygenase is a key enzyme in the biosynthetic pathway of the plant pigment betalain. Homologs of DODA are present not only in betalain-producing plants but also in bacteria and archaea. This enzyme is a member of the class III extradiol dioxygenase family, a group of enzymes which use a non-heme Fe(II) to cleave aromatic rings between a hydroxylated carbon and an adjacent non-hydroxylated carbon.	1.89783e-126
NZ_AP014940.1\|WP_096379480.1\|4482813_4484877_-\|elongation-factor-G	gnl\|CDD\|237186	PRK12740, PRK12740, elongation factor G-like protein EF-G2.	0
NZ_AP014940.1\|WP_096379469.1\|4471850_4472930_-\|OmpA-family-protein	gnl\|CDD\|143586	cd07185, OmpA_C-like, Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA. OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.	2.52183e-36
NZ_AP014940.1\|WP_096379479.1\|4481729_4482746_+\|zinc-binding-alcohol-dehydrogenase-family-protein	gnl\|CDD\|176214	cd08252, AL_MDR, Arginate lyase and other MDR family members. This group contains a structure identified as an arginate lyase. Other members are identified quinone reductases, alginate lyases, and other proteins related to the zinc-dependent dehydrogenases/reductases. QOR catalyzes the conversion of a quinone and NAD(P)H to a hydroquinone and NAD(P+. Quinones are cyclic diones derived from aromatic compounds. Membrane bound QOR acts in the respiratory chains of bacteria and mitochondria, while soluble QOR acts to protect from toxic quinones (e.g. DT-diaphorase) or as a soluble eye-lens protein in some vertebrates (e.g. zeta-crystalin). QOR reduces quinones through a semi-quinone intermediate via a NAD(P)H-dependent single electron transfer. QOR is a member of the medium chain dehydrogenase/reductase family, but lacks the zinc-binding sites of the prototypical alcohol dehydrogenases of this group. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.	0
NZ_AP014940.1\|WP_096379485.1\|4494241_4494850_+\|glutathione-S-transferase-N-terminal-domain-containing-protein	gnl\|CDD\|182533	PRK10542, PRK10542, glutathionine S-transferase; Provisional.	6.72718e-53
NZ_AP014940.1\|WP_172437296.1\|4490785_4493080_+\|NADPH-dependent-2,4-dienoyl-CoA-reductase	gnl\|CDD\|239240	cd02930, DCR_FMN, 2,4-dienoyl-CoA reductase (DCR) FMN-binding domain. DCR in E. coli is an iron-sulfur flavoenzyme which contains FMN, FAD, and a 4Fe-4S cluster. It is also a monomer, unlike that of its eukaryotic counterparts which form homotetramers and lack the flavin and iron-sulfur cofactors. Metabolism of unsaturated fatty acids requires auxiliary enzymes in addition to those used in b-oxidation. After a given number of cycles through the b-oxidation pathway, those unsaturated fatty acyl-CoAs with double bonds at even-numbered carbon positions contain 2-trans, 4-cis double bonds that can not be modified by enoyl-CoA hydratase. DCR utilizes NADPH to remove the C4-C5 double bond. DCR can catalyze the reduction of both natural fatty acids with cis double bonds, as well as substrates containing trans double bonds. The reaction is initiated by hybrid transfer from NADPH to FAD, which in turn transfers electrons, one at a time, to FMN via the 4Fe-4S cluster. The fully reduced FMN provides a hydrid ion to the C5 atom of substrate, and Tyr and His are proposed to form a catalytic dyad that protonates the C4 atom of the substrate and completes the reaction.	0
NZ_AP014940.1\|WP_096383657.1\|4469737_4470439_-\|rRNA-pseudouridine-synthase	gnl\|CDD\|224108	COG1187, RsuA, 16S rRNA uridine-516 pseudouridylate synthase and related pseudouridylate synthases [Translation, ribosomal structure and biogenesis].	1.22519e-79
NZ_AP014940.1\|WP_096379477.1\|4480356_4481601_+\|SGNH/GDSL-hydrolase-family-protein	gnl\|CDD\|238868	cd01830, XynE_like, SGNH_hydrolase subfamily, similar to the putative arylesterase/acylhydrolase from the rumen anaerobe Prevotella bryantii XynE. The P. bryantii XynE gene is located in a xylanase gene cluster. SGNH hydrolases are a diverse family of lipases and esterases. The tertiary fold of the enzyme is substantially different from that of the alpha/beta hydrolase family and unique among all known hydrolases; its active site closely resembles the Ser-His-Asp(Glu) triad found in other serine hydrolases.	4.82244e-94
NZ_AP014940.1\|WP_172437295.1\|4485460_4488268_-\|AAA-family-ATPase	gnl\|CDD\|274008	TIGR02168, Chromosome_partition_protein_Smc, chromosome segregation protein SMC, common bacterial type. SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins].	2.42696e-21
NZ_AP014940.1\|WP_172437294.1\|4478989_4480255_+\|MFS-transporter	gnl\|CDD\|225371	COG2814, AraJ, Arabinose efflux permease [Carbohydrate transport and metabolism].	7.6766e-98
NZ_AP014940.1\|WP_074863946.1\|4493684_4494143_+\|cell-wall-hydrolase	gnl\|CDD\|377847	pfam07486, Hydrolase_2, Cell Wall Hydrolase. These enzymes have been implicated in cell wall hydrolysis, most extensively in Bacillus subtilis. For instance Bacillus subtilis steB is expressed during sporulation as an inactive form and then deposited on the cell outer cortex. During germination the the enzyme is activated and hydrolyzes the cortex. A similar role is carried out by the partially redundant Bacillus subtilis CwlJ. It is not clear whether these enzymes are amidases or peptidases.	4.10368e-22
NZ_AP014940.1\|WP_096379471.1\|4473363_4474443_-\|OmpA-family-protein	gnl\|CDD\|143586	cd07185, OmpA_C-like, Peptidoglycan binding domains similar to the C-terminal domain of outer-membrane protein OmpA. OmpA-like domains (named after the C-terminal domain of Escherichia coli OmpA protein) have been shown to non-covalently associate with peptidoglycan, a network of glycan chains composed of disaccharides, which are crosslinked via short peptide bridges. Well-studied members of this family include the Escherichia coli outer membrane protein OmpA, the Escherichia coli lipoprotein PAL, Neisseria meningitdis RmpM, which interact with the outer membrane, as well as the Escherichia coli motor protein MotB, and the Vibrio flagellar motor proteins PomB and MotY, which interact with the inner membrane.	3.84079e-36

>NZ_AP014940.1|WP_096379474.1|4476370_4477162_+|dioxygenase
MDIPTRLPTLFLSHGSPMLALEDSPAGRFLDALGQQLPWPRAIVIASAHFMTDRPMLGGHAQPHTVHDFGGFPQPLYQIQYPAPGQPRLAEQVLARLADAGLNPKLRDNHGLDHGVWVPLRRMYPQADIPVVPLSVQPYGTAAQHYAVGQALAALRDEGVLVIGSGGFVHNLGDLDWGQREAPMPDWAAQFAGWMHAALAAGDREALLDWQARAPHARRAHPTVEHLMPLFVALGAAGAEPTARTIHRSHEMGSLALDAFAFD
>NZ_AP014940.1|WP_096379472.1|4474713_4476165_-|bifunctional-2-methylcitrate-dehydratase/aconitate-hydratase
MSHFDIRSTVRPDPDKPMADIADYVADYKIDSKEAFDTARYMLLDSLACAALAMDHKECLKHLGPLVPGGEMKGGARVPFTSYELDPVQAAYNIGVQIRWLDFNDTWLAAEWGHPSDNLGAILGVADYLGRKAEAEGGKAMTVRDVLGHAIKAHEIQGGYALKNSFNRVGLDHVILVRLASTAVATQMFGGGKEEIITAVSHSWIDNGVLRTYRHAPNTGPRKSWAAGDACRRAVTHALNANKGVVGYPSALSVKTWGFYDISFKGKQFEFERPFGSYVMENVLFKISFPAEFHAQTAVECAMKLHDQVKDKLDQIERVELETQEAGVRIIDKTGPLANYADRDHCLQYMVAVPLIFGRLTADDYVDAVAADPRIDALRDKMVVKENEQFTKDYFDPDKRYIGNSVQVFFKDGTSTDKVSIDFPIGHRKRRAEGIPVLMAKFEAAIRAKLPAAQAERLLALANDPAALEALPVTEFMSLFVRQ
>NZ_AP014940.1|WP_096379471.1|4473363_4474443_-|OmpA-family-protein
MNKKLLCAALLGGLSLAQVASAQDFDDRWYLTGAAGMNIQDNDRGTRNAPFGAIGLGKFLNKNWSLDGELNYQNPKFDANQDANWSQYGISLDLRRHFVTDGRNWNPYILAGIGYQRSEEEYFIPSPLSPAKRKDGNFAAKVGVGIQGDLGRVGIRTELAYRADFDDQSVNASKEDWFGDVLASVGIVVPLGPEPSAPVVAPPPVQPGCADKDDDGDGVNNCDDKCPNSQAGQTIGPDGCPVPVTIDLKGVNFDFDKATLRPDAIAILNEATEILKRYPELKVEVAGHTDLCGKDAYNQKLSERRAKAAYDYLTSNGVDAGRLVGPIGYGESRPLEQTPQTLPGCKSEKNRRTELNVQN
>NZ_AP014940.1|WP_096379469.1|4471850_4472930_-|OmpA-family-protein
MKIRMLSTALLAGLAFSQVASAQDFDDRWYLTGAAGMNIQDNDRGTRNAPFGAIGLGKFLNKNWSLDGELNYQNPKFDANQDANWSQYGISLDLRRHFVTDGRNWNPYILAGIGYQRSEEEYFIPSPLSPGNRKDGNFAAKVGVGIQGDLGRVGIRTELAYRADFDDQSVNASKEDWFGDVLASVGIVVPLGPEPVAAVAPAPVVEQGCADKDDDGDGVNNCDDKCPNSQAGQTIGPDGCPVPVSIDLKGVNFDFDKATLRPDAVAILNEAAEILKRNPSLRVEVAGHTDLCGKDAYNQKLSERRAKAVYDFLTSNGVDAGRLAGPVGYGESRPLEQTPQTLPGCKSEKNRRTELNAQN
>NZ_AP014940.1|WP_096383659.1|4470851_4471367_-|hypothetical-protein
MLAATSLILIAASAQAQTSAANCAALTASRAQPVQPTLIAPVAPELVAPSHQLGAPTGVLSQALDEALSVDQVLLRMKLDACTVAKATPASTGMPSANDPAAYKPQTEFDNTPWRFDMSQGGKRMTADEFAAWMKAKGVRVAKGAPGAAAAAPAPVAEAEPPKAEEGKKKK
>NZ_AP014940.1|WP_096383657.1|4469737_4470439_-|rRNA-pseudouridine-synthase
MLSKQGVCSRSEAARWIAQGRVSVDGRIVRDPEFAIVQGRQRIRVDGADLGDARRFYLMLNKPRGLVTTAHDECGRDTVYRCLDGAELDGAPLPWLAPVGRLDKASEGLLLFCNDPQWAARITDPELGPDKTYRVQVDAIPDEAQLRALEAGVDDDGERLRAKSVRLLRSGEKNAWLEIVLDEGRNRQIRRLLAAFGLETLRLVRVAIGELPLGELPKGQWRVLDEEDLRKLR
>NZ_AP014940.1|WP_096379467.1|4468774_4469302_-|hypothetical-protein
MSLMSIAVPARQRAGAFFAALRAFALTAALLFSAGVQADPVRAEQHLQVVRSQRAVLDTHMLYVNMYLDAGNVQAAQVSMQMAFAQTMKIVASMSNLSYELRQSRDAGQYTNLQELERAIQFCDSARQRMQLIKTYLLNLQLEQPPSEITRTLLRMKFQEYEMNMRNLELAMSQA
>NZ_AP014940.1|WP_096379465.1|4468170_4468695_-|hypothetical-protein
MFQTFAAPTRRKHAGALISSLRAAALATVLLFSVGAQADPVVAAQIMQKIHVDRQVFDVHMQQVNWYLDFSPNQAAISLVTARVDTVKIGQRLKQLHQENLASRDAGQYNNLQALERAIQHGNQARQRIQSVEIYLLTLEMERPPTAFTRQLLNIQIELFNTSMRELEQAMAEA
>NZ_AP014940.1|WP_096379463.1|4467554_4468088_-|hypothetical-protein
MFETTLAVRRGAYKRASAPIAALRAFALIAALLFCTAAQADPVETERLMQQVRDERSALETNLQEAYAYMDSGQTAQAVASFALARANTTAIGLSLAEVLVEVRKSREQGQYTDAQALERARVRCGRVKETAGFIDASLVPMMQQPGAFGRALIDAQRAQFDRQFAPLELDLALSQA
>NZ_AP014940.1|WP_096379461.1|4466902_4467433_-|hypothetical-protein
MSHTIALSAARRRASAPFAALRAVALTLLMLFAHGASADPAAADQRLAITKQNFTALKQSYTIAKMQLQMGQPTPAGVSFTLAKAQAQQMVANLVTLRNDNQHTLDNGLYLNGAAQQQAVNYTDVAKSLAQQLQTRLMILSIQPTSQLDLVLADQSLTQLTLKMTQLEQAMIAAQQ
>NZ_AP014940.1|WP_096379476.1|4477971_4478886_-|LysR-family-transcriptional-regulator
MDRIADLNLFLRVLDLGSISAAARSLDLSVAVASQRLKRLERDLGVRLLHRTTRQLHATAEGQALAERGRALIEELEGLTDDLRRAGSEPAGLVRVTTSASFGRMYLSPLLPEFQRRYPLVRLSVNLSDENLDLVAAGMDLAIRIGALGDSSLVARKLADNRRVLACSPDYLRQHTAPRVPQDLAEHECLVLVGAHGRLEDWRVLDAAGAETVVRVNGRLESNFGEVLRDAALAGLGIAHFSVWHVHEDLRAGRLVQVLPEHRLPETAIHAVMPQRRYVPLRVRAFIDFVAESFGDVPPWERGG
>NZ_AP014940.1|WP_172437294.1|4478989_4480255_+|MFS-transporter
MHAPSSSADLPAPAAGGRARLPVALYALTVGAFGIGTTEFVIMGLLLQVAADLQVGLAAAGLLISGYALGVFVGAPVLTIATGRMPRKAVLVALMLIFTLGNIVCAIAPNYTVLMIARVITSLAHGTFFGVGAVVATALVPQDRKASAISIMFTGLTVATLLGVPAGAWLGLQFGWRSTFWAVAAIGVIATVVIAALVPRDRAKPEPVALRRELSAVLHPQVLLGLLMTVLGFAGVFTVYTFIQPILTSISGFSEATVSPILLVFGGGMILGNLIGGRFADKRLATALIATLIALAAVLGVMTFALHDKIATVAFVGLLGVAAFATVPPLQLWVLQKTDPAGQNLASSLNIGAFNLGNALGAWLGGAVIEHGPGLGAVTWVAALVTLSGLVLAVVAARLDAKGRVVTPHTAGPATAAACAG
>NZ_AP014940.1|WP_096379477.1|4480356_4481601_+|SGNH/GDSL-hydrolase-family-protein
MNPLRKTFFAAALALSLLAPAHAGEATQWTSTWIASPQATWGADFVLPNNAPDRIGDQTIRQVARISVGGERVRIALSNAYGREPVTIGAAHIARSLGGSRIDAGSDRALTFGGRSSVTLLPGAPVLSDPVELSAPALAEVAVSLYVPQDTALRSFHWEGLRDAYLAQGDRSAQAALDGAATIPSRPYLSGIYVESARRARSVVAFGDSITDGAASTPNRNRRWPDALAERLAPRGIAVLNAGISGAQVLNDGMGVNALARFERDVLAQRPDSVVVLMGINDIGWPGSTFEPAREAMSAQRLIDGYRQLIARARQAGVRIVGATLTPFEDALPDAPVKHYFNPDKERVRQQVNAWIRSSGEFDAVADFDALLRDPAHPTRMRAAFDSGDRLHPGDAGYRAMADSLDEAVLFGAH
>NZ_AP014940.1|WP_096379479.1|4481729_4482746_+|zinc-binding-alcohol-dehydrogenase-family-protein
MKAVALTRYLPIDDPQSLTDVELPAPVASGHDLLVRVEAVSVNPVDTKVRSPKPQVEAQPRVLGYDAAGTVEAVGENVTRFKVGDKVYYSGDITRPGSNSELQLVDERIVGAAPKSLSAAEAAALPLTAITAWELLFQRMPFDSENGGRGKTLLVIAGAGGVGSIAIQIAKRAGFSVIATASRAETVAWCRKMGADHVVDHRQPLTPQLQALGIEQVDAAINLADTARYWDELGELLAPQGSVGLIVEPAGALKIGDPYKLKCIGIHWEMMFARPKFRTPDMIEQGRILDRVAQLIDAGELQGTHTETLGRIDAATLREAHRRLESGATIGKLVLAGW
>NZ_AP014940.1|WP_096379480.1|4482813_4484877_-|elongation-factor-G
MNTPLTSNTPIRRWRNLGIIAHVDAGKTTLTERLLWKTGAIHRTGEVHDGAATTDFDPIERRRGITIGAAAVQARWTPHDGAEHRLTVIDTPGHIDFAIEVERSLRVLDGAVAVFSGVDGVQPQSETVWRQARRHGVPLIAFVNKMDRVGASLERTLAQMREKLDAVPWALGETVGAESELSGWIDYVARESVSWDDAGNLSRQAWTSEEAARFEPARQRLIEAVADHDDALAEAFLDARAIDAALLKAALRRATLAGAGTPVLAGSAFKNKGVEPLLDAIVDYLPSPLDRPAVRAQSERGEVELAPDANGPLAGLVFKIVQQEHGAQTFVRLYSGTLRVGDTVWASRREKALRVGRLQVVQADRGQDVDVAYAGEIVAVVGWKDAISGETLSDAGERLALDSIQAQPAVLSWRLTAAKSSDLIRLGQGLASLAQQDPSFRVGTDADTGETLVWGMGELHLEVMVDRLRELWNVDVRTGSPRVAYQETPSRAVRGVEGKLSKQTGGSGQFARVVIDVTPREDGQFEFVDRTVGGVVPRNFVGATEKGLRAALAEGPQGFPVVGLTVALTDGETHAVDSSEMAFQRAAAEALKAALAQTGTTLLEPVMALVVDTPAANVGDVVGDLQRRSGRVLSIEDKGGRSDVTARAPLAQLSGYTTTLRSLSQGRASASMVFDGYEVARGLPKAA
>NZ_AP014940.1|WP_172437295.1|4485460_4488268_-|AAA-family-ATPase
MFEFRSLEVVHWDYWQRFQLPLDASIVTVVGPNGSGKTTLLDALRTLLAIEDRDTARDYKTYLRHNGKPYAWLRAVVSNSPDRRGGRPFFPIKDDQVTLACRIRKRGGDWSRDYQIVGGDVPVETLEQGGEWLGVRDYRVRLAGAGLTRAICRVLTLEQGATDKLCQYSPRELLQLIFDVFEDKAVLDDYQRARTEQFDVEKELQQLGQDLAGLHLRLESAKADVRSFEEYNALRGQRQRLESEIAPKVELADQRNAIEGAKPRLTGLRRALRERERMLDEMQREDQIASGGRETLVEAMREARRQVGASEQAFTQARDAARDAEMLVKRRDELAKLQAQRGDLDVDSLSAAVENGRRRQAELKLEAERDRKRAGELAAQLAALSGGGRIVEPFERDFRASLLKSNIDHRVLTELVEIVDPQWSVAVEAVLAPYRHLLVLENPKDARAAWQLGESQQYRHFIVAERAPVPKPSAGSLLEVVRFSADPPAWLPRQLDRIRRVTDIEHGSRLPAQQDWITQKGYLRESRGGRHIGGGQQHFGSGARQSQLAELRAEQETIVQRAQAREAELQELSQRVDADQSRLLGLDATQELVTRAGEFAAAAERLPELAETAAAAAAALAEARARIDAAGDQDKAEGIAAAKRQGQIDALARELRERSQQINGERQSLIQRIVDYRRKRALMPESWRTAAALHAAREEYESASAVRREMERIDDRLERGGFVTDESCVPMRDKIGADHDELASSIMRREGHLDRAKRLTEEARGAYINVLRATVRRYKKNLAALGELAGIGVDADMPELANNDVALAQAGLSVRFDFDRKGWIGLDDGEASGGQQVMKSLLLLVALLRDEDQPGGFVFIDEPFAHLDVFNIEKVGRFLRATDAQYILTTPITHNLNVFDPSDLVLTTSKRRGGNTWAEPVAVLKRQVEAKGKAA
>NZ_AP014940.1|WP_172437296.1|4490785_4493080_+|NADPH-dependent-2,4-dienoyl-CoA-reductase
MREGVTTVALAAPACLSSRGLHRPRCESGPQLRRNRARARRRRGFPLEFQGFSRHRAQSIRQRIQPAMTTAAPTAPASAPAADTGAHPLYPHLFAPLDLGFCTLPNRVLMGSMHTGLEDKAADFPKLAAYFAERAAGGVGLIVTGGFAPNIVGWLKPFGGKLSWPWEAAKHKQVTGAVHAHGGRICMQILHAGRYGYHPLQVAPSKLKAPINPFTPRALSAGGVERQIKAFVNSARLAREAGYDGVEVMGSEGYLLNQFTVPRTNKRRDGWGGEAAQRYRFSVEIVRRIREACGPDFIIVYRLSMIDLVDEGSTWSEVIAQARAIEAAGATLINTGIGWHEARVPTIATSVPRGAFTGITGRLKEEVRLPLVTTNRINMPDVAERILAEGDADIVSMARPLLADPEWVNKARHRRAADINTCIGCNQACLDHVFENKHASCLVNPRACAETELNYRPTAAPKRVAVVGAGPAGMACATVAAERGHHVTLFDRAARIGGQFNLAKRIPGKEEFYETLRYFAGRIEQTGVELRLNTDADAAALAGFDEVVLATGIRPRRVDFPGSDHAKVVSYLDVLQGRVVPGARVAIVGAGGIGFDVAEFLVHDGPHSGDDAPHYPDPAQWRAEWGVDLDYADNRGGLAAPQPTPPARQVWLLQRSAGKPGAKLGKTTGWIHRATLKAKQVRMLGGVEYVGVDDEGFHIRIDGSEQTLPVDQVVICAGQEPYKPLAEALAGSGRPVHVIGGADVAAELDAKRAIAQASRLAAQL
>NZ_AP014940.1|WP_074863946.1|4493684_4494143_+|cell-wall-hydrolase
MKLAWILWLASVLPPQTADSLCLSTTVYLEARDQSQRGQQAVAEVALRRRDSGLWGDTVCEVVTANKQFAPTLVSPGTRLSNSEAWAESVNVALAAERNWALPAGQRKEIVPGASHFAAHAIASPSWRNAYQVATIGDHTFYKVQALKPRRG
>NZ_AP014940.1|WP_096379485.1|4494241_4494850_+|glutathione-S-transferase-N-terminal-domain-containing-protein
MKLYSKPGACSTADHIALQWAGGKFEVEIVDKDTMKAPAFLAINPAGAVPAVVDGEFVLTQNSAIMGYIADTFPQAQLAGDGSAQQRAEAARWLAYCNSDIHPAFVPIFSPGKFHPDPAQADVVRQTARERLRAMYAAADQRLADRQWLAGFRSYADPYLYITLRWAAATKVDLSGYEHLAAFKQRMEADSGVQAALKAEGL
>NZ_AP014940.1|WP_096379487.1|4495043_4495553_-|hypothetical-protein
MRDSDVPVKTNEGRDEIEHRTRKLPPMLRSILLIVDGERSARHLRELAVSLHGPADALEQLEGMGLIASSAAVAASLAAQAPVRAAAASVPADAAASPPAQRYQALYSLMSEAVRDHLGLRGYFLQLKIERCSNSDELAAVLPELSAALAKARKDEVAAQIEAQFAAGA

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Crispr_ID: NZ_AP014940_12

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_12

4931113-4931219

Orphan

Consensus_repeat	Method
TGGATTCCGGCTTTCGCCGGAATGACG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP014940_12

>merge|NZ_AP014940|12|4931113-4931219|CRISPRCasFinder
TGGATTCCGGCTTTCGCCGGAATGACGAGCTGGGGGTTGTGAGGCTTCGGGAGGTTACGGCGGAGCTGCGTCGCTTCGGTTGGATTCCGGCTTTCGCCGGAATGACG

>NZ_AP014940|12|12|4931113-4931219|CRISPRCasFinder
TGGATTCCGGCTTTCGCCGGAATGACG	AGCTGGGGGTTGTGAGGCTTCGGGAGGTTACGGCGGAGCTGCGTCGCTTCGGT
TGGATTCCGGCTTTCGCCGGAATGACG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_096380035.1\|4939969_4940686_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|182993
NZ_AP014940.1\|WP_096379967.1\|4912709_4913363_-\|HAD-hydrolase-like-protein	unknown	unknown	gnl\|CDD\|319798
NZ_AP014940.1\|WP_096379970.1\|4913366_4914542_-\|phosphoglycerate-kinase	unknown	unknown	gnl\|CDD\|234613
NZ_AP014940.1\|WP_145960169.1\|4937939_4938131_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_172437311.1\|4931448_4933086_-\|diguanylate-cyclase	unknown	unknown	gnl\|CDD\|143635
NZ_AP014940.1\|WP_096380019.1\|4936358_4937252_+\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293810
NZ_AP014940.1\|WP_096379988.1\|4923362_4924379_+\|ribonucleotide-diphosphate-reductase-subunit-beta	unknown	unknown	gnl\|CDD\|153108
NZ_AP014940.1\|WP_096380006.1\|4933300_4934305_-\|type-I-glyceraldehyde-3-phosphate-dehydrogenase	unknown	unknown	gnl\|CDD\|223135
NZ_AP014940.1\|WP_096383714.1\|4924554_4924929_+\|acyl-CoA-thioesterase	unknown	unknown	gnl\|CDD\|239526
NZ_AP014940.1\|WP_096379979.1\|4917225_4920036_-\|DUF2339-domain-containing-protein	unknown	unknown	gnl\|CDD\|378390
NZ_AP014940.1\|WP_096380010.1\|4934539_4935163_+\|outer-membrane-beta-barrel-protein	unknown	unknown	gnl\|CDD\|182867
NZ_AP014940.1\|WP_096379999.1\|4928358_4930638_+\|5-methyltetrahydropteroyltriglutamate---homocysteine-S-methyltransferase	unknown	unknown	gnl\|CDD\|235367
NZ_AP014940.1\|WP_096379996.1\|4926312_4927494_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|226419
NZ_AP014940.1\|WP_096379974.1\|4915849_4917229_-\|DUF3999-domain-containing-protein	unknown	unknown	gnl\|CDD\|372507
NZ_AP014940.1\|WP_096380031.1\|4939304_4940009_+\|molybdate-ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|181841
NZ_AP014940.1\|WP_096380014.1\|4935412_4936285_+\|S1/P1-nuclease	unknown	unknown	gnl\|CDD\|211382
NZ_AP014940.1\|WP_096379984.1\|4920738_4923231_+\|ribonucleoside-diphosphate-reductase-subunit-alpha	unknown	unknown	gnl\|CDD\|178056
NZ_AP014940.1\|WP_096380027.1\|4938475_4939264_+\|molybdate-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|182641
NZ_AP014940.1\|WP_096379992.1\|4925063_4926110_+\|aldo/keto-reductase	unknown	unknown	gnl\|CDD\|381306
NZ_AP014940.1\|WP_145960168.1\|4937311_4937872_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_096380035.1\|4939969_4940686_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|182993	PRK11144, modC, molybdenum ABC transporter ATP-binding protein ModC.	1.65668e-80
NZ_AP014940.1\|WP_096379967.1\|4912709_4913363_-\|HAD-hydrolase-like-protein	gnl\|CDD\|319798	cd04302, HAD_5NT, haloacid dehalogenase (HAD)-like 5'-nucleotidases similar to the Pseudomonas aeruginosa PA0065. 5'-nucleotidases dephosphorylate nucleoside 5'-monophosphates to nucleosides and inorganic phosphate. Purified Pseudomonas aeruginosa PA0065 displayed high activity toward 5'-UMP and 5'-IMP, significant activity against 5'-XMP and 5'-TMP, and low activity against 5'-CMP. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases.	1.59241e-94
NZ_AP014940.1\|WP_096379970.1\|4913366_4914542_-\|phosphoglycerate-kinase	gnl\|CDD\|234613	PRK00073, pgk, phosphoglycerate kinase; Provisional.	0
NZ_AP014940.1\|WP_172437311.1\|4931448_4933086_-\|diguanylate-cyclase	gnl\|CDD\|143635	cd01949, GGDEF, Diguanylate-cyclase (DGC) or GGDEF domain. Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.	2.66743e-44
NZ_AP014940.1\|WP_096380019.1\|4936358_4937252_+\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293810	cd07724, POD-like_MBL-fold, ETHE1 (PDO type I), persulfide dioxygenase A (PDOA, PDO type II) and related proteins; MBL-fold metallo-hydrolase domain. Persulfide dioxygenase (PDO, also known as sulfur dioxygenase, SDO, EC 1.13.11.18) is a non-heme iron-dependent oxygenase which catalyzes the oxidation of glutathione persulfide to glutathione and persulfite in the mitochondria. Mutations in ethe1 (the human PDO gene) are responsible for a rare autosomal recessive metabolic disorder called ethylmalonic encephalopathy. Arabidopsis thaliana ETHE1 is essential for embryo and endosperm development. Bacterial ETHE1-type PDOs are also called Type 1 PDOs. Type II PDOs (also called PDOAs), are mainly proteobacterial. These enzymes belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions.	2.53443e-59
NZ_AP014940.1\|WP_096379988.1\|4923362_4924379_+\|ribonucleotide-diphosphate-reductase-subunit-beta	gnl\|CDD\|153108	cd01049, RNRR2, Ribonucleotide Reductase, R2/beta subunit, ferritin-like diiron-binding domain. Ribonucleotide Reductase, R2/beta subunit (RNRR2) is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. The RNR protein catalyzes the conversion of ribonucleotides to deoxyribonucleotides and is found in all eukaryotes, many prokaryotes, several viruses, and few archaea. The catalytically active form of RNR is a proposed alpha2-beta2 tetramer. The homodimeric alpha subunit (R1) contains the active site and redox active cysteines as well as the allosteric binding sites. The beta subunit (R2) contains a diiron cluster that, in its reduced state, reacts with dioxygen to form a stable tyrosyl radical and a diiron(III) cluster. This essential tyrosyl radical is proposed to generate a thiyl radical, located on a cysteine residue in the R1 active site that initiates ribonucleotide reduction. The beta subunit is composed of 10-13 helices, the 8 longest helices form an alpha-helical bundle; some have 2 addition beta strands. Yeast is unique in that it assembles both homodimers and heterodimers of RNRR2. The yeast heterodimer, Y2Y4, contains R2 (Y2) and a R2 homolog (Y4) that lacks the diiron center and is proposed to only assist in cofactor assembly, and perhaps stabilize R1 (Y1) in its active conformation.	1.07077e-104
NZ_AP014940.1\|WP_096380006.1\|4933300_4934305_-\|type-I-glyceraldehyde-3-phosphate-dehydrogenase	gnl\|CDD\|223135	COG0057, GapA, Glyceraldehyde-3-phosphate dehydrogenase/erythrose-4-phosphate dehydrogenase [Carbohydrate transport and metabolism].	0
NZ_AP014940.1\|WP_096383714.1\|4924554_4924929_+\|acyl-CoA-thioesterase	gnl\|CDD\|239526	cd03442, BFIT_BACH, Brown fat-inducible thioesterase (BFIT). Brain acyl-CoA hydrolase (BACH). These enzymes deacylate long-chain fatty acids by hydrolyzing acyl-CoA thioesters to free fatty acids and CoA-SH. Eukaryotic members of this family are expressed in brain, testis, and brown adipose tissues. The archeal and eukaryotic members of this family have two tandem copies of the conserved hot dog fold, while most bacterial members have only one copy.	1.36085e-51
NZ_AP014940.1\|WP_096379979.1\|4917225_4920036_-\|DUF2339-domain-containing-protein	gnl\|CDD\|378390	pfam10101, DUF2339, Predicted membrane protein (DUF2339). This domain, found in various hypothetical bacterial proteins, has no known function.	3.86098e-86
NZ_AP014940.1\|WP_096380010.1\|4934539_4935163_+\|outer-membrane-beta-barrel-protein	gnl\|CDD\|182867	PRK10959, PRK10959, outer membrane protein W; Provisional.	9.83681e-56
NZ_AP014940.1\|WP_096379999.1\|4928358_4930638_+\|5-methyltetrahydropteroyltriglutamate---homocysteine-S-methyltransferase	gnl\|CDD\|235367	PRK05222, PRK05222, 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase; Provisional.	0
NZ_AP014940.1\|WP_096379996.1\|4926312_4927494_-\|hypothetical-protein	gnl\|CDD\|226419	COG3904, COG3904, Predicted periplasmic protein [Function unknown].	3.79201e-11
NZ_AP014940.1\|WP_096379974.1\|4915849_4917229_-\|DUF3999-domain-containing-protein	gnl\|CDD\|372507	pfam13163, DUF3999, Protein of unknown function (DUF3999). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are typically between 440 and 470 amino acids in length. There is a single completely conserved residue D that may be functionally important.	1.98922e-86
NZ_AP014940.1\|WP_096380014.1\|4935412_4936285_+\|S1/P1-nuclease	gnl\|CDD\|211382	cd11010, S1-P1_nuclease, S1/P1 nucleases and related enzymes. This family summarizes both S1 and P1 nucleases (EC:3.1.30.1) which cleave RNA and single stranded DNA with no base specificity. S1 nuclease is more active on DNA than RNA. Its reaction products are oligonucleotides or single nucleotides with 5' phosphoryl groups. Although its primary substrate is single-stranded, it may also introduce single-stranded breaks in double-stranded DNA or RNA, or DNA-RNA hybrids. It is used as a reagent in nuclease protection assays and in removing single stranded tails from DNA molecules to create blunt ended molecules and opening hairpin loops generated during synthesis of double stranded cDNA. P1 nuclease cleaves its substrate at every position yielding nucleoside 5' monophosphates, and it does not recognize or act on double-stranded DNA. It is useful at removing single stranded strands hanging off the end of double stranded DNA and at completely cleaving melted DNA for simple DNA composition analysis.	5.54896e-80
NZ_AP014940.1\|WP_096379984.1\|4920738_4923231_+\|ribonucleoside-diphosphate-reductase-subunit-alpha	gnl\|CDD\|178056	PLN02437, PLN02437, ribonucleoside--diphosphate reductase large subunit.	0
NZ_AP014940.1\|WP_096380027.1\|4938475_4939264_+\|molybdate-ABC-transporter-substrate-binding-protein	gnl\|CDD\|182641	PRK10677, modA, molybdate transporter periplasmic protein; Provisional.	2.72317e-95
NZ_AP014940.1\|WP_096379992.1\|4925063_4926110_+\|aldo/keto-reductase	gnl\|CDD\|381306	cd19080, AKR_AKR9A_9B, AKR9A and AKR9B families of aldo-keto reductase (AKR). The AKR9A family includes Aspergillus nidulans sterigmatocystin biosynthesis dehydrogenase StcV, Aspergillus flavus norsolorinic acid reductase (NOR), and Phanerochaete chrysosporium aryl-alcohol dehydrogenase [NADP(+)] (AAD), are founding members of aldo-keto reductase family 9 member A1-3 (AKR9A1-3), respectively. StcV may be involved in the dehydration of 5'-hydroxyaverantin to form averufin. NOR is involved in aflatoxin biosynthesis. AAD (EC1.1.1.91) is involved in lignin degradation and reduces aromatic benzaldehydes to their respective alcohols in the presence of NADP(H). The AKR9B family includes Saccharomyces cerevisiae aryl-alcohol dehydrogenases AAD14p, AAD3p, AAD4p, and AAD10p, which are founding members of aldo-keto reductase family 9 member B1-4 (AKR9B1-4), respectively.	0
NZ_AP014940.1\|WP_096380031.1\|4939304_4940009_+\|molybdate-ABC-transporter-permease-subunit	gnl\|CDD\|181841	PRK09421, modB, molybdate ABC transporter permease subunit.	1.2315e-120

>NZ_AP014940.1|WP_096379999.1|4928358_4930638_+|5-methyltetrahydropteroyltriglutamate---homocysteine-S-methyltransferase
MISVTTLGFPRIGARRELKQALESFWKGDSDAAALQTAAAALRERHWRLAAAAGADSVPCNDFSLYDHVLDTAVLFDAIPASHRAAFEEDPLTGYFALARGLQDGRRDLRALEMTKWFDTNYHYLVPQFEPGQRFALRADKPLAELAQAQALGLDARPVLVGPVTFLKLGKRSDGGDPRELLDALLPAYAELLAKLKAAGANWVQIDEPALALDLDDADRAAYRRAYDALAQADSPQRLLATYFGALGDNAALAAQLPVQALHLDLVRAPQQLEAVLPLLPQDRALSLGVVDGRNIWRADLDAALSLARRAGERARWLAPSCSLLHVPTDLELERKLPGPLKQWMAYAKQKIEELRLIAGALAGDAAAEGELAQAASARAARLASPLLRNAQVRKRLAAVEPAMTRRASAYPQRARLQQQRLNLPLFPTTTIGSFPQTAQVRHARAEHKAGRLDDAGYRAFLENETVQCLREQEALGIDMLVHGEFERNDMVEYFGEQLDGFAFTSHGWVQSYGSRCVKPPVLFGDVARPKPMTVEWSRFAQDHAVKPVKGMLTGPVTILQWSFVRDDQPRADSCRQIALALREEVLDLEAAGIAAIQIDEPALREGLPLRRSDWPAYLDWAGESFRLAASGVDDATQIHTHMCYAEFNDIIDAVAALDADVISIETSRSRMELLDAFVRYRYPNGIGPGVYDIHSPRVPDETEMRELLDKALDVLEPAQLWVNPDCGLKTRGWPEVRAALQAMVGAAQGLREAVQAEA
>NZ_AP014940.1|WP_096379996.1|4926312_4927494_-|hypothetical-protein
MVPQRSPFAPRRLLAASLALLCALALAACGKDEPAPSGAAVTLGSQNDMPKPAPAAVSEEDILKGTYWPPAKLDGGVARISCEYDYPRFGDGDKLESLDFFSLVDAMSPCQARGVVRVRYQGKIGAGFTALAQRVAAMAARMEISTRILDIDSSGGHVEEALRAGDSIAESGWAIWVREESVCHSACVLVLAAGDTRSIEGKVGIHRLMRDRSTATSRAELSRELRAINQQVRDYLERNGVATAVSDLMMTVANRDLRILTPDELKQYGLDGTNAAQDDLDRIRLARKCGDDFVRRRESFRRAFDAQCMGTGKSFESMPECAEQLQSKFGFPDKACPGDSPADLYARDLPPPLLDEVAAAEGGEGKAADAKSADAKSADGKPAKSDKAEKSAK
>NZ_AP014940.1|WP_096379992.1|4925063_4926110_+|aldo/keto-reductase
MQLDHYRTLGRSGLRISPICLGTMTFGQDWGWGSDESEARSVFETYLERGGNYFDTANFYTGGSSETLLGRFAQGRRDRLVIATKFSLCTDPGDPNAGGNHRKNLRRSVEASLRRLDTDYIDLLYLHAWDATTPVEEVMRGFDDLVRAGKVLYAGVSDLPAWQAARLQTLAELRGWSPLVALQTEYSLAQRESERELLPMARELGLGVSAWSPLASGVLTGKYSRADLDPATAQGRRAVAIGNGALTERALDIAQVVVEIARELERPAAQVALAWTLQRPGAIVPVIGARTQAQLLQNLGALEVELSPAQIERLERASAIALGFPHDFLALPGIVGAMFGGAQVRRDW
>NZ_AP014940.1|WP_096383714.1|4924554_4924929_+|acyl-CoA-thioesterase
MTEARMTEIVFPDHTNHLGTLFGGQALAWMDKAAFIAASRYARRTVVTARSEQIDFHLPVPKGALVELIARVVETGRTSMQVEVEMIREDLLTGESQLATRGRFTMIALDIEGKPTAVPALPAA
>NZ_AP014940.1|WP_096379988.1|4923362_4924379_+|ribonucleotide-diphosphate-reductase-subunit-beta
MSIAPPRLLDPGFDLTLRPMRYAQFYEMYRDAIRNTWTVEEVDFSQDVNDLKHKFGPAERHLVERLVAFFATGDSIVANNLVLNLYQHINAPEARMYLSRQLYEEALHVQFYLTLLDTYLPDPNERAKAFDAVEKIPSIRAKAEFCFRWIDSIQGLKRVETREQRRQFLLNLICFAGCIEGLFFFAAFAYVYYLRSRGLLNGLASGTNWVFRDESCHMAFAFEVIRTAREEEPDLFDADLRAQVVKMFEEAVDCEYLFAQDVLSGGVVGLSLKDMRQYLEYCADQRMVQLGMPKHFGSTNPFAFMDLQDVQEVTNFFERRVSAYQVGVQGEVAFDEAF
>NZ_AP014940.1|WP_096379984.1|4920738_4923231_+|ribonucleoside-diphosphate-reductase-subunit-alpha
MTTLETDSSVAPATDAASVPAAAVKPQRSAQDAPGFALTPPAANLTMSVTKRSGRREPVDLNKIVRAVTRCAEGLYSVDPMRVSTRTISGLYDGATTRELDELSIRTAALLTAEEPEYGRLAARLLAGVIEKEVAGIEIHAFSQSVQRGFDLGLINQRLLDFVQANARKLNDAIDRNLDAKFDYFGLRTLYDRYLLRHPTARTVIETPQQFFLRIACALSEDVSDALALYRRMAQLDYIPSSPTLFNSGTTHEQLSSCFLLDSPEDSLEAIYKRYMDVAKLSKFSGGIGLSYTRIRARGSLIRSTNGLSNGIVPWLKTLDASVAAVNQGGKRKGAACVYLEPWHADIEEFLELRDNTGDEARRTHNLNLANWIPDEFMRRVEADADWSLFDPAKVPQLTDLWGESFERAYRAAEATGLAVKKVKARDIYGRMMRTLAQTGNGWMNFKDKSNRACNQTLREGNVVHLSNLCTEILEVTSQDETAVCNLGSINLSHHVEIFEDGKGAFDFDKLAETVRLAVRQLDRVIDLNFYPIETARRANLRWRPVGLGTMGLQDVFFKLRLPFDSEPARKLGREIAEAIYFHALSASNELAMEHGKHPAFDDTRASGGELQFEAWGVEPSQPERWTELRARIKQHGLRNSLLVAIAPTATIASIAGCYECIEPQVSNLFKRETLSGDFLVVNKYLVEELKKLGLWTAEMRDRIKMAEGSIQAVAEIPESLRQVYRTAWELPMRSLIDMAADRGAFIDQSQSLNLFIESPNIGQLSSMYMYAWKKGLKTTYYLRSRPATKIAKTTVSAPAAAPVAPKPEYSEDEAIACSLENPESCEACQ
>NZ_AP014940.1|WP_096379979.1|4917225_4920036_-|DUF2339-domain-containing-protein
MESLIVLLVLVVLAVPVLLVVALVQLSSVRGRVAGLEREVERLRQSGAPVRNEATLAELTARENAARAQAERAATPSVAAAPTAPTTAPPATAPPTPPAPERPAPTPAQPPPLPATAPPIAAPPRPQAPRAPAAPPPPPPDVFTVAARWLRRWFTEGNVPVKVGMLVLLAGVAALLKYASDQGWMRVPVELRLAGVAAAALAALVFGWRQRERKRVFGLSLQGGAIGVLLLVVFAAFKLYGMIPAGAAFALSVVLVAGTGVLSVKQNALALAVFAILAGFLAPIWLSTGSGNHVALFGYYAVLNAGIFAIAWWRPWRVLNLLGFAFTWGIGSLWGVLKYRPEHYSTTEPFLLLFFAFYLLIPVLYARRRAAGRRDLIDGCLVFGTPLIAFTLQAGLLEGARMPLAFCALGLGALYAALAWWLRRDQRFLALSVPYALLAVGFATLAVPLALAAEATACVFALEGAALAWLGLRQQRLLPQLTGAGLQVAAAMAFAIGASDEVWDAQQALLNANFAGALLIALAGLASAASYRRSDSLKPLALLYYLWGLAWWLGAFGSQIVDFVAAPTRADVWLILFVATGWLAAETFARHSWKALSATAMLALGAAVPLAFAQIEAHSWPLRDWGWLAWAAYAALGARSLMALRERAQGELAFAHLAWLWSWALTLGASLCLWLGKGAGLGERLGNGWTLAAALLPALVIAAACVWRPRWAGWPVAPRFAQWRYGACASFIVFLVLAVAALLSVDADPRPLLWLPLLNPMGLVQWAVLLLLGAWLASPMVGDDLRARRVPLLALAGFGLITVEVLRSAHFWGAVPWGPSMLSASLVQTSLTVVWSVLGVAGWIVGSRRGQRGLWLAGAVLMGVVLAKLVLVDRSHLGNLLGIASFIAYGLLCTLVGYFAPAPPSRDAKPDADAGSDETGNDDTPPDQRPPQDASA
>NZ_AP014940.1|WP_096379974.1|4915849_4917229_-|DUF3999-domain-containing-protein
MKPRSLAFALLALALPLSAAPRQDYAQQWPLQLSRDDGGAYRVVLDPAVYAQAQSAQLRDIDVIDASGASVPSDVFAPEQPLARAPQHRALPWFPLPAASSSGAAQGWELVSEVETDGRLRRVEARSTAAGATKLPQTSLLIDASAVRAPIQALQLQWAPGAALDAAYSVEASDDLDHWRSVNSSGRLVDLERDGRRLQQRRIAFDAVGEQARYLRLTPQDPQRAAQIVAVEAELAAGAAGAPLQWRELKGARVELKDGSVAFEYRLDGRFPIQQADVALPGNHALQWRLDSRDSEDEGWRAQAGPWMAYAVAGQGAGDRSAARQLSGVSRDRLWRLRASGAVPGEPVLRLGYRPEVAVFLAQGQPPYALVAGSARAARADSPLAQLVDALRSSRGNEWRPADATLGAASALAGAAALVPAAPERDWRSWLLWAVLVAGALIVVGFAMSLLRSGKAPQA
>NZ_AP014940.1|WP_096379970.1|4913366_4914542_-|phosphoglycerate-kinase
MSIVRMTDLDLAGKRVLIREDLNVPIDDGRITSELRILAAIPTLKLALEKGAAVMVTSHLGRPKEGQWSQADSLAPVAQRLSELLGIDVPLVKDWVDGVEVQPGQLVLLENCRMNVGEGKDDEALARKYAALCDVFVMDAFGTAHRAQASTHGAIRYAKTAAGGPLLMAELDALAKALDNPARPLLAIVAGSKVSTKLELLASLVSKVDQLIVGGGIANTFIAAMGHNVGKSLVETDLIDTAKKIMADAKARGADIPVPSDVVVAPAFAADAPATVKAVDAVGADDMILDIGPDTAARYAELIAQAGTVVWNGPVGVFEFDAFGKGTETLARAIAASKAFSIAGGGDTLAAVDKYGIADEVSYISTGGGAFLEFLEGKELPAVAALKQRAG
>NZ_AP014940.1|WP_096379967.1|4912709_4913363_-|HAD-hydrolase-like-protein
MSAQPQPVLFFDLDGTLIDSSVGITRSIAYALETMRHPVPDEQALRGWIGPALRTSFQPLLGDEDKVEQAVALYLERYGREGWTEHSVYDGIAELLEGLRAAGYRMAVVTAKNENNARKILSHLPFGAYFEDIVGCTDDGRLTHKVELIAEALSRFGLQPGQCVMIGDRRMDIEGAAQHGMTGVGVLWGFGSEQELRDAGARRIAAAPAQLPQLLAA
>NZ_AP014940.1|WP_172437311.1|4931448_4933086_-|diguanylate-cyclase
MRNGLYRQFLRLLVMAVVLPSLAFGAAMVFSRYRSELAQIDAHTVASADILAHELDQSLIALRASLHVLASAGERHRLDWNRELAELQRRYPPILTLIATDARGRVIGAAPASAVARAIGLDVADRAYFQVPARSGRDYVSDAFVGRGIGHDPLVVVSVPRYRDGAFEGVIEASLSPSHLYDDSGHGGYETVLLDRSERVIHASGGMQLSFMQRAADTGFGAALGALDSARARGSLPVMPGGGRAFVARARTADGWSLYAVAPRERAERGVFERAMLMSQLLLLAVFGSALAFVWYARVLARAASSLLLRLRALASGATPEPGAHADDAPMPEELQPVLDAIVELSGRLEHAHAELRQSLSEREDEVVQRTAQLREALRELDRVACTDPLTGALNRRGRDEFVRALAAQGARLGSVAVLLIDVDHFKAYNDRYGHRAGDEALRASVAAIRAEVREGADAVVRTGGEEFCVLIPGVGRARVLNIARAILLGMYRRDIEHRDSEHGRLSCSIGVAMAYAVDELETAMDRADEALYRAKRRGRNGYCF
>NZ_AP014940.1|WP_096380006.1|4933300_4934305_-|type-I-glyceraldehyde-3-phosphate-dehydrogenase
MTIKVGINGFGRIGRNVLRAAVQNFDGEIEIVAINDLLEPDYLAYMLQYDSVHGRFKGTVAVEGNTLIVNGKKIRLTQERDPANLKWDEVGAEVVIESTGLFLDKTTAQKHLDAGAKKVVLSAPSKDDTPMFVFGVNDKTYKGEAIVSNASCTTNCLAPLAKVLNDKWGIKRGLMTTVHAATATQKTVDGPSNKDWRGGRGILENIIPSSTGAAKAVGVVIPELNKKLTGMSFRVPTSDVSVVDLTVELNKDATYAEICAEMKAQSEGALKGVLGYTEDKVVATDFRGDARTSIFDAEAGIALDGTFVKLVSWYDNEWGYSNKCLEMVKVVAGK
>NZ_AP014940.1|WP_096380010.1|4934539_4935163_+|outer-membrane-beta-barrel-protein
MNHRLIGGLVAAALACAAHPALAQQAGTFTLGVGAHQVQPKSNNGSLLGGTAQLEIGDNVQPTVTFEYFFRDNLGIEVLAATPFKHDIDIKGLGKVATTKHLPPTFSLQYHWNSQGVVSPFVGVGVNYTTFFSEKTTGPLRGAKLKLEDSVGVAAHVGVDFVLNERGAIRVDARWMDIGSDVKLNGTKIGKANIDPLVYGLAYVFKF
>NZ_AP014940.1|WP_096380014.1|4935412_4936285_+|S1/P1-nuclease
MIDPRAPTRIRPRFARRLLDAAVVLAVVSAALPLPALAWGRQGHRLVAELAWDEMSPAARAEAQKLLAGEPDPTLPGIANWADLLRDEKPELGKRSAKWHYIDLPEDGDCQYDAARDCPDGNCAVAAILAQTAILADRSKPKAERLEALKFVVHLVGDVHQPLHVGYARDKGGNSFQLAIPGERPGGYGGNLHSLWDSGMLNMSKLDDDRYLAKLKDIQVPAVSALALPPPAADWAEESCKLMRQPGFYPPTHKLAPDYVATWRPLAETQLRLGGEHLAKLLDAALAPGR
>NZ_AP014940.1|WP_096380019.1|4936358_4937252_+|MBL-fold-metallo-hydrolase
MPPPQSNAAAPQVSAFHHRDTGTWSYLVADPATRAAAILDPVLDFDPRSGRTGLDSASALLERAAADGLRIDWLLETHAHADHLSAAHALRERLRAQTGHAPRLAIGRRIGEVRRVFAPLFGLADDAEAGFDHLFDDDEDFAVGALAARAIPVPGHTQDSLAYLIGDALFVGDSLFLPDSGTARCDFPGGDAAMLYQSIQRLYRLDDATRVFVCHDYGKDGREPACETRIGAQKRDNVHVRADTAEAEFVSLREARDRTLAVPALILPALQVNLRGGALPEPEANGVRYLKLPLDQL
>NZ_AP014940.1|WP_145960168.1|4937311_4937872_+|hypothetical-protein
MFASRLLESAEFEGRSSENLLIKSRLLVLPALLAAGFAAHAEHRHGEAAPAAMPQGAVEVKLDEAVLAKLPQVKAEGSAHGRKLSCEGVALVELLRASGAMPTEPLRGAQLSRIAQVRARDGYRAAFSLGELDPSLGNRPVVLTRRCNGADLPAGDGPWRLIVPGESRPARWVRQVESIRVGDADV
>NZ_AP014940.1|WP_145960169.1|4937939_4938131_+|hypothetical-protein
MALKSLDPRVRGDDGVEWRGETRLSRNLRAIKPTYREPTYRHSRERGLCFTSAKPNIQGFIEA
>NZ_AP014940.1|WP_096380027.1|4938475_4939264_+|molybdate-ABC-transporter-substrate-binding-protein
MNLRCRFLGALCALGFALAAGAAPAQDKGAEPLTVFAAASLKESLDEAAAAYQKQTGQAVRASYAASSALARQIEQGAPADLFFSADLDWMDYLQQRQLLVDASRRNVLGNTLVLIAPKDSKAKAPALKPGVDLRPLLGDGRLAVALTASVPAGKYARAAFEKFGVWEQVQPRLAEGENVRAALMLVARGEAPLGVVYGSDAQAEPKVRVLATFPADSHAPIVYPVAVVKASAHPGAAKFAQWLRGKQAAAIFRRHGFAPLP
>NZ_AP014940.1|WP_096380031.1|4939304_4940009_+|molybdate-ABC-transporter-permease-subunit
MSEGWAGFSAAELTAIALSLKVAAAATVCSLPFGVAMGWLLARTRFPGKLLVDTLLYLPLVVPPVVTGYALLLGFGAQGPIGRFLSEHVGIVFAFRWTGAALASAIMGFPLMVRAIRLSIEAVDPRLEQAASTLGANPWRVFFGVTLPLAWPGLLAGAVLCFAKALGEFGATITFVSNIAGETQTLSSAIWGLMQTPGAESGVLRLALVAVALSFAAVFASEWLVQRQRAGTQR
>NZ_AP014940.1|WP_096380035.1|4939969_4940686_+|ATP-binding-cassette-domain-containing-protein
MAGAAPARGNAAMSADADAQTPLQAGFDIDIELRRGSFRRAFAIRSERRVIAVVGDSGAGKTSLLHAIAGLLRPARGRIVVAGETLFDRDRRIDLPAHRRRIGYVFQDARLFPHLDVRANLLYGLRGAAARERRFELADIVELLGIGPLLARGTGGLSGGETQRVALGRALLSQPRILLLDEPLSMLDMNRRDELLPYLQRVRDESGLPMIYVSHYPEEVRRIAEEVHRVGEAAPLAT

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Crispr_ID: NZ_AP014940_13

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_13

5679411-5679502

Orphan

Consensus_repeat	Method
CGACCGCCGCCACCGACAGCACG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP014940_13

>merge|NZ_AP014940|13|5679411-5679502|CRISPRCasFinder
CGACCGCCGCCACCGACAGCACGTTGGCGTAGGACGCCGGATAGCTCTTGCTGCTGTTGCCGGAGTTGCCGGCCGCCGCCACCGACAGCACG

>NZ_AP014940|13|13|5679411-5679502|CRISPRCasFinder
CGACCGCCGCCACCGACAGCACG	TTGGCGTAGGACGCCGGATAGCTCTTGCTGCTGTTGCCGGAGTTGC
CGGCCGCCGCCACCGACAGCACG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_074870372.1\|5691484_5691805_+\|DUF2782-domain-containing-protein	unknown	unknown	gnl\|CDD\|378588
NZ_AP014940.1\|WP_145960211.1\|5668211_5668571_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096383802.1\|5687029_5687944_+\|oxygen-dependent-coproporphyrinogen-oxidase	unknown	unknown	gnl\|CDD\|235413
NZ_AP014940.1\|WP_096381857.1\|5693352_5694600_-\|phytase	unknown	unknown	gnl\|CDD\|271326
NZ_AP014940.1\|WP_096381821.1\|5674820_5678195_-\|ankyrin-repeat-domain-containing-protein	unknown	unknown	gnl\|CDD\|222980
NZ_AP014940.1\|WP_096381807.1\|5668679_5670488_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096381848.1\|5691908_5692337_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_AP014940.1\|WP_074870863.1\|5665235_5665568_+\|thioredoxin	unknown	unknown	gnl\|CDD\|200072
NZ_AP014940.1\|WP_172437339.1\|5670754_5670919_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096381829.1\|5680688_5681693_-\|cytochrome-d-ubiquinol-oxidase-subunit-II	unknown	unknown	gnl\|CDD\|224213
NZ_AP014940.1\|WP_096381862.1\|5694774_5697126_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657
NZ_AP014940.1\|WP_096381816.1\|5672675_5674517_+\|cation:proton-antiporter	unknown	unknown	gnl\|CDD\|235131
NZ_AP014940.1\|WP_145960212.1\|5671525_5672416_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096381838.1\|5684137_5686540_+\|S9-family-peptidase	unknown	unknown	gnl\|CDD\|224423
NZ_AP014940.1\|WP_074870385.1\|5678187_5678457_-\|YcgL-domain-containing-protein	unknown	unknown	gnl\|CDD\|377477
NZ_AP014940.1\|WP_074870380.1\|5681724_5683125_-\|cytochrome-ubiquinol-oxidase-subunit-I	unknown	unknown	gnl\|CDD\|376587
NZ_AP014940.1\|WP_096381802.1\|5665938_5667741_+\|transcription-termination-factor-Rho	unknown	unknown	gnl\|CDD\|236490
NZ_AP014940.1\|WP_172437387.1\|5678715_5679111_-\|S8-family-serine-peptidase	unknown	unknown	gnl\|CDD\|173798
NZ_AP014940.1\|WP_096381843.1\|5688589_5691355_-\|DNA-polymerase-I	unknown	unknown	gnl\|CDD\|235591
NZ_AP014940.1\|WP_145960214.1\|5692703_5693261_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_074870372.1\|5691484_5691805_+\|DUF2782-domain-containing-protein	gnl\|CDD\|378588	pfam11191, DUF2782, Protein of unknown function (DUF2782). This is a bacterial family of proteins whose function is unknown.	2.80787e-17
NZ_AP014940.1\|WP_096383802.1\|5687029_5687944_+\|oxygen-dependent-coproporphyrinogen-oxidase	gnl\|CDD\|235413	PRK05330, PRK05330, oxygen-dependent coproporphyrinogen oxidase.	0
NZ_AP014940.1\|WP_096381857.1\|5693352_5694600_-\|phytase	gnl\|CDD\|271326	cd14956, NHL_like_3, Uncharacterized NHL-repeat domain in bacterial proteins. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.	8.60842e-05
NZ_AP014940.1\|WP_096381821.1\|5674820_5678195_-\|ankyrin-repeat-domain-containing-protein	gnl\|CDD\|222980	PHA03095, PHA03095, ankyrin-like protein; Provisional.	1.35656e-18
NZ_AP014940.1\|WP_074870863.1\|5665235_5665568_+\|thioredoxin	gnl\|CDD\|200072	TIGR01068, Thioredoxin-like_protein_slr0233, thioredoxin. Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport].	6.13947e-39
NZ_AP014940.1\|WP_096381816.1\|5672675_5674517_+\|cation:proton-antiporter	gnl\|CDD\|235131	PRK03562, PRK03562, glutathione-regulated potassium-efflux system protein KefC; Provisional.	0
NZ_AP014940.1\|WP_096381829.1\|5680688_5681693_-\|cytochrome-d-ubiquinol-oxidase-subunit-II	gnl\|CDD\|224213	COG1294, AppB, Cytochrome bd-type quinol oxidase, subunit 2 [Energy production and conversion].	2.99682e-87
NZ_AP014940.1\|WP_096381862.1\|5694774_5697126_+\|TonB-dependent-receptor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	3.64405e-54
NZ_AP014940.1\|WP_096381848.1\|5691908_5692337_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	2.76077e-09
NZ_AP014940.1\|WP_096381838.1\|5684137_5686540_+\|S9-family-peptidase	gnl\|CDD\|224423	COG1506, DAP2, Dipeptidyl aminopeptidases/acylaminoacyl-peptidases [Amino acid transport and metabolism].	1.80589e-79
NZ_AP014940.1\|WP_074870385.1\|5678187_5678457_-\|YcgL-domain-containing-protein	gnl\|CDD\|377477	pfam05166, YcgL, YcgL domain. This family of proteins formerly called DUF709 includes the E. coli gene ycgL. homologs of YcgL are found in gammaproteobacteria. The structure of this protein shows a novel alpha/beta/alpha sandwich structure.	2.10278e-33
NZ_AP014940.1\|WP_074870380.1\|5681724_5683125_-\|cytochrome-ubiquinol-oxidase-subunit-I	gnl\|CDD\|376587	pfam01654, Cyt_bd_oxida_I, Cytochrome bd terminal oxidase subunit I. This family are the alternative oxidases found in many bacteria which oxidize ubiquinol and reduce oxygen as part of the electron transport chain. This family is the subunit I of the oxidase E. coli has two copies of the oxidase, bo and bd', both of which are represented here In some nitrogen fixing bacteria, e.g. Klebsiella pneumoniae this oxidase is responsible for removing oxygen in microaerobic conditions, making the oxidase required for nitrogen fixation. This subunit binds a single b-haem, through ligands at His186 and Met393 (using SW:P11026 numbering). In addition His19 is a ligand for the haem b found in subunit II.	0
NZ_AP014940.1\|WP_096381802.1\|5665938_5667741_+\|transcription-termination-factor-Rho	gnl\|CDD\|236490	PRK09376, rho, transcription termination factor Rho; Provisional.	0
NZ_AP014940.1\|WP_172437387.1\|5678715_5679111_-\|S8-family-serine-peptidase	gnl\|CDD\|173798	cd05562, Peptidases_S53_like, Peptidase domain in the S53 family. Members of the peptidase S53 (sedolisin) family include endopeptidases and exopeptidases. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of Asn in subtilisin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. Characterized sedolisins include Kumamolisin, an extracellular calcium-dependent thermostable endopeptidase from Bacillus. The enzyme is synthesized with a 188 amino acid N-terminal preprotein region which is cleaved after the extraction into the extracellular space with low pH. One kumamolysin paralog, kumamolisin-As, is believed to be a collagenase. TPP1 is a serine protease that functions as a tripeptidyl exopeptidase as well as an endopeptidase. Less is known about PSCP from Pseudomonas which is thought to be an aspartic proteinase.	2.17488e-15
NZ_AP014940.1\|WP_096381843.1\|5688589_5691355_-\|DNA-polymerase-I	gnl\|CDD\|235591	PRK05755, PRK05755, DNA polymerase I; Provisional.	0

>NZ_AP014940.1|WP_172437387.1|5678715_5679111_-|S8-family-serine-peptidase
MVLYNNVADPFPYSTGVAGSAGISGVAVSQGSGVALRSLAGQVATLNPTTVFDTHSYAVLSGTSMASPHVAGVAALLFAAKPSATAAQVRDAMTATALDLGAPGRDNEYGFGMVRAFEALDRLTATGTSAN
>NZ_AP014940.1|WP_074870385.1|5678187_5678457_-|YcgL-domain-containing-protein
MQAYVYKSLRKADTYVFLSARDDFARVPEPVLQQLGSLQFVLEVELGPERKLARADAATVRENLAARGFHLQFPPLPGMPVAEAAQPDA
>NZ_AP014940.1|WP_096381821.1|5674820_5678195_-|ankyrin-repeat-domain-containing-protein
MPDAPTSRALSKGFAIALAAGLALALATGFGGTSAGAVVALLGGALAQPAFALAARLWRRRDDRPDWKPELLNLSALWGGATAATAALAAWPLSALLQSGSLLAALGLSVVAGLLLLGLWRLWPLWTGTERDGAPLPPQWARLADLDLGAWRGLGVAGIVAGLVAVGLLLAWPGLLSTGARWTLAVAFALASPALHLLLQSIRAADPLPGLEFDPELDTVHASDELLDGDTGELSDAELAQALYAAARAGKVERALELIELGADVNAAPPADDERDRRSLSVLAAVLPDLRLLRGLIARGADLNATHAGMTPLLAATRDSWHGRPDAVMTLLANGADPRLADHEGNTPLHHAARSSDPGVAALLRDAQAELETLNHDGLSPLGVACASGNWRLAKFLLERGAKTEHAGGSPALLAAAGGDEDDPAGVQLLLKHKARIDARDGQRRSALHTAAFAGHLDIVTTLLAAGADAAAIDSQQRTPVLEAARGGRPGVLERLLEHLPHGGVEQAKALDADGASALILACQAETASPPLVLRLLELGLDPELRDRQGKRAVDRAAEAGRWSLVAALDRAYPLPAAVSGEGDADAPEGERVIVDRMPAALLRDGLREGRSSELTGLAKLLSPAELGAQLHEEDGQAPSAERIDWLLGQGADANVRNAAGDTVLFALLDRAPGSLPALHALLRHGVSPAGRGGLGRFLATCSAGEQAARGLEQFALDLIERGADVFARTPAGDPPLAIAVRMGWARLLERLLASGVDLNARDSHGMSALHLAAALGRENMLKRLVAHGAAPDLLAADGQTPLGVALASGRRDLADWLDWRGWPLPKRPLLAADVPAAAIVGDADAVRRLLDLGLSVDALDSQGCTALLRAAGGGHRAVVDLLLARGADPQRAANSGATPLSAAVSMRHGEIVDRLVAAGASLEQRLPGELTVLMVACALGLTDLAARLLAAGADVQARDAQGRMALHCAAMYGFTARERSRLVALFDTLLLAGVDADQSAAGATPLLLLLGARAEPGTAADEDVLIAGLELLLDHEASLDVQDPRGFGPLHLASLHGLLRVVQRLLRHGANPDQRDALNRTPREIAVMRGFVDIAAEFAPATPAGGTSGGVSMARFLRGGPGN
>NZ_AP014940.1|WP_096381816.1|5672675_5674517_+|cation:proton-antiporter
MHGGGLELALLFLLAAVIAVPVFRKFGLGAVLGYLAAGVVLGPYGVKVIADAEPVLAASEIGVVMMLFVIGLELSPSRLRVMRKPVFGAGGLQVILSGIALGALAMFGGGLGWKAATVVGLGLALSSTAVCLQLLSERKGLSADYGKLAFAILLFQDLAAIPLLAAIPLLGKAAGVDGLNWISVAKAVGAIAAVVFGGRVLLRQVFRVVARTQMPEVFTGAALLTVLGSAWILQTAGLSAGLGAFLAGVLLADSEFRHELESQIEPFKGLLLGLFFMAVGMSIDLQRVMNEPLTIGAIVLTLLTVKFALLFAVGISAGGLDKRGAFQLSTVMALGGEFAFVVFNEAFKAKLLDDPTRDRLIAAVGVSMALTPLLMIAAQRLLDSAPAAKPKRPYDEITDDHHPQVLLAGMGRFGQIVARLLVAHRTPFIAIENSAEQVDFMRRFGNMVYYGDPARPELLRSAGAAQVKVFVIAIDDRDACIRTVRTVRRLYPKAKVFARARDRRHSWELMDLGAEPMRETFHSSLKLGEDVLVELGVQPATARDHVERFRELDERMLNAQYLVHDDEDALMQSARDARKELEELFEADRGEGVLGGMVDKQATTVSSENTTRH
>NZ_AP014940.1|WP_145960212.1|5671525_5672416_-|hypothetical-protein
MKGMSRIAGTLLLAVLAVLALPATVAAQGVAAVRKQVEMSLVVVGQVRIAADGRVEGLQLDRESELPAPVVQLVRESVPRWRFDPLPADVPAQTAQTPMTLRVVLRPAPESAEPAAAQPQPASFVLRIVSARFGDTPADAMPRMLSAPPPRFPKDALGARMPATVYLVVRVGRDGRVVESFAEQVNLFALGSEQQMARFRQQFADTSLAAVKRWRFAPPTRGDEVGADSWQLRVPVDFLFDVRRPKPGTWRVYVPGPRQRAPWARETADSGVDAFADSGPQPIGGGRRLLSALGDG
>NZ_AP014940.1|WP_172437339.1|5670754_5670919_-|hypothetical-protein
MKTLMILFAALCLSACDPAFDQPPMLKGDKATTAKAASTAALPRLSTPTARIGG
>NZ_AP014940.1|WP_096381807.1|5668679_5670488_-|hypothetical-protein
MNAAVDSLPPAGVAPAGDPAAALRRYAGQGIPPGLPTAYTALLPADGQWGRETVMRAFVADALQRNGMVVDEDTLDATVAAATVPTGAFAGVEFEWKLQPGESRADGRPSPPFQGYSLQVPAAAQEELAAFAKEWAAQHDPHAPGSEDAPLRKLKGLAGAAGKSDVLETLEALDAAIKAGTTAQQAGKPLDAVALSAVLEFATRSGHEREAAKLLERYTAVKGITTDARELSQHAGRVFNGRDPVTGKALTADDRVNSAFDLLSGGFKLAGNIGSTALLMGAGNSGLVAGLIGVAPVGIAVVAFAAGAYQLIKHIREAILKPQWDEFRERFPFAEGMEPKQAITGVMRQIAGMPTDGRNALATATRIMEGMGENPETRERFLSFLKQKVQPESLVDALASGRGGQLTEQQAMLLAQAAKSSSKEFLDLELKDVKRYVKDRDGERERGTYLLPAAQQEAANRNGNKLGGAVEEGLRVAGILTSGANALNGQYRDLLDKLKGVDLPNKLGEQQQKNLAAALVPAVREGGLSQVDHLIPSKDGSRLFAVQGDPNSPDRRMVALDVEKGTQQSIETSSKLAAHHAANGGGGGQDPLQNQNQGGRGF
>NZ_AP014940.1|WP_145960211.1|5668211_5668571_-|hypothetical-protein
MVIEERVRSSSSLAELQDRIHGADRKAPVAHRTGPPARCFSLRPRCLRPGPIEKHRAGGLVRFRRVASSVGTRRASRIGRAALPAQRRLRSLAAFLCQNVTPCQNVIPAKAGIQGVIAA
>NZ_AP014940.1|WP_096381802.1|5665938_5667741_+|transcription-termination-factor-Rho
MSDKTPDAGDTAEKRVRKPRASKAAEAAPAIVADASPLIPAPMPASEPAAAAAPAPRPSKAAASAPAASAGESAPAASGAAETAAPQNNGPSNNGHANDGGGQSNNAQQQGQQNQAGQQRDGGYDNNRGGNNRRDRFRNRRERDRNNRQQQRGGSGGEDFGDNGENFVPRPHPQVPEGFPQYSLGDLKRMPAPKLLDLADQLSIQEGVARARKQDVIFALLKVLTRHGEGVAADGVLEILPDGFGFLRAAEASYLAGPDDTYISPSQIRRFNLRTGDHLSGRIRFPKDGERYFALSVVDSINGEPLEASKNKVLFENLTPLFPRKRFRLERGDGSTEDITGRILDLMAPQGKGQRALIVSPPKAGKTMMMQQVATAITHNHPDVHLIVLLVDERPEEVTEMQRTVRGEVVSSTFDEPAARHVQVAEMVIERAKRLVEHKKDVVILLDSITRLARAYNNVVPSSGKVLSGGVDANALHRPKRFFGAARNVEEGGSLTIIATALIDTGSKMDEVIYEEFKGTGNSEVHLNRRIAEKRVYPAIDINRSGTRREDLLIEPELLQKIWILRKLLHGMDEIGAMEFLLDKMKTTKSNDEFFSSMKR
>NZ_AP014940.1|WP_074870863.1|5665235_5665568_+|thioredoxin
MSEKVLHAGATDFDATVLQSSEPVLVDFWAPWCGPCKAIGPIVEQLAEQYDGRAKVVKVDVQEHPALGVRFNIRSIPMLMMFKDGQIHSTQLGAPPNIKTLLTQMIDKAI
>NZ_AP014940.1|WP_096381829.1|5680688_5681693_-|cytochrome-d-ubiquinol-oxidase-subunit-II
MDYWLPVIWFGVIGFGVLMYVLLDGFVLGLGILAPFAEDEKQLDHMMNTAAPIWDGNETWLVLGGVGLLTAFPKAYSLVLSALYLPVLLMLIALVFRGVAFEFRFKARRAKAAWGAAFSLGSLFCAFAQGVILGAIVEGMPMQEGKYVGGVFDWFSPFSMLTGAAVVFGYALLGSTWLVLKTEGRLQYIARTLARPLVLVVAVFIGLVSAWLPFLDSRIMARWFEGGNFYWLFPVPLLVIANAWALWRAVRREDRDGAPFLYSLGFFVLGFVGLVLGIWPNIVPGLTLWDAAAAPSSQMFVLGGMVILLPAILGYTYWSYRVFRGKVAADAGYH
>NZ_AP014940.1|WP_074870380.1|5681724_5683125_-|cytochrome-ubiquinol-oxidase-subunit-I
MDALLLSRIQFGFVISFHILFPAFTIGLASWLAFVEWRWLRTRDTLWRDLFFFWTKVFAVSFGMGVVSGIVMSFQFGTNWAVLSEQAGNILGPLLSYEVLTAFFLEATFLGVMLFGWNRVSERMHFLATCMVALGTLISTFWIISANSWMQTPTGHRIVDGVFVPDDWWAIVFNPSFPYRLAHMVLAAFITTCFVIGGTGASYLLRGIHVEAGKRMLKAAVLFAAITVPAQVFVGDLHGLNAREHQPIKVAAMEAHWESNPPGEGVPLILFAVPNEKAERNDLEVAIPKLGSLILTHTLDGDIQPLKSVPASERPPVKPVFYAFRVMVGLGMAMLALVACSLWLLWRKRLYQSRAVLWGWRVMIMSGFVAILAGWYVVEIGRQPYVIYGLLRTADAVSPVEAASVMTSLIVFAVVYFTVFGAGFRYLVKLIRKGPHPHEPPPRSAHGDKTPARPLSVPDESTEAGA
>NZ_AP014940.1|WP_096381838.1|5684137_5686540_+|S9-family-peptidase
MRPAYARLAALPLALLASAAFAQSAAAPTAPLILADTMADPDWIGPPVERAWWSWDGQRVQYQLKRDGAIIRDTWQTNAAGGAAQRLDGAARNDVDAVNPVYDAARSRMAFIRNGDVFVRDLRSGALTQVTRSNETESRPQFSRDGNLVFRVDNQWFQWRAGQGVSQAAQVLAQNDPAKAPKADALRDYQLATIDTLRNDRAQREASREQDEAWRKSDPSRAPRAVYLGSDVEIVDTALSPDGRYLLAVTQDKKGEAGTGGKMPKYVTESGYEEFEEVRTRVGRNEPLPQKLWLVDVATGKSSELKFDKLPGISEDPLAAMRKAAKKDALKGDRPVRIETDGDGRNAAVRWSDDGRHAGVLIRATDNKDRWIASVDLAGAALQARHRLNDKAWIGWDYNDFGWLPDGGLWLLSEQSGYSHLYVSDGGAAKPITSGKWEVSDPQLGADGKTFFFLCNRKWPGDYEVCAVDRNGGAVREVTALDGVENFALSPDGRKVLVRYSESYVPPQLAVVDASGEGAGEGRAVKLTDTRKDGFKQREWIQPEYVQVPSKHGAGTVWGKFYGPKNFDPGKKYPIVMFVHGAGFLQNVSERYPNYFREQMFHNLLVQQGYVVLDLDYRASQGYGRDWRTAIYRQMGHPELEDYLDGLDWLVANKQGDAGRAGIYGGSYGGFMTFMALYRAPGKFKAGAALRPVSDWSQYNHEYTSNILNTPELDPEAYKKSSPIEYAAGLQDNLLIAHGMIDDNVFFKDSVMMTQKLIELRKDKWEIAPYPLERHGFVHPDAWYDEYRRIYELFERTLKK
>NZ_AP014940.1|WP_096383802.1|5687029_5687944_+|oxygen-dependent-coproporphyrinogen-oxidase
MNDFDRVRDYLSGLQDRICAAIETADGGAGFNEDQWQRAEGGGGRTRILRGGRVFEQAGIGFSDVSGSKLPPSASAARPELAGASWRAVGVSLVFHPHNPYLPTTHANVRHFRAMRDGETVAWWFGGGFDLTPFYPFAEDVRHWHRTARELCEPYGGEERYQAHKRWCDDYFFLKHRNETRGVGGLFFDDLHGDFERDFGYMRAVGDGFLDAYLPLVDKRRDTPFGERERQFQLYRRGRYVEFNLVFDRGTLFGLQSGGRTESILMSLPPLVRWEYGFQPEADSDEAKLAQFLVPRDWLGEDAG
>NZ_AP014940.1|WP_096381843.1|5688589_5691355_-|DNA-polymerase-I
MKRLVLIDGSSYLYRAFHALPPLSNDAGEPTGALFGVVNMLRATLNERPDYVAFVVDAPGKTFRDDLDPNYKANRPPMPDDLRAQVLPMCEIVEALGIPILRIDGVEADDVIGTLALRANQDGIDVTISTGDKDFAQLVRPGVVLVNTMSGSRMDSDAAVIDKFGVRPDQIIDLLSLMGDSVDNIPGVEKCGPKTAAKWLGEYGSLDGVIEHAGQIKGKIGDNLRAALPRLPLNRQLATIKTDVELERGPDQLALRERDADVLRGLYARYGFKQALRELEGASTANDLASDRAGLRATAAGHARSGGAGETPDAALAVKGEYEAVTEQAQLDALVASLQAVEEFAFDSETDSLDPMQANLVGLSFASETGRAVYIPLGHDYPGAPAQLDREAVLAALRPVFADPARRKLGQHGKYDLHVLRRHGVEVAGYADDTMLESFVYNATASRHDMDSLAKRYLGYDTIKYSDVAGKGAKQILFSQVAIDDATKYAAEDADVTLRLHRVLGARLAAEPALEKVYREIEMPLVPVLARVEANGVMIDGDELRRQSQNLGKRMLEAQMKATELAGRTFNLDSPKQLQALLFDELKLPVLVKTPTGQPSTNEEALEAIADQHELPRVILEYRGLAKLRSTYTDKLPEMVNPHTGRVHTSYHQAGAATGRLASSDPNLQNIPIRTEDGRRIRRAFVAPAGRKLVACDYSQIELRIMAHLSQDEGLVRAFESGADVHRATAAEVFGKKSLDEVSANERRAAKAINFGLMYGMSAFGLARQLGIGRGEAQDYIALYFSRYPGVRDFMERTRQDARENGYVETVFGRRLYLENIKASNQGLRAGAERAAINAPMQGTAADIIKRAMIDIDGWLADHRERALMILQVHDELVFEADESFVPELLEQASRRMSAAATLRVPLVVDSGIGINWDEAH
>NZ_AP014940.1|WP_074870372.1|5691484_5691805_+|DUF2782-domain-containing-protein
MRAPLAPHAALAVAALLALAGCASTGGAAKAADPTAGLSNAEVRTHTVENGDTIEEYRVAGQLRVVKVVPARGPIYYLVDENGDGRLDTSKGEGTVSPVYFKLFSW
>NZ_AP014940.1|WP_096381848.1|5691908_5692337_+|GNAT-family-N-acetyltransferase
MTTIRTLSGDADLRAVWPLVSQLRPEFDEDRFVAQMHRQIAQGCRATVAFDEDGAPRAFACWRVMEMLAVGLHVYVDDLIVDQTVRSRGYGKAMLDWLKAEAKRLGCARLQLDSGTQRQDAHAFYLRERLRIEAFHFGVQLD
>NZ_AP014940.1|WP_145960214.1|5692703_5693261_+|hypothetical-protein
MTRMPGLRAVCVGGLSLALAALLAACGEPAANVAEPKAYDRLGVQVQIPGNWKLADDQRLGGVHYLTVESPGTAVFIAMVQSDRNRELEEFARSFSAEADKQLPNALEHQGRFDLSAFDQGTIREHYTVSLGGVKVPHLREYHKITGARRTAFLITQSADEDQAQAKPGFDLMLKSFKFNEAAGG
>NZ_AP014940.1|WP_096381857.1|5693352_5694600_-|phytase
MPKFSVLAAGLAAAATVAALVSCATPQAVRNDAGAPAPAIAADAGQREPDQRPAQAGDPLLAQAGIAHETVDEAFLTPATPQDNIDSPAIWRAPNGRLWLLATAKQGDALAIYDGDNGERVGRYGRSGAALGQFRRPNGIAVFGDLAFVVERDNRRVQVLQLSLPPARSAQPGVADRRTPQLRPLAAFGQAELQQPYGLWVRQRAPGTLEAIVTDAYMAGEDAAGEAIVPPLERLGRRLQRYELRVGAGAPQVRNLGAFGDTSADGAIRVPESVWGDPAHDRLLIAEEDLATGTALREYGLDGRYRGRTIGRELFKAQAEGIALWQCADGSGYWIATDQYKDRSLFHVFDRATLQHLGAFAGRSVGNTDGVWLQQVGSVRFPDGVFYAVHDDQAVGAFDWRDVARALGLRSRCEA
>NZ_AP014940.1|WP_096381862.1|5694774_5697126_+|TonB-dependent-receptor
MRSLQSTPFRRHHALCAALLAACGSPALAAEAELENERRATELDRVTVTGEIAYRDRSDATAPTLSYGLDYFQRFEPLTVGDMLKRVPSVGFVSDVLEYDGARLRGLDPGYTQILINGKKVPGAGGDRSFYVDRIPAELVERIEIVRSPSANRSGDAVAGALNIVLRDAYEFDGGYLRAGAMHFDDGKTKPVLGAVGSGEFAGGRLLGGVNVQGRHNPKRKRSDRFEAPGGDFVDREDQSDVRDGTDTSGNLSYTRDLGAGRLRLDGFYVRTDRTETEHSREYDHASSRARERLLSVNDQKVEIDQKNLVLSASYDFAMAGGRSEIDLGYARFDDDRFDTEQETGYDNEDSPPSFDGFEGTRILTDARDREFSLKLAHKREFGATHFEFGVDGVDKRRDSSLRTSEVEAKKEGQPLPPYAQFEHQRSRIQERRADPYAMLSGKNGRVDWETGLRYETTRAKIDLRSEENAPALRQDKDYNLLLPSAHLRFNPTEHDRFSASLARTVRRPDFDKLLPLTLEGEYGDNDFVGNPLLRPETAWGLDLGYERRLGRRGVVGLNLFYRKVRDLIEIAGTGRPSAKSLEDHEEAVEEFLDEHPGAGPATPGYPAFDPDSFLFTAANVGDGAAWGAEFDLSTPLTALGLEHTGVFLNYSWLDSEVEDEFGKRRFNNQPRFVLNVGFIQDLPEWGVSFGASYRRQGGAYSRVLGEEVGTDYGADLEAFVEKRFGSQIAVRLTGSNLLDASKDEAFHKFDTFGDQVGRDYDEYERETETAGPVYQLTVRYAF

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Crispr_ID: NZ_AP014940_14

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_14

5683641-5683759

Orphan

Consensus_repeat	Method
CCCGCGAAGGCGGGGATCTAGAGACTTCAGAGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP014940_14

>merge|NZ_AP014940|14|5683641-5683759|CRISPRCasFinder
CCCGCGAAGGCGGGGATCTAGAGACTTCAGAGCTTATGTCTCGACTCGGCACTCCCGCCAACCCGCACCCTCACCAGAACGTCATCCCCGCGAAGGCGGGGATCCAGAGACTTCAGAGC

>NZ_AP014940|14|14|5683641-5683759|CRISPRCasFinder
CCCGCGAAGGCGGGGATCTAGAGACTTCAGAGC	TTATGTCTCGACTCGGCACTCCCGCCAACCCGCACCCTCACCAGAACGTCATC
CCCGCGAAGGCGGGGATCCAGAGACTTCAGAGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_074870372.1\|5691484_5691805_+\|DUF2782-domain-containing-protein	unknown	unknown	gnl\|CDD\|378588
NZ_AP014940.1\|WP_145960211.1\|5668211_5668571_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096383802.1\|5687029_5687944_+\|oxygen-dependent-coproporphyrinogen-oxidase	unknown	unknown	gnl\|CDD\|235413
NZ_AP014940.1\|WP_096381857.1\|5693352_5694600_-\|phytase	unknown	unknown	gnl\|CDD\|271326
NZ_AP014940.1\|WP_096381821.1\|5674820_5678195_-\|ankyrin-repeat-domain-containing-protein	unknown	unknown	gnl\|CDD\|222980
NZ_AP014940.1\|WP_096381807.1\|5668679_5670488_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096381848.1\|5691908_5692337_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_AP014940.1\|WP_172437339.1\|5670754_5670919_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_074870360.1\|5697294_5699472_-\|DNA-helicase-II	unknown	unknown	gnl\|CDD\|236976
NZ_AP014940.1\|WP_096381829.1\|5680688_5681693_-\|cytochrome-d-ubiquinol-oxidase-subunit-II	unknown	unknown	gnl\|CDD\|224213
NZ_AP014940.1\|WP_145960215.1\|5699525_5700563_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|226483
NZ_AP014940.1\|WP_096381816.1\|5672675_5674517_+\|cation:proton-antiporter	unknown	unknown	gnl\|CDD\|235131
NZ_AP014940.1\|WP_145960212.1\|5671525_5672416_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096381838.1\|5684137_5686540_+\|S9-family-peptidase	unknown	unknown	gnl\|CDD\|224423
NZ_AP014940.1\|WP_074870385.1\|5678187_5678457_-\|YcgL-domain-containing-protein	unknown	unknown	gnl\|CDD\|377477
NZ_AP014940.1\|WP_074870380.1\|5681724_5683125_-\|cytochrome-ubiquinol-oxidase-subunit-I	unknown	unknown	gnl\|CDD\|376587
NZ_AP014940.1\|WP_096381862.1\|5694774_5697126_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657
NZ_AP014940.1\|WP_172437387.1\|5678715_5679111_-\|S8-family-serine-peptidase	unknown	unknown	gnl\|CDD\|173798
NZ_AP014940.1\|WP_096381843.1\|5688589_5691355_-\|DNA-polymerase-I	unknown	unknown	gnl\|CDD\|235591
NZ_AP014940.1\|WP_145960214.1\|5692703_5693261_+\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_074870372.1\|5691484_5691805_+\|DUF2782-domain-containing-protein	gnl\|CDD\|378588	pfam11191, DUF2782, Protein of unknown function (DUF2782). This is a bacterial family of proteins whose function is unknown.	2.80787e-17
NZ_AP014940.1\|WP_096383802.1\|5687029_5687944_+\|oxygen-dependent-coproporphyrinogen-oxidase	gnl\|CDD\|235413	PRK05330, PRK05330, oxygen-dependent coproporphyrinogen oxidase.	0
NZ_AP014940.1\|WP_096381857.1\|5693352_5694600_-\|phytase	gnl\|CDD\|271326	cd14956, NHL_like_3, Uncharacterized NHL-repeat domain in bacterial proteins. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.	8.60842e-05
NZ_AP014940.1\|WP_096381821.1\|5674820_5678195_-\|ankyrin-repeat-domain-containing-protein	gnl\|CDD\|222980	PHA03095, PHA03095, ankyrin-like protein; Provisional.	1.35656e-18
NZ_AP014940.1\|WP_096381816.1\|5672675_5674517_+\|cation:proton-antiporter	gnl\|CDD\|235131	PRK03562, PRK03562, glutathione-regulated potassium-efflux system protein KefC; Provisional.	0
NZ_AP014940.1\|WP_096381829.1\|5680688_5681693_-\|cytochrome-d-ubiquinol-oxidase-subunit-II	gnl\|CDD\|224213	COG1294, AppB, Cytochrome bd-type quinol oxidase, subunit 2 [Energy production and conversion].	2.99682e-87
NZ_AP014940.1\|WP_145960215.1\|5699525_5700563_+\|hypothetical-protein	gnl\|CDD\|226483	COG3975, COG3975, Predicted protease with the C-terminal PDZ domain [General function prediction only].	1.37117e-07
NZ_AP014940.1\|WP_096381848.1\|5691908_5692337_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	2.76077e-09
NZ_AP014940.1\|WP_096381838.1\|5684137_5686540_+\|S9-family-peptidase	gnl\|CDD\|224423	COG1506, DAP2, Dipeptidyl aminopeptidases/acylaminoacyl-peptidases [Amino acid transport and metabolism].	1.80589e-79
NZ_AP014940.1\|WP_074870385.1\|5678187_5678457_-\|YcgL-domain-containing-protein	gnl\|CDD\|377477	pfam05166, YcgL, YcgL domain. This family of proteins formerly called DUF709 includes the E. coli gene ycgL. homologs of YcgL are found in gammaproteobacteria. The structure of this protein shows a novel alpha/beta/alpha sandwich structure.	2.10278e-33
NZ_AP014940.1\|WP_074870380.1\|5681724_5683125_-\|cytochrome-ubiquinol-oxidase-subunit-I	gnl\|CDD\|376587	pfam01654, Cyt_bd_oxida_I, Cytochrome bd terminal oxidase subunit I. This family are the alternative oxidases found in many bacteria which oxidize ubiquinol and reduce oxygen as part of the electron transport chain. This family is the subunit I of the oxidase E. coli has two copies of the oxidase, bo and bd', both of which are represented here In some nitrogen fixing bacteria, e.g. Klebsiella pneumoniae this oxidase is responsible for removing oxygen in microaerobic conditions, making the oxidase required for nitrogen fixation. This subunit binds a single b-haem, through ligands at His186 and Met393 (using SW:P11026 numbering). In addition His19 is a ligand for the haem b found in subunit II.	0
NZ_AP014940.1\|WP_096381862.1\|5694774_5697126_+\|TonB-dependent-receptor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	3.64405e-54
NZ_AP014940.1\|WP_172437387.1\|5678715_5679111_-\|S8-family-serine-peptidase	gnl\|CDD\|173798	cd05562, Peptidases_S53_like, Peptidase domain in the S53 family. Members of the peptidase S53 (sedolisin) family include endopeptidases and exopeptidases. The S53 family contains a catalytic triad Glu/Asp/Ser with an additional acidic residue Asp in the oxyanion hole, similar to that of Asn in subtilisin. The stability of these enzymes may be enhanced by calcium, some members have been shown to bind up to 4 ions via binding sites with different affinity. Some members of this clan contain disulfide bonds. These enzymes can be intra- and extracellular, some function at extreme temperatures and pH values. Characterized sedolisins include Kumamolisin, an extracellular calcium-dependent thermostable endopeptidase from Bacillus. The enzyme is synthesized with a 188 amino acid N-terminal preprotein region which is cleaved after the extraction into the extracellular space with low pH. One kumamolysin paralog, kumamolisin-As, is believed to be a collagenase. TPP1 is a serine protease that functions as a tripeptidyl exopeptidase as well as an endopeptidase. Less is known about PSCP from Pseudomonas which is thought to be an aspartic proteinase.	2.17488e-15
NZ_AP014940.1\|WP_096381843.1\|5688589_5691355_-\|DNA-polymerase-I	gnl\|CDD\|235591	PRK05755, PRK05755, DNA polymerase I; Provisional.	0
NZ_AP014940.1\|WP_074870360.1\|5697294_5699472_-\|DNA-helicase-II	gnl\|CDD\|236976	PRK11773, uvrD, DNA-dependent helicase II; Provisional.	0

>NZ_AP014940.1|WP_074870380.1|5681724_5683125_-|cytochrome-ubiquinol-oxidase-subunit-I
MDALLLSRIQFGFVISFHILFPAFTIGLASWLAFVEWRWLRTRDTLWRDLFFFWTKVFAVSFGMGVVSGIVMSFQFGTNWAVLSEQAGNILGPLLSYEVLTAFFLEATFLGVMLFGWNRVSERMHFLATCMVALGTLISTFWIISANSWMQTPTGHRIVDGVFVPDDWWAIVFNPSFPYRLAHMVLAAFITTCFVIGGTGASYLLRGIHVEAGKRMLKAAVLFAAITVPAQVFVGDLHGLNAREHQPIKVAAMEAHWESNPPGEGVPLILFAVPNEKAERNDLEVAIPKLGSLILTHTLDGDIQPLKSVPASERPPVKPVFYAFRVMVGLGMAMLALVACSLWLLWRKRLYQSRAVLWGWRVMIMSGFVAILAGWYVVEIGRQPYVIYGLLRTADAVSPVEAASVMTSLIVFAVVYFTVFGAGFRYLVKLIRKGPHPHEPPPRSAHGDKTPARPLSVPDESTEAGA
>NZ_AP014940.1|WP_096381829.1|5680688_5681693_-|cytochrome-d-ubiquinol-oxidase-subunit-II
MDYWLPVIWFGVIGFGVLMYVLLDGFVLGLGILAPFAEDEKQLDHMMNTAAPIWDGNETWLVLGGVGLLTAFPKAYSLVLSALYLPVLLMLIALVFRGVAFEFRFKARRAKAAWGAAFSLGSLFCAFAQGVILGAIVEGMPMQEGKYVGGVFDWFSPFSMLTGAAVVFGYALLGSTWLVLKTEGRLQYIARTLARPLVLVVAVFIGLVSAWLPFLDSRIMARWFEGGNFYWLFPVPLLVIANAWALWRAVRREDRDGAPFLYSLGFFVLGFVGLVLGIWPNIVPGLTLWDAAAAPSSQMFVLGGMVILLPAILGYTYWSYRVFRGKVAADAGYH
>NZ_AP014940.1|WP_172437387.1|5678715_5679111_-|S8-family-serine-peptidase
MVLYNNVADPFPYSTGVAGSAGISGVAVSQGSGVALRSLAGQVATLNPTTVFDTHSYAVLSGTSMASPHVAGVAALLFAAKPSATAAQVRDAMTATALDLGAPGRDNEYGFGMVRAFEALDRLTATGTSAN
>NZ_AP014940.1|WP_074870385.1|5678187_5678457_-|YcgL-domain-containing-protein
MQAYVYKSLRKADTYVFLSARDDFARVPEPVLQQLGSLQFVLEVELGPERKLARADAATVRENLAARGFHLQFPPLPGMPVAEAAQPDA
>NZ_AP014940.1|WP_096381821.1|5674820_5678195_-|ankyrin-repeat-domain-containing-protein
MPDAPTSRALSKGFAIALAAGLALALATGFGGTSAGAVVALLGGALAQPAFALAARLWRRRDDRPDWKPELLNLSALWGGATAATAALAAWPLSALLQSGSLLAALGLSVVAGLLLLGLWRLWPLWTGTERDGAPLPPQWARLADLDLGAWRGLGVAGIVAGLVAVGLLLAWPGLLSTGARWTLAVAFALASPALHLLLQSIRAADPLPGLEFDPELDTVHASDELLDGDTGELSDAELAQALYAAARAGKVERALELIELGADVNAAPPADDERDRRSLSVLAAVLPDLRLLRGLIARGADLNATHAGMTPLLAATRDSWHGRPDAVMTLLANGADPRLADHEGNTPLHHAARSSDPGVAALLRDAQAELETLNHDGLSPLGVACASGNWRLAKFLLERGAKTEHAGGSPALLAAAGGDEDDPAGVQLLLKHKARIDARDGQRRSALHTAAFAGHLDIVTTLLAAGADAAAIDSQQRTPVLEAARGGRPGVLERLLEHLPHGGVEQAKALDADGASALILACQAETASPPLVLRLLELGLDPELRDRQGKRAVDRAAEAGRWSLVAALDRAYPLPAAVSGEGDADAPEGERVIVDRMPAALLRDGLREGRSSELTGLAKLLSPAELGAQLHEEDGQAPSAERIDWLLGQGADANVRNAAGDTVLFALLDRAPGSLPALHALLRHGVSPAGRGGLGRFLATCSAGEQAARGLEQFALDLIERGADVFARTPAGDPPLAIAVRMGWARLLERLLASGVDLNARDSHGMSALHLAAALGRENMLKRLVAHGAAPDLLAADGQTPLGVALASGRRDLADWLDWRGWPLPKRPLLAADVPAAAIVGDADAVRRLLDLGLSVDALDSQGCTALLRAAGGGHRAVVDLLLARGADPQRAANSGATPLSAAVSMRHGEIVDRLVAAGASLEQRLPGELTVLMVACALGLTDLAARLLAAGADVQARDAQGRMALHCAAMYGFTARERSRLVALFDTLLLAGVDADQSAAGATPLLLLLGARAEPGTAADEDVLIAGLELLLDHEASLDVQDPRGFGPLHLASLHGLLRVVQRLLRHGANPDQRDALNRTPREIAVMRGFVDIAAEFAPATPAGGTSGGVSMARFLRGGPGN
>NZ_AP014940.1|WP_096381816.1|5672675_5674517_+|cation:proton-antiporter
MHGGGLELALLFLLAAVIAVPVFRKFGLGAVLGYLAAGVVLGPYGVKVIADAEPVLAASEIGVVMMLFVIGLELSPSRLRVMRKPVFGAGGLQVILSGIALGALAMFGGGLGWKAATVVGLGLALSSTAVCLQLLSERKGLSADYGKLAFAILLFQDLAAIPLLAAIPLLGKAAGVDGLNWISVAKAVGAIAAVVFGGRVLLRQVFRVVARTQMPEVFTGAALLTVLGSAWILQTAGLSAGLGAFLAGVLLADSEFRHELESQIEPFKGLLLGLFFMAVGMSIDLQRVMNEPLTIGAIVLTLLTVKFALLFAVGISAGGLDKRGAFQLSTVMALGGEFAFVVFNEAFKAKLLDDPTRDRLIAAVGVSMALTPLLMIAAQRLLDSAPAAKPKRPYDEITDDHHPQVLLAGMGRFGQIVARLLVAHRTPFIAIENSAEQVDFMRRFGNMVYYGDPARPELLRSAGAAQVKVFVIAIDDRDACIRTVRTVRRLYPKAKVFARARDRRHSWELMDLGAEPMRETFHSSLKLGEDVLVELGVQPATARDHVERFRELDERMLNAQYLVHDDEDALMQSARDARKELEELFEADRGEGVLGGMVDKQATTVSSENTTRH
>NZ_AP014940.1|WP_145960212.1|5671525_5672416_-|hypothetical-protein
MKGMSRIAGTLLLAVLAVLALPATVAAQGVAAVRKQVEMSLVVVGQVRIAADGRVEGLQLDRESELPAPVVQLVRESVPRWRFDPLPADVPAQTAQTPMTLRVVLRPAPESAEPAAAQPQPASFVLRIVSARFGDTPADAMPRMLSAPPPRFPKDALGARMPATVYLVVRVGRDGRVVESFAEQVNLFALGSEQQMARFRQQFADTSLAAVKRWRFAPPTRGDEVGADSWQLRVPVDFLFDVRRPKPGTWRVYVPGPRQRAPWARETADSGVDAFADSGPQPIGGGRRLLSALGDG
>NZ_AP014940.1|WP_172437339.1|5670754_5670919_-|hypothetical-protein
MKTLMILFAALCLSACDPAFDQPPMLKGDKATTAKAASTAALPRLSTPTARIGG
>NZ_AP014940.1|WP_096381807.1|5668679_5670488_-|hypothetical-protein
MNAAVDSLPPAGVAPAGDPAAALRRYAGQGIPPGLPTAYTALLPADGQWGRETVMRAFVADALQRNGMVVDEDTLDATVAAATVPTGAFAGVEFEWKLQPGESRADGRPSPPFQGYSLQVPAAAQEELAAFAKEWAAQHDPHAPGSEDAPLRKLKGLAGAAGKSDVLETLEALDAAIKAGTTAQQAGKPLDAVALSAVLEFATRSGHEREAAKLLERYTAVKGITTDARELSQHAGRVFNGRDPVTGKALTADDRVNSAFDLLSGGFKLAGNIGSTALLMGAGNSGLVAGLIGVAPVGIAVVAFAAGAYQLIKHIREAILKPQWDEFRERFPFAEGMEPKQAITGVMRQIAGMPTDGRNALATATRIMEGMGENPETRERFLSFLKQKVQPESLVDALASGRGGQLTEQQAMLLAQAAKSSSKEFLDLELKDVKRYVKDRDGERERGTYLLPAAQQEAANRNGNKLGGAVEEGLRVAGILTSGANALNGQYRDLLDKLKGVDLPNKLGEQQQKNLAAALVPAVREGGLSQVDHLIPSKDGSRLFAVQGDPNSPDRRMVALDVEKGTQQSIETSSKLAAHHAANGGGGGQDPLQNQNQGGRGF
>NZ_AP014940.1|WP_145960211.1|5668211_5668571_-|hypothetical-protein
MVIEERVRSSSSLAELQDRIHGADRKAPVAHRTGPPARCFSLRPRCLRPGPIEKHRAGGLVRFRRVASSVGTRRASRIGRAALPAQRRLRSLAAFLCQNVTPCQNVIPAKAGIQGVIAA
>NZ_AP014940.1|WP_096381838.1|5684137_5686540_+|S9-family-peptidase
MRPAYARLAALPLALLASAAFAQSAAAPTAPLILADTMADPDWIGPPVERAWWSWDGQRVQYQLKRDGAIIRDTWQTNAAGGAAQRLDGAARNDVDAVNPVYDAARSRMAFIRNGDVFVRDLRSGALTQVTRSNETESRPQFSRDGNLVFRVDNQWFQWRAGQGVSQAAQVLAQNDPAKAPKADALRDYQLATIDTLRNDRAQREASREQDEAWRKSDPSRAPRAVYLGSDVEIVDTALSPDGRYLLAVTQDKKGEAGTGGKMPKYVTESGYEEFEEVRTRVGRNEPLPQKLWLVDVATGKSSELKFDKLPGISEDPLAAMRKAAKKDALKGDRPVRIETDGDGRNAAVRWSDDGRHAGVLIRATDNKDRWIASVDLAGAALQARHRLNDKAWIGWDYNDFGWLPDGGLWLLSEQSGYSHLYVSDGGAAKPITSGKWEVSDPQLGADGKTFFFLCNRKWPGDYEVCAVDRNGGAVREVTALDGVENFALSPDGRKVLVRYSESYVPPQLAVVDASGEGAGEGRAVKLTDTRKDGFKQREWIQPEYVQVPSKHGAGTVWGKFYGPKNFDPGKKYPIVMFVHGAGFLQNVSERYPNYFREQMFHNLLVQQGYVVLDLDYRASQGYGRDWRTAIYRQMGHPELEDYLDGLDWLVANKQGDAGRAGIYGGSYGGFMTFMALYRAPGKFKAGAALRPVSDWSQYNHEYTSNILNTPELDPEAYKKSSPIEYAAGLQDNLLIAHGMIDDNVFFKDSVMMTQKLIELRKDKWEIAPYPLERHGFVHPDAWYDEYRRIYELFERTLKK
>NZ_AP014940.1|WP_096383802.1|5687029_5687944_+|oxygen-dependent-coproporphyrinogen-oxidase
MNDFDRVRDYLSGLQDRICAAIETADGGAGFNEDQWQRAEGGGGRTRILRGGRVFEQAGIGFSDVSGSKLPPSASAARPELAGASWRAVGVSLVFHPHNPYLPTTHANVRHFRAMRDGETVAWWFGGGFDLTPFYPFAEDVRHWHRTARELCEPYGGEERYQAHKRWCDDYFFLKHRNETRGVGGLFFDDLHGDFERDFGYMRAVGDGFLDAYLPLVDKRRDTPFGERERQFQLYRRGRYVEFNLVFDRGTLFGLQSGGRTESILMSLPPLVRWEYGFQPEADSDEAKLAQFLVPRDWLGEDAG
>NZ_AP014940.1|WP_096381843.1|5688589_5691355_-|DNA-polymerase-I
MKRLVLIDGSSYLYRAFHALPPLSNDAGEPTGALFGVVNMLRATLNERPDYVAFVVDAPGKTFRDDLDPNYKANRPPMPDDLRAQVLPMCEIVEALGIPILRIDGVEADDVIGTLALRANQDGIDVTISTGDKDFAQLVRPGVVLVNTMSGSRMDSDAAVIDKFGVRPDQIIDLLSLMGDSVDNIPGVEKCGPKTAAKWLGEYGSLDGVIEHAGQIKGKIGDNLRAALPRLPLNRQLATIKTDVELERGPDQLALRERDADVLRGLYARYGFKQALRELEGASTANDLASDRAGLRATAAGHARSGGAGETPDAALAVKGEYEAVTEQAQLDALVASLQAVEEFAFDSETDSLDPMQANLVGLSFASETGRAVYIPLGHDYPGAPAQLDREAVLAALRPVFADPARRKLGQHGKYDLHVLRRHGVEVAGYADDTMLESFVYNATASRHDMDSLAKRYLGYDTIKYSDVAGKGAKQILFSQVAIDDATKYAAEDADVTLRLHRVLGARLAAEPALEKVYREIEMPLVPVLARVEANGVMIDGDELRRQSQNLGKRMLEAQMKATELAGRTFNLDSPKQLQALLFDELKLPVLVKTPTGQPSTNEEALEAIADQHELPRVILEYRGLAKLRSTYTDKLPEMVNPHTGRVHTSYHQAGAATGRLASSDPNLQNIPIRTEDGRRIRRAFVAPAGRKLVACDYSQIELRIMAHLSQDEGLVRAFESGADVHRATAAEVFGKKSLDEVSANERRAAKAINFGLMYGMSAFGLARQLGIGRGEAQDYIALYFSRYPGVRDFMERTRQDARENGYVETVFGRRLYLENIKASNQGLRAGAERAAINAPMQGTAADIIKRAMIDIDGWLADHRERALMILQVHDELVFEADESFVPELLEQASRRMSAAATLRVPLVVDSGIGINWDEAH
>NZ_AP014940.1|WP_074870372.1|5691484_5691805_+|DUF2782-domain-containing-protein
MRAPLAPHAALAVAALLALAGCASTGGAAKAADPTAGLSNAEVRTHTVENGDTIEEYRVAGQLRVVKVVPARGPIYYLVDENGDGRLDTSKGEGTVSPVYFKLFSW
>NZ_AP014940.1|WP_096381848.1|5691908_5692337_+|GNAT-family-N-acetyltransferase
MTTIRTLSGDADLRAVWPLVSQLRPEFDEDRFVAQMHRQIAQGCRATVAFDEDGAPRAFACWRVMEMLAVGLHVYVDDLIVDQTVRSRGYGKAMLDWLKAEAKRLGCARLQLDSGTQRQDAHAFYLRERLRIEAFHFGVQLD
>NZ_AP014940.1|WP_145960214.1|5692703_5693261_+|hypothetical-protein
MTRMPGLRAVCVGGLSLALAALLAACGEPAANVAEPKAYDRLGVQVQIPGNWKLADDQRLGGVHYLTVESPGTAVFIAMVQSDRNRELEEFARSFSAEADKQLPNALEHQGRFDLSAFDQGTIREHYTVSLGGVKVPHLREYHKITGARRTAFLITQSADEDQAQAKPGFDLMLKSFKFNEAAGG
>NZ_AP014940.1|WP_096381857.1|5693352_5694600_-|phytase
MPKFSVLAAGLAAAATVAALVSCATPQAVRNDAGAPAPAIAADAGQREPDQRPAQAGDPLLAQAGIAHETVDEAFLTPATPQDNIDSPAIWRAPNGRLWLLATAKQGDALAIYDGDNGERVGRYGRSGAALGQFRRPNGIAVFGDLAFVVERDNRRVQVLQLSLPPARSAQPGVADRRTPQLRPLAAFGQAELQQPYGLWVRQRAPGTLEAIVTDAYMAGEDAAGEAIVPPLERLGRRLQRYELRVGAGAPQVRNLGAFGDTSADGAIRVPESVWGDPAHDRLLIAEEDLATGTALREYGLDGRYRGRTIGRELFKAQAEGIALWQCADGSGYWIATDQYKDRSLFHVFDRATLQHLGAFAGRSVGNTDGVWLQQVGSVRFPDGVFYAVHDDQAVGAFDWRDVARALGLRSRCEA
>NZ_AP014940.1|WP_096381862.1|5694774_5697126_+|TonB-dependent-receptor
MRSLQSTPFRRHHALCAALLAACGSPALAAEAELENERRATELDRVTVTGEIAYRDRSDATAPTLSYGLDYFQRFEPLTVGDMLKRVPSVGFVSDVLEYDGARLRGLDPGYTQILINGKKVPGAGGDRSFYVDRIPAELVERIEIVRSPSANRSGDAVAGALNIVLRDAYEFDGGYLRAGAMHFDDGKTKPVLGAVGSGEFAGGRLLGGVNVQGRHNPKRKRSDRFEAPGGDFVDREDQSDVRDGTDTSGNLSYTRDLGAGRLRLDGFYVRTDRTETEHSREYDHASSRARERLLSVNDQKVEIDQKNLVLSASYDFAMAGGRSEIDLGYARFDDDRFDTEQETGYDNEDSPPSFDGFEGTRILTDARDREFSLKLAHKREFGATHFEFGVDGVDKRRDSSLRTSEVEAKKEGQPLPPYAQFEHQRSRIQERRADPYAMLSGKNGRVDWETGLRYETTRAKIDLRSEENAPALRQDKDYNLLLPSAHLRFNPTEHDRFSASLARTVRRPDFDKLLPLTLEGEYGDNDFVGNPLLRPETAWGLDLGYERRLGRRGVVGLNLFYRKVRDLIEIAGTGRPSAKSLEDHEEAVEEFLDEHPGAGPATPGYPAFDPDSFLFTAANVGDGAAWGAEFDLSTPLTALGLEHTGVFLNYSWLDSEVEDEFGKRRFNNQPRFVLNVGFIQDLPEWGVSFGASYRRQGGAYSRVLGEEVGTDYGADLEAFVEKRFGSQIAVRLTGSNLLDASKDEAFHKFDTFGDQVGRDYDEYERETETAGPVYQLTVRYAF
>NZ_AP014940.1|WP_074870360.1|5697294_5699472_-|DNA-helicase-II
MDVSHLLDALNPAQREAVSAPPGHYLVLAGAGSGKTRVLTHRIAWLNEVLGVPTHGILAVTFTNKAAGEMRARVDAQLARGARGMWIGTFHGLAHRLLRLHWQEAKLPEGFQVLDSDDQLRLVKRVVQALELDETRFPPRQIAWWINAQKDEGRRPRNIQPGGDDWQDVMLRCYEAYQERCERAGLVDFAELLLRAHELLRDNAALLAHYRTRFREILVDEFQDTNAIQYAFVRVLAGDSGHVFVVGDDDQAIYGWRGAKVENVQRFLRDFPDAQTIRLEQNYRSSGNILEAANAVIAHNPDRLGKKLWTDTGHGESIDLYAAYNEMDEARFVVERLRQWVRDGGSYGDVAVLYRSNAQSRAFEEALLSEQVPYRVYGGQRFFERAEIKDTLAYLRLIANRADDAAFERAVNTPTRGIGERTLDEVRKRARTDAVPLWEGARRVAGETVLAARARNALAGFALMIDTMQADVAEMPLQEKIDHVLQRSGLRDHYANESRGQLDSRTDNLDELVSVASRFSRSDEDEAAQMPELIAFLSYAALEAGEGQAQADEDGVQLMTLHSAKGLEFPLVFLGGLEEGLFPSGRSTEESGRLEEERRLAYVGITRAREKLVLSYAETRRIHGMDMYGVPSRFLREIPSPLLNEVRPKVQVSRPMYRAAPRRDMGHARIDESPIKLGAQVRHGTFGVGTVTDYEGDGAHARVQVNFDDVGSKWLVLAYANLQPA
>NZ_AP014940.1|WP_145960215.1|5699525_5700563_+|hypothetical-protein
MTRMHPRCGPIRQACACLAALALAWAMPVAAQAQAPAAAVAANAASERVLRVGDGRLRVIVENPPDPARADQLQAWLAECVRAQLSAFGRFPLREATVRVRLVPRRGRDPSPVPWGQTVREDGVSVLLFVRDDAGSEELRADWTAVHELSHLFHPYLGDAGRWLAEGLASYYQNVLRARIGLLDGEEAWRRLDGGFRRGRDAGAGPRMDEIGWRRGATMRIYWAGAAFWLDADLALRRERGRSLNQVLAAYSQCCLRENSRATPEEFVAALDRAGGGGTIARAYARHAAMTGFPSLQADYAALGIDTDGEQLTFSPDPAKARLRAAIMGPRAAVAVRSSAVDGDD

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Crispr_ID: NZ_AP014940_15

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_15

5741399-5741501

Orphan

Consensus_repeat	Method
TTCCGGCTTTCGCCGGAATGACG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP014940_15

>merge|NZ_AP014940|15|5741399-5741501|CRISPRCasFinder
TTCCGGCTTTCGCCGGAATGACGGGGTGGGAGTTTCGGGTCTTCGGGGGAGTTCGGCGGAGCTACGTCGCTGCGGCTGGATTCCGGCTTTCGCCGGAATGACG

>NZ_AP014940|15|15|5741399-5741501|CRISPRCasFinder
TTCCGGCTTTCGCCGGAATGACG	GGGTGGGAGTTTCGGGTCTTCGGGGGAGTTCGGCGGAGCTACGTCGCTGCGGCTGGA
TTCCGGCTTTCGCCGGAATGACG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_096381955.1\|5733089_5733401_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096382019.1\|5756404_5757289_+\|DUF2007-domain-containing-protein	unknown	unknown	gnl\|CDD\|378182
NZ_AP014940.1\|WP_172437340.1\|5738173_5738929_+\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|227044
NZ_AP014940.1\|WP_096381990.1\|5744912_5745656_+\|VIT-family-protein	unknown	unknown	gnl\|CDD\|153123
NZ_AP014940.1\|WP_096381999.1\|5746939_5747968_+\|LacI-family-DNA-binding-transcriptional-regulator	unknown	unknown	gnl\|CDD\|380518
NZ_AP014940.1\|WP_096382014.1\|5754577_5756353_+\|alpha-glucosidase	unknown	unknown	gnl\|CDD\|200469
NZ_AP014940.1\|WP_096381980.1\|5740066_5741014_+\|DMT-family-transporter	unknown	unknown	gnl\|CDD\|307170
NZ_AP014940.1\|WP_096383808.1\|5733409_5734519_-\|S-(hydroxymethyl)glutathione-dehydrogenase/class-III-alcohol-dehydrogenase	unknown	unknown	gnl\|CDD\|176260
NZ_AP014940.1\|WP_172437342.1\|5751574_5754382_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|224544
NZ_AP014940.1\|WP_096381961.1\|5734604_5734877_-\|formaldehyde-responsive-transcriptional-repressor-FrmR	unknown	unknown	gnl\|CDD\|197388
NZ_AP014940.1\|WP_096381995.1\|5745655_5746588_+\|ABC-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|181886
NZ_AP014940.1\|WP_096382005.1\|5748248_5749940_-\|cyclomaltodextrin-glucanotransferase	unknown	unknown	gnl\|CDD\|200478
NZ_AP014940.1\|WP_145960216.1\|5739046_5740000_-\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|182990
NZ_AP014940.1\|WP_096381950.1\|5732248_5733079_-\|S-formylglutathione-hydrolase	unknown	unknown	gnl\|CDD\|178061
NZ_AP014940.1\|WP_096381946.1\|5730922_5732083_+\|efflux-RND-transporter-periplasmic-adaptor-subunit	unknown	unknown	gnl\|CDD\|273776
NZ_AP014940.1\|WP_172437341.1\|5743338_5744916_+\|peptide-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|173869
NZ_AP014940.1\|WP_074872622.1\|5749936_5751439_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340871
NZ_AP014940.1\|WP_096381942.1\|5727710_5730926_+\|efflux-RND-transporter-permease-subunit	unknown	unknown	gnl\|CDD\|223911
NZ_AP014940.1\|WP_096383810.1\|5741702_5743064_-\|glutamate--cysteine-ligase	unknown	unknown	gnl\|CDD\|178221
NZ_AP014940.1\|WP_096381966.1\|5735153_5737925_-\|phosphoenolpyruvate-carboxylase	unknown	unknown	gnl\|CDD\|234570

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_096382019.1\|5756404_5757289_+\|DUF2007-domain-containing-protein	gnl\|CDD\|378182	pfam09413, DUF2007, Putative prokaryotic signal transducing protein. This is a family of putative prokaryotic signal transducing proteins of Pii-type.	9.88406e-13
NZ_AP014940.1\|WP_172437340.1\|5738173_5738929_+\|tetratricopeptide-repeat-protein	gnl\|CDD\|227044	COG4700, COG4700, Uncharacterized protein conserved in bacteria containing a divergent form of TPR repeats [Function unknown].	9.31531e-63
NZ_AP014940.1\|WP_096381990.1\|5744912_5745656_+\|VIT-family-protein	gnl\|CDD\|153123	cd02432, Nodulin-21_like_1, Nodulin-21 and CCC1-related protein family. Nodulin-21_like_1: This is a family of proteins closely related to nodulin-21, a plant nodule-specific protein that may be involved in symbiotic nitrogen fixation. This family is also related to CCC1, a yeast vacuole transmembrane protein that functions as an iron and manganese transporter. .	2.36422e-94
NZ_AP014940.1\|WP_096381999.1\|5746939_5747968_+\|LacI-family-DNA-binding-transcriptional-regulator	gnl\|CDD\|380518	cd06295, PBP1_CelR, ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators. This group includes the ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators. The binding of CelR to the celE promoter is inhibited specifically by cellobiose. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.	5.03787e-109
NZ_AP014940.1\|WP_096382014.1\|5754577_5756353_+\|alpha-glucosidase	gnl\|CDD\|200469	cd11330, AmyAc_OligoGlu, Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.	0
NZ_AP014940.1\|WP_096381980.1\|5740066_5741014_+\|DMT-family-transporter	gnl\|CDD\|307170	pfam00892, EamA, EamA-like transporter family. This family includes many hypothetical membrane proteins of unknown function. Many of the proteins contain two copies of the aligned region. The family used to be known as DUF6. Members of this family usually carry 5+5 transmembrane domains, and this domain attempts to model five of these.	3.32296e-05
NZ_AP014940.1\|WP_096383808.1\|5733409_5734519_-\|S-(hydroxymethyl)glutathione-dehydrogenase/class-III-alcohol-dehydrogenase	gnl\|CDD\|176260	cd08300, alcohol_DH_class_III, class III alcohol dehydrogenases. Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.	0
NZ_AP014940.1\|WP_172437342.1\|5751574_5754382_-\|TonB-dependent-receptor	gnl\|CDD\|224544	COG1629, CirA, Outer membrane receptor proteins, mostly Fe transport [Inorganic ion transport and metabolism].	1.32841e-18
NZ_AP014940.1\|WP_096381961.1\|5734604_5734877_-\|formaldehyde-responsive-transcriptional-repressor-FrmR	gnl\|CDD\|197388	cd10153, RcnR-FrmR-like_DUF156, Transcriptional regulators RcnR and FrmR, and related domains; this domain family was previously known as part of DUF156. This domain family includes various transcriptional regulators that respond to different stressors. It includes Escherichia coli RncR (formally known as YohL, nickel and cobalt-sensitive), and E. coli FrmR (formally known as YaiN, formaldehyde sensitive). Escherichia coli RncR represses expression of the gene encoding the nickel and cobalt-efflux protein RcnA; RcnA may act through modulating NikR, to repress the NIkABCDE nickel transporter. In vitro, purified RncR binds to the rncA promoter DNA fragment in the absence of Ni2+ or Co2+, and the affinity of RncR for this promoter is reduced in the presence of excess nickel. Escherichia coli FrmR regulates the formaldehyde degradation frmRAB operon. This family belongs to a larger superfamily that includes CsoRs (copper-sensitive operon repressors). CsoRs form homotetramers (dimer of dimers). In Mycobacterium tuberculosis CsoR, within each dimer, two Cys residues on opposite subunits, along with a His residue, bind the Cu(I) ion (forming a triagonal S2N coordination complex, C-H-C). These residues are conserved in the majority of members of this superfamily. In this family, however, not all these residues are conserved; in E.coli RcnR and FrmR there is a His or a Thr instead of the second Cys (C-H-H or C-H-T) respectively. For E. coli FrmR, an N-terminal His residue, not conserved in all members of this family, is also involved in metal binding (H-C-H-H). A conserved Tyr and a Glu residue that facilitate allosteric regulation of DNA binding for CsoRs are poorly conserved in this family.	2.19021e-38
NZ_AP014940.1\|WP_096381995.1\|5745655_5746588_+\|ABC-transporter-permease-subunit	gnl\|CDD\|181886	PRK09471, oppB, oligopeptide ABC transporter permease OppB.	7.31124e-112
NZ_AP014940.1\|WP_096382005.1\|5748248_5749940_-\|cyclomaltodextrin-glucanotransferase	gnl\|CDD\|200478	cd11339, AmyAc_bac_CMD_like_2, Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.	3.17545e-136
NZ_AP014940.1\|WP_145960216.1\|5739046_5740000_-\|LysR-family-transcriptional-regulator	gnl\|CDD\|182990	PRK11139, PRK11139, DNA-binding transcriptional activator GcvA; Provisional.	7.64283e-36
NZ_AP014940.1\|WP_096381950.1\|5732248_5733079_-\|S-formylglutathione-hydrolase	gnl\|CDD\|178061	PLN02442, PLN02442, S-formylglutathione hydrolase.	3.89908e-139
NZ_AP014940.1\|WP_096381946.1\|5730922_5732083_+\|efflux-RND-transporter-periplasmic-adaptor-subunit	gnl\|CDD\|273776	TIGR01730, COG0845:_Membrane-fusion_protein, RND family efflux transporter, MFP subunit. This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate].	6.2517e-55
NZ_AP014940.1\|WP_172437341.1\|5743338_5744916_+\|peptide-ABC-transporter-substrate-binding-protein	gnl\|CDD\|173869	cd08504, PBP2_OppA, The substrate-binding component of an ABC-type oligopetide import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding component of an ATP-binding cassette (ABC)-type oligopeptide transport system comprised of 5 subunits. The transport system OppABCDEF contains two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	5.238e-177
NZ_AP014940.1\|WP_074872622.1\|5749936_5751439_-\|MFS-transporter	gnl\|CDD\|340871	cd17313, MFS_SLC45_SUC, Solute carrier family 45 and similar sugar transporters of the Major Facilitator Superfamily of transporters. This group includes the solute carrier 45 (SLC45) family as well as plant sucrose transporters (SUCs or SUTs) and similar proteins such as Schizosaccharomyces pombe general alpha-glucoside permease. the SLC45 family is composed of four (A1-A4) vertebrate proteins as well as related insect proteins such as Drosophila sucrose transporter SCRT or Slc45-1. Members of this group transport sucrose and other sugars like maltose into the cell, with the concomitant uptake of protons (symport system). Plant sucrose transporters are crucial to carbon partitioning, playing a key role in phloem loading/unloading. They play a key role in loading and unloading of sucrose into the phloem and as a result, they control sucrose distribution throughout the whole plant and drive the osmotic flow system in the phloem. They also play a role in the exchange of sucrose between beneficial symbionts (mycorrhiza and Rhizobium) as well as pathogens such as nematodes and parasitic fungi. There are nine sucrose transporter genes in Arabidopsis and five in rice. Vertebrate SLC45 family proteins have been implicated in the regulation of glucose homoeostasis in the brain (SLC45A1), with skin and hair pigmentation (SLC45A2), and with prostate cancer and myelination (SLC45A3). Mutations in SLC45A2, also called MATP (membrane-associated transporter protein) or melanoma antigen AIM1, cause oculocutaneous albinism type 4 (OCA4), an autosomal recessive disorder of melanin biosynthesis that results in congenital hypopigmentation of ocular and cutaneous tissues. The SLC45 family and related sugar transporters belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	3.20144e-67
NZ_AP014940.1\|WP_096381942.1\|5727710_5730926_+\|efflux-RND-transporter-permease-subunit	gnl\|CDD\|223911	COG0841, AcrB, Cation/multidrug efflux pump [Defense mechanisms].	0
NZ_AP014940.1\|WP_096383810.1\|5741702_5743064_-\|glutamate--cysteine-ligase	gnl\|CDD\|178221	PLN02611, PLN02611, glutamate--cysteine ligase.	0
NZ_AP014940.1\|WP_096381966.1\|5735153_5737925_-\|phosphoenolpyruvate-carboxylase	gnl\|CDD\|234570	PRK00009, PRK00009, phosphoenolpyruvate carboxylase; Reviewed.	0

>NZ_AP014940.1|WP_096381980.1|5740066_5741014_+|DMT-family-transporter
MSTAPLTATAAVAARPLLLRAGLMAAASTSLALLALLSRYTRGLAPELVTWGRFILPALILTAFVRGPDWRAAWSLADRPGWVRALCAVIAQVCFVFAATQGDLLQAVLLYNTGPLFIPLVAWLWLGERLRPATLAGLALGFLGVLAVLQPGTRGLDPLALIALTGGLAMAVSQVLFYRSAQRQPPLRNQFKLYTQASLLSLPLAALGAAHTPWGAVLAGEAASEPVWVLSLALLGMTACSLGNQSLRDLAYRGMDNASTLAPLMYVAVPVSAALDWLLFDRVAAPSALLGAALVVVGAVVALRSGARAQRAEAS
>NZ_AP014940.1|WP_145960216.1|5739046_5740000_-|LysR-family-transcriptional-regulator
MTTKPGSLPPGSGDDAPARRLPPLRALQAFAAVVRHDGMRRAAERLHLSHAALSQHVQHLEEAFGLRLLDRSGGRARPTPLGREFGEALIDGFERIEAATARLRLRGDESRRLQLGAPTSLSVSLLLPRIEEFSARAGFELQLFCPAGPADLAQARVHALLMHREPAEHGLRGELLFEQALLPVASPGLLARLDPQRWWLDPVPGARLLHVVSDGWREDWPAWFGADTAAWPLPQLSLSSPMPAISAALAGQGIALLYPRLIAERLASGELAPLPLPQPAPVKRLYLAWLPEAEGAARLQWVRDWVVALLRGEDGGG
>NZ_AP014940.1|WP_172437340.1|5738173_5738929_+|tetratricopeptide-repeat-protein
MPYFGLGLHVVVALYFAVHAVRSGQDRYWLMVLFMFPLLGSVVYAFAIWLPEQRHSRHGRALVGNVRRMLDPGRELRQAQDAFDDSATTDNRLRLADALLGAGRAGDALPLYRAALSGVHREDPHIQVKLAHALLEAGEPAQARQLLDELIAKRPDFRSPEGHLTYARAVAAQGDKSNAKEEFEALTAYSSGFEAHAYYVECLIGWGDTGRARELCEQAQAKARRLPAYARKMHRVELDKLRELEKRAQAL
>NZ_AP014940.1|WP_096381966.1|5735153_5737925_-|phosphoenolpyruvate-carboxylase
MTDSSDEPLRAAEWAEQAAERAADFAPTDALLREDVKTLGALVGEILAEQRGQGFLDGVERLRRAAIRRREAGEPIDALAAALVDIDLEQAADLVRAFATYFQAVNLAERVHRIRRRRDYERSGAGAQPGGLRDALATLARQGVSAEEVAALLPRLRIEPVFTAHPTEAVRRALLEKERTIVECLVADIDRGRTPPERRADRERIRLALTASWQTAEAPAAKPSVADEFEHVGFYLSDVLYRVLPVYYEVFEEALRETYGGAPALPDVLGFGTWVGGDMDGNPNVGADTIAATLAGQRALVLAAYRRDLASLEELLSQSVHRVRVDDAVLAKVEDYRYLLPKAAALLKPRHADMPYRNLLGLMSARLQATLEESVHGYPDAAAFLADIDLIERSLAAHQGAHAGGFAVRRLRRRAECFGFHLAGLDLRQDSATHDAALAALFEQPEWAALDVAARAARLHQLLDGEAPPARPAAAAAQPTLDVFRAVARLRPRFGARAFGPYIVSMSRSAADALAVLALARTAGCADDKGRVPLDVAPLFETVDDLDAAADTLRALFSDPVYRDHLCSRGDRQVVMLGYSDSAKDGGMVASRWALQQTQIALTALAADSGVRIAFFHGRGGSISRGGGKTERAVIAAPRGSVDGYLRLTEQGEVIHRKYGIRALALRNLEQTSGAVLRATLRPRAPEPREAGWRRIAGELAGEARAHYRALVHEDPQFPAYFRAATPIDVIERLRIGSRPAKRAGSGDISSLRAIPWVFAWSQNRAGLTAWYGVGTGLAAALDRHGRDTLAEMARDWPFFGTLIDDLEMVLAKSDPAIFERYSQLASALPDGDLHARFHPSIAAEFERTRDAVLAIKGSDELLRGDHRLRQSIRLRNPYVDPISLLQVDLLARWRAADRPDDALLQALVATVNGIAAGVQNTG
>NZ_AP014940.1|WP_096381961.1|5734604_5734877_-|formaldehyde-responsive-transcriptional-repressor-FrmR
MPHSPAEKKRVLTRVRRIKGQTEALERALEAGSECAAVLQQIAAIRGAVNGLMSEVLESHIREELGQAVADRGRDASIDEIAALVRSYLK
>NZ_AP014940.1|WP_096383808.1|5733409_5734519_-|S-(hydroxymethyl)glutathione-dehydrogenase/class-III-alcohol-dehydrogenase
MKSRAAVAFAAGEPLKIVEIDVQPPKAGEVLVRIHATGVCHTDAFTLSGDDPEGLFPAVLGHEGGGVVVEVGEGVTSLKPGDHVIPLYTAECRKCKFCLSSKTNLCQAVRATQGKGLMPDGTTRFSYEGQPIHHYMGCSTFSEYTVVPEISLAVVNPEAPLEKVCLLGCGVTTGIGAVHNTAKVQPGDTVAVFGLGGIGLAVIQGAVQAKAGRIIGVDTNATKFELAKSMGATDCVNPKDFDRPIQEVLVEMTDGGVDFSFECIGNVEVMRSALECCHKGWGESVIIGVAGAGQEIKTRPFQLVTGRVWRGTAFGGVKGRTQLPGMVEQAMKGEIDLDPFITHTLPLERINEAFDLMHEGKSIRTVIHY
>NZ_AP014940.1|WP_096381955.1|5733089_5733401_-|hypothetical-protein
MKNIQVIDSAINCVYDVFALDEAEFDLLFPPGQDIAFIDEVLARHPPHVLEPVFERLWRNRVPKREAMGLHGLLFYDLDEKKPFYPQRADELAVNPNGSPLRR
>NZ_AP014940.1|WP_096381950.1|5732248_5733079_-|S-formylglutathione-hydrolase
MEKIESHGCFGGRQQVWSHTATTLGCTMRFGVYLPPQAESGDCPVLYWLSGLTCTEQNFITKSGAQRYAAEHGLILVAPDTSPRGEGIPDAEGYDLGIGAGFYLNATRPKWAGHYRMYDYVVDELPALVDAHFPTTSARAISGHSMGGHGALTIALKNPGRYRSVSAFSPIAAPSQSPWGEKAFSAYLGEDREAWLEWDATALVGGAKERLPLLIDQGGDDEFLATQLKPELLRTACEVAGHPLQLRLRPGYDHSYYFISTFIGEHIAHHAKALRG
>NZ_AP014940.1|WP_096381946.1|5730922_5732083_+|efflux-RND-transporter-periplasmic-adaptor-subunit
MNRSIPTQATVRAPSLRTALSLAVAGLVLAAATGCGRSEAETAQAPATPEVLTVQAKPADAAYDLSLPARAQAGESAALYARATGFVSERKVELGDKVGAGQVLATISAPEIDQAVREARAVLAQTTADEELAKINFQRAQQLIGTGAVSKEYFSDRKGTFDVAVAARNAAQARLTSALERQSFTAVRAPFAGVVVARNIERGDRVVGDSATATVPMFEVAVLDPLRVVVDVPQNVSLQIQNGLQAEVTFPELPGQVFKAEVARSARALSRDAGVMRTELRLPNPDGRIPAGMVGSARLHLPRAAAAVVLPVSTVVQRAAGTQIATVTQGSTLAYRDVTLGRNLGNEIEVLTGIAPGDTVVLAPNALLADGNKVSAKALPPPAKKS
>NZ_AP014940.1|WP_096381942.1|5727710_5730926_+|efflux-RND-transporter-permease-subunit
MWIVQYALSRRYTIGVLAILILLFGVLSARKMPTDILPEVGIPSVNLVWTYSGLPAADVAAKMTSFSEAAILNTVDDLKEVRSETLNGASIVRIDFQPTVSLDRALVQITSVSQTILRRMPPGTSPPLVVRNNVSSTPVLQLVLSSDSLTEAQLYDYARLQLRSQIQTIPGIRMTLPYGGAPRQIMVDLDPARLQTYGLTPADVTAALERGSPTLPSGSIREGAREMQISIDTSPATATEFLDIPVASRAGTVIYVRDIASVRDGGALQTNVARMDGSSAVSVALIKLGGASAVEIVRAVRERLPEIEASAPPGTRIHAIFDQSVFVDNAIGSIQHEAMLVGLLVALVVLVFIGSWRSSLIVLSAIPLALLASVAMLHLLGYTFNVMTLGGLALAIGILVDNAVVDVENTNRNIALGKDVRTAILDSAKEVVFPEMVSTISICIVLTPILLMTGLSAWVFTPLALAVIFAMLASFLLSRTLIPVLCYLLLPADIQSRANPRWAPEKLLLNINHKVEHTLDSLREKHHALLVKLGHHGGVLALTALLVFALGAGAAMSLGREYFPQVDAGQLRLQVRLPTGTRLEETAAKLSEIQREIRAIIPPAELQTVYEQIGVPDAINLSLVDSTVVGSFEAEIMLQLRSPHANSHDYLVKIRKRIAERFPDVKLFERPPDATSRTLAGSAAAAFEVRLIGRDVPGNMALAREIEKRLHQVPGAVDIALRQVLDLPEYQVKIDRTRAAQLGLDPQQAARAVLAVLGSAGTVSPVYWTDTVNAIAYTVQVQAPLNQMQNIDQLMNSPLRIGANGEAVLLRNIATVTPRNVPASIARTTLAPTISVIANVEGTDLGSVYDKLSAITKELNGQLKPGNRIEIVGQAGEMQNAYGELAAGLVMSAILVFLVLVVNFQSWIQPAVAMSGLPIAIAGAAVGLFVTGTPLSVPALMGVMMVIGVSTANSVLVTSFARGLIADGHDPELAAYESAAVRLRPVLMTASAMILGIVPMAIGLGDGGEQNAPLGRAVIGGLLFGTPATLILVPSILAVVGRRRKPAGGEDATTDTTAAAPGDGTPAGANA
>NZ_AP014940.1|WP_096383810.1|5741702_5743064_-|glutamate--cysteine-ligase
MKDLEIPDVKGGGRAVLIDYLASGARPESDWKIGTEHEKFGFRTDDLRPPTFDGERGIEALLKGLVQFGWAPVEENGRVIALTRDQASVSLEPAGQLELSGAPLATLHDTCVEAATHLREVRTVAEPMGLGFLGMGFQPKWRREDMPWMPKGRYKIMRDYMPKVGQLGLDMMTRTSTVQVNLDVRDEADMVKKFRVSLALQPIATALFADSPFLEGRPNGYLSYRSHIWTDTDADRTGLLDFVFEDGFGYERYVDYLLDVPMYFVYRDGRYIDASGQSFRDFMDGRLPAYPDQRPTLKDWADHSTTAFPEVRLKKYLEMRGADSGPWNRICALSAFWVGLLYDAEALDAAWDLVLDFTPEERHALRDGVPRHGFQLPFRDGKVLELARRALEISAHGLKRRGRLNGNGADESIYLEPLMEFVAMGKSPAERKLELFHGEWDGNVDRVFREFAY
>NZ_AP014940.1|WP_172437341.1|5743338_5744916_+|peptide-ABC-transporter-substrate-binding-protein
MPAVPAQPAHAAAAQLERGNGPEPSTLDAHRCQEVACGNVLRDLYEGLVTEDAQGRLVPGLAERWTVSADGRTWTFALRPGLRWSNGEALDAAQVVASFRRAFAPATAAPFGELFDALDGAQAVQAGDLPPERLGVSAPDPHTVVFRLTRSASLPALLTLPIAFPVYLPAVQKYAAQHTQPGRLVSNGAYRLAAWTPQANLVVEKNPNFHDAARVALPRVRFHVTEDAAAELQRFAAGDLHITEVVPPQPLAALRERFGEQLRLSPYLGAFWFGLNTTQPPFRPACASARCGEQALALRRALTMAIDRDKLTRYVTGLGETPAYGIVPPGIAGYAPAAMPWASWTQAQREAHARALYRHAGYSDEHPLVLELRYNTSTPHRRLALAVAAMWKQTLGVQVRLRNEEWKVFVQNRKQRAITQAFRGGWIGDLPDARNFLAAFANDGPLNWMGYDDAGYRERLARADAAATQAARNAWLRAAEQRLLNDNAAIPLYFYTSKHLVSRRVRGFEPNALDRHASRWLSLTP
>NZ_AP014940.1|WP_096381990.1|5744912_5745656_+|VIT-family-protein
MTTQPAPSPPARPRAHARSRHPEAHRSERVGWLRAAVLGANDGIVSVAGLVVGVAASGADAGAILTSGIAGTVAGAMSMAAGEYVSVRSQADTEHADIAVEKRELAENPHAELEELAHIYVQRGLTPELAREVARQLSEHDALASHARDELGITDTLRARPVQAALASAAAFISGAALPIAAVVLAPHSQVQPAAIATTLAALSVSGALAAWAGGAPVLRGALRVMFWGALAMAAATAVGHLFGVQV
>NZ_AP014940.1|WP_096381995.1|5745655_5746588_+|ABC-transporter-permease-subunit
MRAHPRLLRLGGRLLEAAITLWLLGTLCFVLLRAAPGGPFDTEKAAPPEVQAVLDAQYRLDQSLPMQYLGWLGDALRGDLGPSFQYPDYTVNQLIANALPVSALNGGLALLLALLCGVALGAWAALRAGGWSDRALMFLAGLGLAIPKFVVAPLLVLLFAVTLHWLPAGGWGEWDNVVLPVIALALPNIAYCARLTRASLLDTLSADYLRAARARGLSETRLLFAHALKPALLPVAAWLSPALINVVTGSAVVEQVFGIPGMGRYFVQGALNRDYTLVLGVVLVIGALIVAINVAVDALRGWMDPRLEQD
>NZ_AP014940.1|WP_096381999.1|5746939_5747968_+|LacI-family-DNA-binding-transcriptional-regulator
MRKKTKATSVDIAHLAGVSQATVSRVLSGSPLVNAETRKRVEAVVRELNYKVDRHASSLRRQRSGTLALLLFEDPTPDESHINPFFLSMLGSITRACARHGQDLLISFQQLSDDWAADYEDSMKADGLILLGYGDYLAYQGKLQRLVEQGTRFVRWGAVLPDQPGLSIGCENLGGGRQAGAHLVALGRRRVAFLGDASSHYPEFLDRFLGCEQALHEAGLALDRTLQVDAESSEDAGHAAALELLARELPFDAVFAASDLIAIGAMRALTERGLRVPEDVSVIGFDDLPTARFAHPPLTTVFQDTKQAGELLVEALMQLIRGEPAQSQRLPTTLVVRKSCGG
>NZ_AP014940.1|WP_096382005.1|5748248_5749940_-|cyclomaltodextrin-glucanotransferase
MRALALAALSLTLAACVHGGAAREAAARRDYYGTLEPMASEAVYFVVTDRFVNGDPGNDQRAQGGPDPDTRSFDRPVPGGPPGESDNIGYLGGDFKGLLDNAGYIRDMGFGAVWLTPIVDNPDQAFTGGDAVTWGGAFQDRGKTGYHGYWGVDFYRLDEHLPSPGLDFAGLTRGMKQHGLKTVLDIVANHGSPSFTMRKPQPKYGRIYRDGVLVADHQNLPPERLDPAHNPLHRFFHNERDLVQLSNIDDTNPEVMEYFVGAYSQWIDQGADAFRIDTIRHMPLAFWRVFAERIRAKRPGFFMFGEAFDYKAENIAPFTWAENGGVSVLDFPLKERLAEVFGRTRADYARLDERLYLQDGPYANPYELMTFYDNHDMPRLDASDEGFIDAHNWLFTARGIPVIYYGSEVGFERGRAEHAGNRNYFGQPRVDAARSHPIRLALKRIAEVRRQSPALQRGLQLNVSLQGERAAFYRVYEHGDTAQIALVLLNKGDAPAPFAVSEYLQAGRWRAALGGGEIAVGEGGTLRASVPAHGVEVYLLDAPVRRADLAAALDQAMAHARKR
>NZ_AP014940.1|WP_074872622.1|5749936_5751439_-|MFS-transporter
MTDRPDATPRKPTLTFWQIWNMCFGFLGIQFGFALQNANVSRIFQTLGAPIDDIPMLWIAAPLTGLIVQPIVGYLSDRTWTGLGRRRPYFLVGAILATLALIAMPNSPTLWIAAGLLWMLDASINVSMEPFRAFVGDQLPQQQRAAGYAMQSFFIGVGSVVASLLPYLLAHFGVGNTAAAGEVPDTVRYSFYFGGAVLLLSVGWTVLRSREYPPQQLQAYDEAPPIEPSPERDRVRCLLFGASWMVIGGICATAISMLRLDRQLYVLAALIAAFGVALLARGIVRDGGGFATVMDDLGAMPAAMTRLAVVQFFSWFALFSMWIYTTPAVTQLHYHTSDVASAAYNEGANWVGVLFAAYNGFAALAAIAIAPMARRWGLRRSHLFNLTLGGAGLISVALVRDPQMLLLSMVGIGFAWASILSLPYAMLSDSVPAAKMGVFMGIFNFFIVIPQLVAASLLGFLVRHLFGGHPVAALVIGGVSLFVAGACTLWVREPDAQVRA
>NZ_AP014940.1|WP_172437342.1|5751574_5754382_-|TonB-dependent-receptor
MSHSKPAARGPKQLDRHLLTLALAALGLCGFAPAWAADAPAPQDSAPAAAAAPQTAHELDAVQVTGNRRVQSIQKYAGTIQSFSGEDIAKLGINTDFRNLQAVVPGLQITKQEGKYEIFLRGIGAADSDFSSDPSVATYYNGIYLPRPRSIGPMFFDVERIEVNKGPQGTVRGRNATGGSINVISKRPELGVTSGGLKIGAGNYDYTNAEGVLNLPIGDTFALRAALFDEERSSYITNGYPKSLFSAEGPSALDNQAARLSALWQPNDKFSAYVMLDKVTERGTGDPGLFAERGLAAGYDIKDLDDPFKQYFRTQGKTTNDIEGIAATFTYAFNDAVSVEFNTSYRKYDFYNRNASREWQLGPVYPGSDREAYFNPERLDWYDTFYQADKSSSRINELRFFGDTGKLIWSAGLFNYEEKYDYVSWDVGNGYFGDCDWWRPGTVCGYQDGLGGENRGDNSKVESNAVYGDFSFAATDSLRLIGGIRYTRDKKIARESNVKYQFIIPEELFQQFTGQPINTSTNPYTTGLILGSPGFQLAGPGRRRGGDPSICTGWSPADLRCGPGGNTLDYFLGGFQNFGANDNWAQFLQKNRDQIQVIARSDFPNGRSEDVYKDNYVDWRVGFEYDLAAKVMLYGTVSTGTRAGGINRPLTLNDGSALAPSFAPEELTAYEAGIKGDYVWGETPVRLNASVFYYDYKNKVLQNLIDVPAPTPTNPNATSRQVFNDNAANASVLGLELEGKVGLPHGFDIGYNFTYLDATFDDSKVLDTRSGGLGLIVPLDGNRLPNTSKYNANVSLSQTIDIGRGALNSFDWTINLTYRSDYYLTAFNSRGFGLDANGKVIEIPLKDMPFNNGSNPAAGGGPANGLAMRDDVDGFFTVNVSAGLNFGSENQFRVDGFVSNLTDEVYSGKGFVNNSTNIRYLNTPRMYGIRFASQF
>NZ_AP014940.1|WP_096382014.1|5754577_5756353_+|alpha-glucosidase
MQAPRPSRTAAVSWRASPQRSVVARRAIEPLYAAVLQKQGSHLSAAVSSQPAQRDPSWWRGAVIYQVYPRSFRDLDGDGVGDLPGIVEKLGYIADLGVDAIWISPFFKSPMADFGYDIADYLAVDPLFGNLEDFDRLLAKAHALGLKVMIDQVLSHTSNEHEWFKRSRESRDNEFADWYVWADARADGTAPNNWMSLFGGVAWRWEPRRQQYYLHNFLSAQPDLNFHHPAVRAAVLDNVRFWLERGVDGLRLDAINFCFHDAQLRDNPPKPPAQRVGRGFSPDNPYAFQYHHYNNTQPENLAFLGELRALLDRYPGAVALGEISSEDSLATMDEYTRNGRLHMGYSFELLTEDYNVEHIRGTVQRVEASMREGWPCWAISNHDVQRVVTRWGRGEAPKHFATLVSALACSLRGSVCVYQGEELGLPEAEVPFEALQDPYGKTFWPNFKGRDGCRTPLPWDDSEGAGFSRGRPWLPIPADHRALNVAAQQDDPASPLNGFRGFLGWRKRHRALLDGAIAFLPSAEPVIAFVRGEGADALLMAFNLGPGEATLELGERAGWIADRGHGLPSGAVEGGRLRLPGHAAYAARPAA
>NZ_AP014940.1|WP_096382019.1|5756404_5757289_+|DUF2007-domain-containing-protein
MQIVYQAAHSADAQLVRSLLAQEGIRSFVFGGALEGGAGLLPVGGSVRVEVADEDVERARAIIDEWQAAEVPESDDDDEPDRDYGDDATPEHVEDANLYRPLNARKPAAGGFGMAGIVFALVVGALAGALATGAALQPTASVENVDYDADGIADERLSYEDERLVRSDSDRNTDGDVDLVTAYDGNGLPASIEEDQDFNGVRETVSTLAKGLLVTRSADYDGDGVPERQENYLRGVLHTVEWLDKQGRVTKRDTYTGGRLSGGEIDRDGDGALDTARVYDERGEVRHSEPMSAN

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Crispr_ID: NZ_AP014940_16

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_16

5746580-5746746

Orphan

I-E

Consensus_repeat	Method
CAAGACTGAGCGCTGCTCACCCACCGTCATTCCCGCGAAGGCGGGAATCCAGAGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP014940_16

>merge|NZ_AP014940|16|5746580-5746746|CRISPRCasFinder
CAAGACTGAGCGCTGCTCACCCACCGTCATTCCCGCGAAGGCGGGAATCCAGAGCGCTGTACATTCCCGCCCGCGAGCCCGTCGTTCCGACTCGATGGATCCGCGGCTGGAGCAAGACTGAGCGCTACTCACCCACCGTCATTCCCGCGAAGGCGGGAATCCAGAGC

>NZ_AP014940|16|16|5746580-5746746|CRISPRCasFinder
CAAGACTGAGCGCTGCTCACCCACCGTCATTCCCGCGAAGGCGGGAATCCAGAGC	GCTGTACATTCCCGCCCGCGAGCCCGTCGTTCCGACTCGATGGATCCGCGGCTGGAG
CAAGACTGAGCGCTACTCACCCACCGTCATTCCCGCGAAGGCGGGAATCCAGAGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_096382030.1\|5760580_5761243_+\|thiol:disulfide-interchange-protein-DsbA/DsbL	unknown	unknown	gnl\|CDD\|239317
NZ_AP014940.1\|WP_096381955.1\|5733089_5733401_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096382019.1\|5756404_5757289_+\|DUF2007-domain-containing-protein	unknown	unknown	gnl\|CDD\|378182
NZ_AP014940.1\|WP_172437340.1\|5738173_5738929_+\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|227044
NZ_AP014940.1\|WP_096381990.1\|5744912_5745656_+\|VIT-family-protein	unknown	unknown	gnl\|CDD\|153123
NZ_AP014940.1\|WP_096381999.1\|5746939_5747968_+\|LacI-family-DNA-binding-transcriptional-regulator	unknown	unknown	gnl\|CDD\|380518
NZ_AP014940.1\|WP_096381980.1\|5740066_5741014_+\|DMT-family-transporter	unknown	unknown	gnl\|CDD\|307170
NZ_AP014940.1\|WP_096383808.1\|5733409_5734519_-\|S-(hydroxymethyl)glutathione-dehydrogenase/class-III-alcohol-dehydrogenase	unknown	unknown	gnl\|CDD\|176260
NZ_AP014940.1\|WP_172437342.1\|5751574_5754382_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|224544
NZ_AP014940.1\|WP_096382027.1\|5759324_5760206_+\|cytochrome-c4	unknown	unknown	gnl\|CDD\|225418
NZ_AP014940.1\|WP_096381961.1\|5734604_5734877_-\|formaldehyde-responsive-transcriptional-repressor-FrmR	unknown	unknown	gnl\|CDD\|197388
NZ_AP014940.1\|WP_074872741.1\|5758435_5759080_-\|YihA-family-ribosome-biogenesis-GTP-binding-protein	unknown	unknown	gnl\|CDD\|234770
NZ_AP014940.1\|WP_096382023.1\|5757403_5758285_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096382005.1\|5748248_5749940_-\|cyclomaltodextrin-glucanotransferase	unknown	unknown	gnl\|CDD\|200478
NZ_AP014940.1\|WP_145960216.1\|5739046_5740000_-\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|182990
NZ_AP014940.1\|WP_172437341.1\|5743338_5744916_+\|peptide-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|173869
NZ_AP014940.1\|WP_074872622.1\|5749936_5751439_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340871
NZ_AP014940.1\|WP_096382014.1\|5754577_5756353_+\|alpha-glucosidase	unknown	unknown	gnl\|CDD\|200469
NZ_AP014940.1\|WP_096383810.1\|5741702_5743064_-\|glutamate--cysteine-ligase	unknown	unknown	gnl\|CDD\|178221
NZ_AP014940.1\|WP_096381966.1\|5735153_5737925_-\|phosphoenolpyruvate-carboxylase	unknown	unknown	gnl\|CDD\|234570

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_096382030.1\|5760580_5761243_+\|thiol:disulfide-interchange-protein-DsbA/DsbL	gnl\|CDD\|239317	cd03019, DsbA_DsbA, DsbA family, DsbA subfamily; DsbA is a monomeric thiol disulfide oxidoreductase protein containing a redox active CXXC motif imbedded in a TRX fold. It is involved in the oxidative protein folding pathway in prokaryotes, and is the strongest thiol oxidant known, due to the unusual stability of the thiolate anion form of the first cysteine in the CXXC motif. The highly unstable oxidized form of DsbA directly donates disulfide bonds to reduced proteins secreted into the bacterial periplasm. This rapid and unidirectional process helps to catalyze the folding of newly-synthesized polypeptides. To regain catalytic activity, reduced DsbA is then reoxidized by the membrane protein DsbB, which generates its disulfides from oxidized quinones, which in turn are reoxidized by the electron transport chain.	1.82473e-49
NZ_AP014940.1\|WP_096382019.1\|5756404_5757289_+\|DUF2007-domain-containing-protein	gnl\|CDD\|378182	pfam09413, DUF2007, Putative prokaryotic signal transducing protein. This is a family of putative prokaryotic signal transducing proteins of Pii-type.	9.88406e-13
NZ_AP014940.1\|WP_172437340.1\|5738173_5738929_+\|tetratricopeptide-repeat-protein	gnl\|CDD\|227044	COG4700, COG4700, Uncharacterized protein conserved in bacteria containing a divergent form of TPR repeats [Function unknown].	9.31531e-63
NZ_AP014940.1\|WP_096381990.1\|5744912_5745656_+\|VIT-family-protein	gnl\|CDD\|153123	cd02432, Nodulin-21_like_1, Nodulin-21 and CCC1-related protein family. Nodulin-21_like_1: This is a family of proteins closely related to nodulin-21, a plant nodule-specific protein that may be involved in symbiotic nitrogen fixation. This family is also related to CCC1, a yeast vacuole transmembrane protein that functions as an iron and manganese transporter. .	2.36422e-94
NZ_AP014940.1\|WP_096381999.1\|5746939_5747968_+\|LacI-family-DNA-binding-transcriptional-regulator	gnl\|CDD\|380518	cd06295, PBP1_CelR, ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators. This group includes the ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators. The binding of CelR to the celE promoter is inhibited specifically by cellobiose. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.	5.03787e-109
NZ_AP014940.1\|WP_096381980.1\|5740066_5741014_+\|DMT-family-transporter	gnl\|CDD\|307170	pfam00892, EamA, EamA-like transporter family. This family includes many hypothetical membrane proteins of unknown function. Many of the proteins contain two copies of the aligned region. The family used to be known as DUF6. Members of this family usually carry 5+5 transmembrane domains, and this domain attempts to model five of these.	3.32296e-05
NZ_AP014940.1\|WP_096383808.1\|5733409_5734519_-\|S-(hydroxymethyl)glutathione-dehydrogenase/class-III-alcohol-dehydrogenase	gnl\|CDD\|176260	cd08300, alcohol_DH_class_III, class III alcohol dehydrogenases. Members identified as glutathione-dependent formaldehyde dehydrogenase(FDH), a member of the zinc dependent/medium chain alcohol dehydrogenase family. FDH converts formaldehyde and NAD(P) to formate and NAD(P)H. The initial step in this process the spontaneous formation of a S-(hydroxymethyl)glutathione adduct from formaldehyde and glutathione, followed by FDH-mediated oxidation (and detoxification) of the adduct to S-formylglutathione. MDH family uses NAD(H) as a cofactor in the interconversion of alcohols and aldehydes or ketones. Like many zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), these FDHs form dimers, with 4 zinc ions per dimer. The medium chain alcohol dehydrogenase family (MDR) have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding.	0
NZ_AP014940.1\|WP_172437342.1\|5751574_5754382_-\|TonB-dependent-receptor	gnl\|CDD\|224544	COG1629, CirA, Outer membrane receptor proteins, mostly Fe transport [Inorganic ion transport and metabolism].	1.32841e-18
NZ_AP014940.1\|WP_096382027.1\|5759324_5760206_+\|cytochrome-c4	gnl\|CDD\|225418	COG2863, COG2863, Cytochrome c553 [Energy production and conversion].	2.6603e-19
NZ_AP014940.1\|WP_096381961.1\|5734604_5734877_-\|formaldehyde-responsive-transcriptional-repressor-FrmR	gnl\|CDD\|197388	cd10153, RcnR-FrmR-like_DUF156, Transcriptional regulators RcnR and FrmR, and related domains; this domain family was previously known as part of DUF156. This domain family includes various transcriptional regulators that respond to different stressors. It includes Escherichia coli RncR (formally known as YohL, nickel and cobalt-sensitive), and E. coli FrmR (formally known as YaiN, formaldehyde sensitive). Escherichia coli RncR represses expression of the gene encoding the nickel and cobalt-efflux protein RcnA; RcnA may act through modulating NikR, to repress the NIkABCDE nickel transporter. In vitro, purified RncR binds to the rncA promoter DNA fragment in the absence of Ni2+ or Co2+, and the affinity of RncR for this promoter is reduced in the presence of excess nickel. Escherichia coli FrmR regulates the formaldehyde degradation frmRAB operon. This family belongs to a larger superfamily that includes CsoRs (copper-sensitive operon repressors). CsoRs form homotetramers (dimer of dimers). In Mycobacterium tuberculosis CsoR, within each dimer, two Cys residues on opposite subunits, along with a His residue, bind the Cu(I) ion (forming a triagonal S2N coordination complex, C-H-C). These residues are conserved in the majority of members of this superfamily. In this family, however, not all these residues are conserved; in E.coli RcnR and FrmR there is a His or a Thr instead of the second Cys (C-H-H or C-H-T) respectively. For E. coli FrmR, an N-terminal His residue, not conserved in all members of this family, is also involved in metal binding (H-C-H-H). A conserved Tyr and a Glu residue that facilitate allosteric regulation of DNA binding for CsoRs are poorly conserved in this family.	2.19021e-38
NZ_AP014940.1\|WP_074872741.1\|5758435_5759080_-\|YihA-family-ribosome-biogenesis-GTP-binding-protein	gnl\|CDD\|234770	PRK00454, engB, GTP-binding protein YsxC; Reviewed.	4.87813e-100
NZ_AP014940.1\|WP_096382005.1\|5748248_5749940_-\|cyclomaltodextrin-glucanotransferase	gnl\|CDD\|200478	cd11339, AmyAc_bac_CMD_like_2, Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.	3.17545e-136
NZ_AP014940.1\|WP_145960216.1\|5739046_5740000_-\|LysR-family-transcriptional-regulator	gnl\|CDD\|182990	PRK11139, PRK11139, DNA-binding transcriptional activator GcvA; Provisional.	7.64283e-36
NZ_AP014940.1\|WP_172437341.1\|5743338_5744916_+\|peptide-ABC-transporter-substrate-binding-protein	gnl\|CDD\|173869	cd08504, PBP2_OppA, The substrate-binding component of an ABC-type oligopetide import system contains the type 2 periplasmic binding fold. This family represents the periplasmic substrate-binding component of an ATP-binding cassette (ABC)-type oligopeptide transport system comprised of 5 subunits. The transport system OppABCDEF contains two homologous integral membrane proteins OppB and OppF that form the translocation pore; two homologous nucleotide-binding domains OppD and OppF that drive the transport process through binding and hydrolysis of ATP; and the substrate-binding protein or receptor OppA that determines the substrate specificity of the transport system. The dipeptide (DppA) and oligopeptide (OppA) binding proteins differ in several ways. The DppA binds dipeptides and some tripeptides and is involved in chemotaxis toward dipeptides, whereas the OppA binds peptides of a wide range of lengths (2-35 amino acid residues) and plays a role in recycling of cell wall peptides, which precludes any involvement in chemotaxis. Most of other periplasmic binding proteins are comprised of only two globular subdomains corresponding to domains I and III of the dipeptide/oligopeptide binding proteins. The structural topology of these domains is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the ligand-binding domains from ionotropic glutamate receptors, LysR-type transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.	5.238e-177
NZ_AP014940.1\|WP_074872622.1\|5749936_5751439_-\|MFS-transporter	gnl\|CDD\|340871	cd17313, MFS_SLC45_SUC, Solute carrier family 45 and similar sugar transporters of the Major Facilitator Superfamily of transporters. This group includes the solute carrier 45 (SLC45) family as well as plant sucrose transporters (SUCs or SUTs) and similar proteins such as Schizosaccharomyces pombe general alpha-glucoside permease. the SLC45 family is composed of four (A1-A4) vertebrate proteins as well as related insect proteins such as Drosophila sucrose transporter SCRT or Slc45-1. Members of this group transport sucrose and other sugars like maltose into the cell, with the concomitant uptake of protons (symport system). Plant sucrose transporters are crucial to carbon partitioning, playing a key role in phloem loading/unloading. They play a key role in loading and unloading of sucrose into the phloem and as a result, they control sucrose distribution throughout the whole plant and drive the osmotic flow system in the phloem. They also play a role in the exchange of sucrose between beneficial symbionts (mycorrhiza and Rhizobium) as well as pathogens such as nematodes and parasitic fungi. There are nine sucrose transporter genes in Arabidopsis and five in rice. Vertebrate SLC45 family proteins have been implicated in the regulation of glucose homoeostasis in the brain (SLC45A1), with skin and hair pigmentation (SLC45A2), and with prostate cancer and myelination (SLC45A3). Mutations in SLC45A2, also called MATP (membrane-associated transporter protein) or melanoma antigen AIM1, cause oculocutaneous albinism type 4 (OCA4), an autosomal recessive disorder of melanin biosynthesis that results in congenital hypopigmentation of ocular and cutaneous tissues. The SLC45 family and related sugar transporters belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	3.20144e-67
NZ_AP014940.1\|WP_096382014.1\|5754577_5756353_+\|alpha-glucosidase	gnl\|CDD\|200469	cd11330, AmyAc_OligoGlu, Alpha amylase catalytic domain found in oligo-1,6-glucosidase (also called isomaltase; sucrase-isomaltase; alpha-limit dextrinase) and related proteins. Oligo-1,6-glucosidase (EC 3.2.1.10) hydrolyzes the alpha-1,6-glucosidic linkage of isomalto-oligosaccharides, pannose, and dextran. Unlike alpha-1,4-glucosidases (EC 3.2.1.20), it fails to hydrolyze the alpha-1,4-glucosidic bonds of maltosaccharides. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.	0
NZ_AP014940.1\|WP_096383810.1\|5741702_5743064_-\|glutamate--cysteine-ligase	gnl\|CDD\|178221	PLN02611, PLN02611, glutamate--cysteine ligase.	0
NZ_AP014940.1\|WP_096381966.1\|5735153_5737925_-\|phosphoenolpyruvate-carboxylase	gnl\|CDD\|234570	PRK00009, PRK00009, phosphoenolpyruvate carboxylase; Reviewed.	0

>NZ_AP014940.1|WP_096381990.1|5744912_5745656_+|VIT-family-protein
MTTQPAPSPPARPRAHARSRHPEAHRSERVGWLRAAVLGANDGIVSVAGLVVGVAASGADAGAILTSGIAGTVAGAMSMAAGEYVSVRSQADTEHADIAVEKRELAENPHAELEELAHIYVQRGLTPELAREVARQLSEHDALASHARDELGITDTLRARPVQAALASAAAFISGAALPIAAVVLAPHSQVQPAAIATTLAALSVSGALAAWAGGAPVLRGALRVMFWGALAMAAATAVGHLFGVQV
>NZ_AP014940.1|WP_172437341.1|5743338_5744916_+|peptide-ABC-transporter-substrate-binding-protein
MPAVPAQPAHAAAAQLERGNGPEPSTLDAHRCQEVACGNVLRDLYEGLVTEDAQGRLVPGLAERWTVSADGRTWTFALRPGLRWSNGEALDAAQVVASFRRAFAPATAAPFGELFDALDGAQAVQAGDLPPERLGVSAPDPHTVVFRLTRSASLPALLTLPIAFPVYLPAVQKYAAQHTQPGRLVSNGAYRLAAWTPQANLVVEKNPNFHDAARVALPRVRFHVTEDAAAELQRFAAGDLHITEVVPPQPLAALRERFGEQLRLSPYLGAFWFGLNTTQPPFRPACASARCGEQALALRRALTMAIDRDKLTRYVTGLGETPAYGIVPPGIAGYAPAAMPWASWTQAQREAHARALYRHAGYSDEHPLVLELRYNTSTPHRRLALAVAAMWKQTLGVQVRLRNEEWKVFVQNRKQRAITQAFRGGWIGDLPDARNFLAAFANDGPLNWMGYDDAGYRERLARADAAATQAARNAWLRAAEQRLLNDNAAIPLYFYTSKHLVSRRVRGFEPNALDRHASRWLSLTP
>NZ_AP014940.1|WP_096383810.1|5741702_5743064_-|glutamate--cysteine-ligase
MKDLEIPDVKGGGRAVLIDYLASGARPESDWKIGTEHEKFGFRTDDLRPPTFDGERGIEALLKGLVQFGWAPVEENGRVIALTRDQASVSLEPAGQLELSGAPLATLHDTCVEAATHLREVRTVAEPMGLGFLGMGFQPKWRREDMPWMPKGRYKIMRDYMPKVGQLGLDMMTRTSTVQVNLDVRDEADMVKKFRVSLALQPIATALFADSPFLEGRPNGYLSYRSHIWTDTDADRTGLLDFVFEDGFGYERYVDYLLDVPMYFVYRDGRYIDASGQSFRDFMDGRLPAYPDQRPTLKDWADHSTTAFPEVRLKKYLEMRGADSGPWNRICALSAFWVGLLYDAEALDAAWDLVLDFTPEERHALRDGVPRHGFQLPFRDGKVLELARRALEISAHGLKRRGRLNGNGADESIYLEPLMEFVAMGKSPAERKLELFHGEWDGNVDRVFREFAY
>NZ_AP014940.1|WP_096381980.1|5740066_5741014_+|DMT-family-transporter
MSTAPLTATAAVAARPLLLRAGLMAAASTSLALLALLSRYTRGLAPELVTWGRFILPALILTAFVRGPDWRAAWSLADRPGWVRALCAVIAQVCFVFAATQGDLLQAVLLYNTGPLFIPLVAWLWLGERLRPATLAGLALGFLGVLAVLQPGTRGLDPLALIALTGGLAMAVSQVLFYRSAQRQPPLRNQFKLYTQASLLSLPLAALGAAHTPWGAVLAGEAASEPVWVLSLALLGMTACSLGNQSLRDLAYRGMDNASTLAPLMYVAVPVSAALDWLLFDRVAAPSALLGAALVVVGAVVALRSGARAQRAEAS
>NZ_AP014940.1|WP_145960216.1|5739046_5740000_-|LysR-family-transcriptional-regulator
MTTKPGSLPPGSGDDAPARRLPPLRALQAFAAVVRHDGMRRAAERLHLSHAALSQHVQHLEEAFGLRLLDRSGGRARPTPLGREFGEALIDGFERIEAATARLRLRGDESRRLQLGAPTSLSVSLLLPRIEEFSARAGFELQLFCPAGPADLAQARVHALLMHREPAEHGLRGELLFEQALLPVASPGLLARLDPQRWWLDPVPGARLLHVVSDGWREDWPAWFGADTAAWPLPQLSLSSPMPAISAALAGQGIALLYPRLIAERLASGELAPLPLPQPAPVKRLYLAWLPEAEGAARLQWVRDWVVALLRGEDGGG
>NZ_AP014940.1|WP_172437340.1|5738173_5738929_+|tetratricopeptide-repeat-protein
MPYFGLGLHVVVALYFAVHAVRSGQDRYWLMVLFMFPLLGSVVYAFAIWLPEQRHSRHGRALVGNVRRMLDPGRELRQAQDAFDDSATTDNRLRLADALLGAGRAGDALPLYRAALSGVHREDPHIQVKLAHALLEAGEPAQARQLLDELIAKRPDFRSPEGHLTYARAVAAQGDKSNAKEEFEALTAYSSGFEAHAYYVECLIGWGDTGRARELCEQAQAKARRLPAYARKMHRVELDKLRELEKRAQAL
>NZ_AP014940.1|WP_096381966.1|5735153_5737925_-|phosphoenolpyruvate-carboxylase
MTDSSDEPLRAAEWAEQAAERAADFAPTDALLREDVKTLGALVGEILAEQRGQGFLDGVERLRRAAIRRREAGEPIDALAAALVDIDLEQAADLVRAFATYFQAVNLAERVHRIRRRRDYERSGAGAQPGGLRDALATLARQGVSAEEVAALLPRLRIEPVFTAHPTEAVRRALLEKERTIVECLVADIDRGRTPPERRADRERIRLALTASWQTAEAPAAKPSVADEFEHVGFYLSDVLYRVLPVYYEVFEEALRETYGGAPALPDVLGFGTWVGGDMDGNPNVGADTIAATLAGQRALVLAAYRRDLASLEELLSQSVHRVRVDDAVLAKVEDYRYLLPKAAALLKPRHADMPYRNLLGLMSARLQATLEESVHGYPDAAAFLADIDLIERSLAAHQGAHAGGFAVRRLRRRAECFGFHLAGLDLRQDSATHDAALAALFEQPEWAALDVAARAARLHQLLDGEAPPARPAAAAAQPTLDVFRAVARLRPRFGARAFGPYIVSMSRSAADALAVLALARTAGCADDKGRVPLDVAPLFETVDDLDAAADTLRALFSDPVYRDHLCSRGDRQVVMLGYSDSAKDGGMVASRWALQQTQIALTALAADSGVRIAFFHGRGGSISRGGGKTERAVIAAPRGSVDGYLRLTEQGEVIHRKYGIRALALRNLEQTSGAVLRATLRPRAPEPREAGWRRIAGELAGEARAHYRALVHEDPQFPAYFRAATPIDVIERLRIGSRPAKRAGSGDISSLRAIPWVFAWSQNRAGLTAWYGVGTGLAAALDRHGRDTLAEMARDWPFFGTLIDDLEMVLAKSDPAIFERYSQLASALPDGDLHARFHPSIAAEFERTRDAVLAIKGSDELLRGDHRLRQSIRLRNPYVDPISLLQVDLLARWRAADRPDDALLQALVATVNGIAAGVQNTG
>NZ_AP014940.1|WP_096381961.1|5734604_5734877_-|formaldehyde-responsive-transcriptional-repressor-FrmR
MPHSPAEKKRVLTRVRRIKGQTEALERALEAGSECAAVLQQIAAIRGAVNGLMSEVLESHIREELGQAVADRGRDASIDEIAALVRSYLK
>NZ_AP014940.1|WP_096383808.1|5733409_5734519_-|S-(hydroxymethyl)glutathione-dehydrogenase/class-III-alcohol-dehydrogenase
MKSRAAVAFAAGEPLKIVEIDVQPPKAGEVLVRIHATGVCHTDAFTLSGDDPEGLFPAVLGHEGGGVVVEVGEGVTSLKPGDHVIPLYTAECRKCKFCLSSKTNLCQAVRATQGKGLMPDGTTRFSYEGQPIHHYMGCSTFSEYTVVPEISLAVVNPEAPLEKVCLLGCGVTTGIGAVHNTAKVQPGDTVAVFGLGGIGLAVIQGAVQAKAGRIIGVDTNATKFELAKSMGATDCVNPKDFDRPIQEVLVEMTDGGVDFSFECIGNVEVMRSALECCHKGWGESVIIGVAGAGQEIKTRPFQLVTGRVWRGTAFGGVKGRTQLPGMVEQAMKGEIDLDPFITHTLPLERINEAFDLMHEGKSIRTVIHY
>NZ_AP014940.1|WP_096381955.1|5733089_5733401_-|hypothetical-protein
MKNIQVIDSAINCVYDVFALDEAEFDLLFPPGQDIAFIDEVLARHPPHVLEPVFERLWRNRVPKREAMGLHGLLFYDLDEKKPFYPQRADELAVNPNGSPLRR
>NZ_AP014940.1|WP_096381999.1|5746939_5747968_+|LacI-family-DNA-binding-transcriptional-regulator
MRKKTKATSVDIAHLAGVSQATVSRVLSGSPLVNAETRKRVEAVVRELNYKVDRHASSLRRQRSGTLALLLFEDPTPDESHINPFFLSMLGSITRACARHGQDLLISFQQLSDDWAADYEDSMKADGLILLGYGDYLAYQGKLQRLVEQGTRFVRWGAVLPDQPGLSIGCENLGGGRQAGAHLVALGRRRVAFLGDASSHYPEFLDRFLGCEQALHEAGLALDRTLQVDAESSEDAGHAAALELLARELPFDAVFAASDLIAIGAMRALTERGLRVPEDVSVIGFDDLPTARFAHPPLTTVFQDTKQAGELLVEALMQLIRGEPAQSQRLPTTLVVRKSCGG
>NZ_AP014940.1|WP_096382005.1|5748248_5749940_-|cyclomaltodextrin-glucanotransferase
MRALALAALSLTLAACVHGGAAREAAARRDYYGTLEPMASEAVYFVVTDRFVNGDPGNDQRAQGGPDPDTRSFDRPVPGGPPGESDNIGYLGGDFKGLLDNAGYIRDMGFGAVWLTPIVDNPDQAFTGGDAVTWGGAFQDRGKTGYHGYWGVDFYRLDEHLPSPGLDFAGLTRGMKQHGLKTVLDIVANHGSPSFTMRKPQPKYGRIYRDGVLVADHQNLPPERLDPAHNPLHRFFHNERDLVQLSNIDDTNPEVMEYFVGAYSQWIDQGADAFRIDTIRHMPLAFWRVFAERIRAKRPGFFMFGEAFDYKAENIAPFTWAENGGVSVLDFPLKERLAEVFGRTRADYARLDERLYLQDGPYANPYELMTFYDNHDMPRLDASDEGFIDAHNWLFTARGIPVIYYGSEVGFERGRAEHAGNRNYFGQPRVDAARSHPIRLALKRIAEVRRQSPALQRGLQLNVSLQGERAAFYRVYEHGDTAQIALVLLNKGDAPAPFAVSEYLQAGRWRAALGGGEIAVGEGGTLRASVPAHGVEVYLLDAPVRRADLAAALDQAMAHARKR
>NZ_AP014940.1|WP_074872622.1|5749936_5751439_-|MFS-transporter
MTDRPDATPRKPTLTFWQIWNMCFGFLGIQFGFALQNANVSRIFQTLGAPIDDIPMLWIAAPLTGLIVQPIVGYLSDRTWTGLGRRRPYFLVGAILATLALIAMPNSPTLWIAAGLLWMLDASINVSMEPFRAFVGDQLPQQQRAAGYAMQSFFIGVGSVVASLLPYLLAHFGVGNTAAAGEVPDTVRYSFYFGGAVLLLSVGWTVLRSREYPPQQLQAYDEAPPIEPSPERDRVRCLLFGASWMVIGGICATAISMLRLDRQLYVLAALIAAFGVALLARGIVRDGGGFATVMDDLGAMPAAMTRLAVVQFFSWFALFSMWIYTTPAVTQLHYHTSDVASAAYNEGANWVGVLFAAYNGFAALAAIAIAPMARRWGLRRSHLFNLTLGGAGLISVALVRDPQMLLLSMVGIGFAWASILSLPYAMLSDSVPAAKMGVFMGIFNFFIVIPQLVAASLLGFLVRHLFGGHPVAALVIGGVSLFVAGACTLWVREPDAQVRA
>NZ_AP014940.1|WP_172437342.1|5751574_5754382_-|TonB-dependent-receptor
MSHSKPAARGPKQLDRHLLTLALAALGLCGFAPAWAADAPAPQDSAPAAAAAPQTAHELDAVQVTGNRRVQSIQKYAGTIQSFSGEDIAKLGINTDFRNLQAVVPGLQITKQEGKYEIFLRGIGAADSDFSSDPSVATYYNGIYLPRPRSIGPMFFDVERIEVNKGPQGTVRGRNATGGSINVISKRPELGVTSGGLKIGAGNYDYTNAEGVLNLPIGDTFALRAALFDEERSSYITNGYPKSLFSAEGPSALDNQAARLSALWQPNDKFSAYVMLDKVTERGTGDPGLFAERGLAAGYDIKDLDDPFKQYFRTQGKTTNDIEGIAATFTYAFNDAVSVEFNTSYRKYDFYNRNASREWQLGPVYPGSDREAYFNPERLDWYDTFYQADKSSSRINELRFFGDTGKLIWSAGLFNYEEKYDYVSWDVGNGYFGDCDWWRPGTVCGYQDGLGGENRGDNSKVESNAVYGDFSFAATDSLRLIGGIRYTRDKKIARESNVKYQFIIPEELFQQFTGQPINTSTNPYTTGLILGSPGFQLAGPGRRRGGDPSICTGWSPADLRCGPGGNTLDYFLGGFQNFGANDNWAQFLQKNRDQIQVIARSDFPNGRSEDVYKDNYVDWRVGFEYDLAAKVMLYGTVSTGTRAGGINRPLTLNDGSALAPSFAPEELTAYEAGIKGDYVWGETPVRLNASVFYYDYKNKVLQNLIDVPAPTPTNPNATSRQVFNDNAANASVLGLELEGKVGLPHGFDIGYNFTYLDATFDDSKVLDTRSGGLGLIVPLDGNRLPNTSKYNANVSLSQTIDIGRGALNSFDWTINLTYRSDYYLTAFNSRGFGLDANGKVIEIPLKDMPFNNGSNPAAGGGPANGLAMRDDVDGFFTVNVSAGLNFGSENQFRVDGFVSNLTDEVYSGKGFVNNSTNIRYLNTPRMYGIRFASQF
>NZ_AP014940.1|WP_096382014.1|5754577_5756353_+|alpha-glucosidase
MQAPRPSRTAAVSWRASPQRSVVARRAIEPLYAAVLQKQGSHLSAAVSSQPAQRDPSWWRGAVIYQVYPRSFRDLDGDGVGDLPGIVEKLGYIADLGVDAIWISPFFKSPMADFGYDIADYLAVDPLFGNLEDFDRLLAKAHALGLKVMIDQVLSHTSNEHEWFKRSRESRDNEFADWYVWADARADGTAPNNWMSLFGGVAWRWEPRRQQYYLHNFLSAQPDLNFHHPAVRAAVLDNVRFWLERGVDGLRLDAINFCFHDAQLRDNPPKPPAQRVGRGFSPDNPYAFQYHHYNNTQPENLAFLGELRALLDRYPGAVALGEISSEDSLATMDEYTRNGRLHMGYSFELLTEDYNVEHIRGTVQRVEASMREGWPCWAISNHDVQRVVTRWGRGEAPKHFATLVSALACSLRGSVCVYQGEELGLPEAEVPFEALQDPYGKTFWPNFKGRDGCRTPLPWDDSEGAGFSRGRPWLPIPADHRALNVAAQQDDPASPLNGFRGFLGWRKRHRALLDGAIAFLPSAEPVIAFVRGEGADALLMAFNLGPGEATLELGERAGWIADRGHGLPSGAVEGGRLRLPGHAAYAARPAA
>NZ_AP014940.1|WP_096382019.1|5756404_5757289_+|DUF2007-domain-containing-protein
MQIVYQAAHSADAQLVRSLLAQEGIRSFVFGGALEGGAGLLPVGGSVRVEVADEDVERARAIIDEWQAAEVPESDDDDEPDRDYGDDATPEHVEDANLYRPLNARKPAAGGFGMAGIVFALVVGALAGALATGAALQPTASVENVDYDADGIADERLSYEDERLVRSDSDRNTDGDVDLVTAYDGNGLPASIEEDQDFNGVRETVSTLAKGLLVTRSADYDGDGVPERQENYLRGVLHTVEWLDKQGRVTKRDTYTGGRLSGGEIDRDGDGALDTARVYDERGEVRHSEPMSAN
>NZ_AP014940.1|WP_096382023.1|5757403_5758285_-|hypothetical-protein
MDATSASGGALAVATGLDAGTILAAGAYGTALLFFAYGGYALLKAKSAEQSKNVRWYLGIGAVVALAMIGFDAFKQQIGGARAQPDVFLAFSPKFSAVGLPEPAVEYRGQALKLSAPIRVSDQSSINISVDAIIEKVKGLQQNNQQLRSALGSAALAGQPKELGERIAAADSAGQDPCASGGDATLCGWKQLSNGELASAETTLTQAVKDAPAADHGAKSAALSGLGEIYVGQGRIDEAKVLLRKAADLGNEGAKKRLQTLVLPVRETAPAPGAALRPELRERPQREVRLPQR
>NZ_AP014940.1|WP_074872741.1|5758435_5759080_-|YihA-family-ribosome-biogenesis-GTP-binding-protein
MSNPLARARYLLSAHNVKQLPPDGGFEVAFAGRSNAGKSSALNALCQQNALARVSKTPGRTQQLVFFDVSPLHRGPEPAPEPDRFLVDLPGYGYAKVPQDLQAHWQAFLDRYFQTRQALRGLVVVMDIRHPLKDYDRQMIAYAVNRGLPAHALLTKADKFGRGQQQQALMAVRKDLHASYGDTVSVQTFSGESKQGVDEARAVVGGWLELGAAK
>NZ_AP014940.1|WP_096382027.1|5759324_5760206_+|cytochrome-c4
MSQARVLSLVGLAVFAVAAVAYAQTTVTPIPDKEPVQTAPLNAGPQSKWGDVKAGATKAGTCAACHGLDGNPTDPQYPRLAGQSERYIAHQIALFKSGERNTGMAAAMKPFADALSEQDARDLGAYFATQKSGAGVADDTVVASGPNKDKKFYQVGEDLFRRGDKARGIPACMACHGPGGAGNPGPAYPHLAGQQAAYSQRRLEEYRAGTTTQKDPHLFNVMAGVAKQLTDEEIGSLASYLQGLHERADDIAAAGAPAPAAKPAAAPAPAAAPSATPAPAPKPAGAPATPAKG
>NZ_AP014940.1|WP_096382030.1|5760580_5761243_+|thiol:disulfide-interchange-protein-DsbA/DsbL
MNRRLATLLLLAVIPFAAAAAPKAAAPAGPAPEPGVDYVEIPGGKPFATPAGKVEVVEVFGYTCPHCAHFEPLVSKWKAKLPADVNFVPLAAPWGGYWTPYAQAFYTAQSLKLLPQTHEAVFKALHEDKSLPIQNASTQEIAGFYAKFGADPSTFAATMTGKATEQAMKRATDFIMASGVDGTPGMVVAGKYRITTQKGFDDMLRVADHLIARERAKTKR

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Crispr_ID: NZ_AP014940_17

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_17

5821566-5821949

Orphan

Consensus_repeat	Method
ACNGTCAACGGCNGCATC	CRT

7 spacers

The CRISPR arrays of NZ_AP014940_17

>merge|NZ_AP014940|17|5821566-5821949|CRT
AAGGTCAACGGCAGCATCACCGTCGACGCCGGCCAGACCCGCGGCGACCTGGACACCGTCAATGGCAGCATCCGCATCGGCGACAACGCCAGCGTCGATGAAGCCAAGACGGTCAACGGCAGCATCAGCGTCGGCAACAACTCGCGCGCCAACCGGCTGGAAACGGTCAACGGCAGCATCCGCGCCGGGACCAAGCTCACCGCCAGCGGCGGCCTAGAAACCGTCAACGGCGGCATCTTCGTCGACCGCGGCGGCCGCCTCGGCGGCGACGTGAGCACGGTCAACGGCTCCATCGGCCTGGTCGCCACCGAGCTCAACGGCGGCATCGACACGGTCAACGGCGACGTCACCGTCGGCGTCGACTCGCACGTCACCGGCGGCATC

>NZ_AP014940|17|1|5821566-5821949|CRT
AAGGTCAACGGCAGCATC	ACCGTCGACGCCGGCCAGACCCGCGGCGACCTGGAC
ACCGTCAATGGCAGCATC	CGCATCGGCGACAACGCCAGCGTCGATGAAGCCAAG
ACGGTCAACGGCAGCATC	AGCGTCGGCAACAACTCGCGCGCCAACCGGCTGGAA
ACGGTCAACGGCAGCATC	CGCGCCGGGACCAAGCTCACCGCCAGCGGCGGCCTAGAA
ACCGTCAACGGCGGCATC	TTCGTCGACCGCGGCGGCCGCCTCGGCGGCGACGTGAGC
ACGGTCAACGGCTCCATC	GGCCTGGTCGCCACCGAGCTCAACGGCGGCATCGAC
ACGGTCAACGGCGACGTC	ACCGTCGGCGTCGACTCG
CACGTCACCGGCGGCATC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_074872529.1\|5815214_5815910_+\|rhomboid-family-intramembrane-serine-protease	unknown	unknown	gnl\|CDD\|366759
NZ_AP014940.1\|WP_096382164.1\|5813570_5814950_-\|porin	unknown	unknown	gnl\|CDD\|367457
NZ_AP014940.1\|WP_145960217.1\|5838554_5839967_-\|AmpG-family-muropeptide-MFS-transporter	unknown	unknown	gnl\|CDD\|341039
NZ_AP014940.1\|WP_096382195.1\|5824992_5825727_+\|2OG-Fe-dioxygenase-family-protein	unknown	unknown	gnl\|CDD\|370779
NZ_AP014940.1\|WP_096382212.1\|5836645_5837824_+\|anhydro-N-acetylmuramic-acid-kinase	unknown	unknown	gnl\|CDD\|236579
NZ_AP014940.1\|WP_096382173.1\|5818449_5819712_-\|peptidoglycan-DD-metalloendopeptidase-family-protein	unknown	unknown	gnl\|CDD\|227278
NZ_AP014940.1\|WP_096382150.1\|5811357_5811612_-\|DUF2164-domain-containing-protein	unknown	unknown	gnl\|CDD\|378315
NZ_AP014940.1\|WP_096382177.1\|5819711_5821247_-\|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase	unknown	unknown	gnl\|CDD\|235463
NZ_AP014940.1\|WP_096382208.1\|5834960_5836454_+\|M23-family-metallopeptidase	unknown	unknown	gnl\|CDD\|366703
NZ_AP014940.1\|WP_096382217.1\|5839956_5840730_-\|exodeoxyribonuclease-III	unknown	unknown	gnl\|CDD\|197336
NZ_AP014940.1\|WP_096382200.1\|5825826_5827071_-\|right-handed-parallel-beta-helix-repeat-containing-protein	unknown	unknown	gnl\|CDD\|379079
NZ_AP014940.1\|WP_096383819.1\|5824290_5824680_+\|MAPEG-family-protein	unknown	unknown	gnl\|CDD\|226211
NZ_AP014940.1\|WP_074872537.1\|5812400_5812637_-\|thioredoxin-family-protein	unknown	unknown	gnl\|CDD\|379063
NZ_AP014940.1\|WP_074872525.1\|5816042_5816363_+\|DUF1820-family-protein	unknown	unknown	gnl\|CDD\|226900
NZ_AP014940.1\|WP_096382191.1\|5824710_5824899_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096382155.1\|5811644_5812349_-\|MOSC-domain-containing-protein	unknown	unknown	gnl\|CDD\|225167
NZ_AP014940.1\|WP_172437343.1\|5812717_5813446_-\|MarR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197670
NZ_AP014940.1\|WP_096382186.1\|5822311_5824132_+\|M28-family-peptidase	unknown	unknown	gnl\|CDD\|349910
NZ_AP014940.1\|WP_096382169.1\|5816542_5818186_-\|S41-family-peptidase	unknown	unknown	gnl\|CDD\|223864
NZ_AP014940.1\|WP_096382204.1\|5833556_5834768_-\|tyrosine--tRNA-ligase	unknown	unknown	gnl\|CDD\|235645

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_074872529.1\|5815214_5815910_+\|rhomboid-family-intramembrane-serine-protease	gnl\|CDD\|366759	pfam01694, Rhomboid, Rhomboid family. This family contains integral membrane proteins that are related to Drosophila rhomboid protein. Members of this family are found in bacteria and eukaryotes. Rhomboid promotes the cleavage of the membrane-anchored TGF-alpha-like growth factor Spitz, allowing it to activate the Drosophila EGF receptor. Analysis has shown that Rhomboid-1 is an intramembrane serine protease (EC:3.4.21.105). Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite.	2.19958e-23
NZ_AP014940.1\|WP_096382164.1\|5813570_5814950_-\|porin	gnl\|CDD\|367457	pfam03349, Toluene_X, Outer membrane protein transport protein (OMPP1/FadL/TodX). This family includes TodX from Pseudomonas putida F1 and TbuX from Ralstonia pickettii PKO1. These are membrane proteins of uncertain function that are involved in toluene catabolism. Related proteins involved in the degradation of similar aromatic hydrocarbons are also in this family, such as CymD. This family also includes FadL involved in translocation of long-chain fatty acids across the outer membrane. It is also a receptor for the bacteriophage T2.	6.52767e-109
NZ_AP014940.1\|WP_145960217.1\|5838554_5839967_-\|AmpG-family-muropeptide-MFS-transporter	gnl\|CDD\|341039	cd17486, MFS_AmpG_like, AmpG and similar transporters of the Major Facilitator Superfamily. AmpG acts as an inner membrane permease in the beta-lactamase induction system and in peptidoglycan recycling. It transports meuropeptide from the periplasm into the cytosol in gram-negative bacteria, which is essential for the induction of the ampC encoding beta-lactamase. The AmpG family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.20753e-107
NZ_AP014940.1\|WP_096382195.1\|5824992_5825727_+\|2OG-Fe-dioxygenase-family-protein	gnl\|CDD\|370779	pfam10014, 2OG-Fe_Oxy_2, 2OG-Fe dioxygenase. This family contains 2-oxoglutarate (2OG) and Fe-dependent dioxygenases. It includes L-isoleucine dioxygenase (IDO).	1.40279e-84
NZ_AP014940.1\|WP_096382173.1\|5818449_5819712_-\|peptidoglycan-DD-metalloendopeptidase-family-protein	gnl\|CDD\|227278	COG4942, COG4942, Membrane-bound metallopeptidase [Cell division and chromosome partitioning].	5.84923e-89
NZ_AP014940.1\|WP_096382150.1\|5811357_5811612_-\|DUF2164-domain-containing-protein	gnl\|CDD\|378315	pfam09932, DUF2164, Uncharacterized conserved protein (DUF2164). This domain, found in various hypothetical prokaryotic proteins, has no known function.	1.4861e-28
NZ_AP014940.1\|WP_096382177.1\|5819711_5821247_-\|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase	gnl\|CDD\|235463	PRK05434, PRK05434, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase.	0
NZ_AP014940.1\|WP_096382208.1\|5834960_5836454_+\|M23-family-metallopeptidase	gnl\|CDD\|366703	pfam01551, Peptidase_M23, Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.	4.58201e-43
NZ_AP014940.1\|WP_096382217.1\|5839956_5840730_-\|exodeoxyribonuclease-III	gnl\|CDD\|197336	cd10281, Nape_like_AP-endo, Neisseria meningitides Nape-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases. This subfamily includes Neisseria meningitides Nape and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity; for example, Neisseria meningitides Nape and NExo. Nape, found in this subfamily, is the dominant AP endonuclease. It exhibits strong AP endonuclease activity, and also exhibits 3'-5'exonuclease and 3'-deoxyribose phosphodiesterase activities.	2.34607e-143
NZ_AP014940.1\|WP_096382212.1\|5836645_5837824_+\|anhydro-N-acetylmuramic-acid-kinase	gnl\|CDD\|236579	PRK09585, anmK, anhydro-N-acetylmuramic acid kinase; Reviewed.	0
NZ_AP014940.1\|WP_096383819.1\|5824290_5824680_+\|MAPEG-family-protein	gnl\|CDD\|226211	COG3686, COG3686, Predicted membrane protein [Function unknown].	5.80834e-29
NZ_AP014940.1\|WP_074872537.1\|5812400_5812637_-\|thioredoxin-family-protein	gnl\|CDD\|379063	pfam13192, Thioredoxin_3, Thioredoxin domain.	2.2475e-06
NZ_AP014940.1\|WP_074872525.1\|5816042_5816363_+\|DUF1820-family-protein	gnl\|CDD\|226900	COG4517, COG4517, Uncharacterized protein conserved in bacteria [Function unknown].	5.33237e-47
NZ_AP014940.1\|WP_096382200.1\|5825826_5827071_-\|right-handed-parallel-beta-helix-repeat-containing-protein	gnl\|CDD\|379079	pfam13229, Beta_helix, Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases.	3.06987e-10
NZ_AP014940.1\|WP_096382155.1\|5811644_5812349_-\|MOSC-domain-containing-protein	gnl\|CDD\|225167	COG2258, COG2258, Uncharacterized protein conserved in bacteria [Function unknown].	9.33474e-82
NZ_AP014940.1\|WP_172437343.1\|5812717_5813446_-\|MarR-family-transcriptional-regulator	gnl\|CDD\|197670	smart00347, HTH_MARR, helix_turn_helix multiple antibiotic resistance protein.	1.37335e-12
NZ_AP014940.1\|WP_096382186.1\|5822311_5824132_+\|M28-family-peptidase	gnl\|CDD\|349910	cd05660, M28_like_PA, M28 Zn-peptidase containing a protease-associated (PA) domain insert. Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate.	7.0577e-109
NZ_AP014940.1\|WP_096382169.1\|5816542_5818186_-\|S41-family-peptidase	gnl\|CDD\|223864	COG0793, Prc, Periplasmic protease [Cell envelope biogenesis, outer membrane].	1.9915e-121
NZ_AP014940.1\|WP_096382204.1\|5833556_5834768_-\|tyrosine--tRNA-ligase	gnl\|CDD\|235645	PRK05912, PRK05912, tyrosyl-tRNA synthetase; Validated.	0

>NZ_AP014940.1|WP_096382177.1|5819711_5821247_-|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase
MSATSCPKPVVLLILDGWGHRDDPADNALAQAELPNWRALLASQAHTLIHTEGRHVGLPDGQMGNSEVGHMNLGAGRIVYQDLTRIDAAIEDGSFYANDELRAACAAAKAAGTTLHLLGLLSPGGVHSHERHIFAMIELARREGVAKVAVHAFLDGRDMPPKSAAPSLQRLQQACDEAGNARIASIGGRYYAMDRDKRWDRQLRAWDAIVEAKSEHHAATALEGLDAAYARGETDEFVAPTVIGDAQPMADGDAVVFMNFRADRARQLTAAFVDPNFDGYEARKPKLSRFVCLTEYDARLPAPVAFGPDDLRNTLGELLAAHGLTQLRIAETEKYAHVTFFFSGGREEPYAGESRILVPSPKVATYDLQPEMSCPEVTAKLVETIRTQAVDVAICNIANPDMVGHTGDLQAAIQAAQAVDKAIGAIAAAVQDVHGALLITADHGNLEMMRDASTGQPHTAHTVGPVPLVYIGPRKASLRAGGALRDVAPTILDLLGLPQPEEMTGRSLLEG
>NZ_AP014940.1|WP_096382173.1|5818449_5819712_-|peptidoglycan-DD-metalloendopeptidase-family-protein
MRTACAWLLVLLAALPPALPQARAAAQGNSRETERKLEKVKTELKSVAAERRKLEGQRGDAAQRLRAADEQVGRSNRVLRDTETRLAREHAALKQTQDKRDALKKTLGTRRQELEQLLRAAYAQGNDAPLKALLSQDRVADSGRILTYHGYLQRDRARRIDELTAQLRELDALEREIVDRRASLDSTRKQQRSQLGQLEKDRKDRAALVAQINEKYEDRSTRERELGRDAKGLEQLLAKLRAAAARAEAQRRAAAKARAEREAREAREAAAAAAKGKPAPVRKPPVQVASAPAPQVGGLGWPVSGALLAGFGGTMPDGRSSEGLLIGAAAGATVKAVGDGTVVYSEWMTGYGLLLIVDHGNGYMSLYANNDALLKDAGATVKKGDAIATVGSSGGHGRPALYFELRRGGQPVNPSVWLRR
>NZ_AP014940.1|WP_096382169.1|5816542_5818186_-|S41-family-peptidase
MSLRHPLRSLLPLALALGAVPALAQQQPAPPAQATPPAASQPAPADDADDADAQDGDQAAPAQAPAKRSAKTGKDDSDSKVPIDEIRRYVAVYNAVKQAYVEPVDDAKLMHSAIRGLLFDLDPHSVYFDKADAESFDEQSRGNYEGIGVELQRQPDGTLRVISPIDDTPAARAGIKAGDLITAIDGKPFKVDEGDSSGPLRGPAGSKVVLTIVREGRDKPFDVTVARETIRVASVKSRMLEPGYGYLRLAQFQADTAADFETHLRKLKEQSGGKLRGLVLDLRSNPGGLLTSAVQIADDLLERGKIVSTRGRIAISDAEFSATPGDMLDGAPLVVLVDAGSASASEVLAGALRDNGRGRVVGSRTFGKGSVQTVLPLDNGDSVKLTTARYYTPSGKSIQALGIVPEVVLRAPKKDKDERPSYTEAALPGHLHGDEEGAPGSNAGEVLEGDAPIASALAELKTPGATARADAQAKASAGKRKAVEAKAAEAKAAEAKAAEFKAAEPKAVGAKATEAKAVDSKAAEPKAVDPKPADPKAAEPKAVEPKR
>NZ_AP014940.1|WP_074872525.1|5816042_5816363_+|DUF1820-family-protein
MSTLYKVTFLNAGKIYELYARKIGAGTLWGFTEISELVFDVHDGLVVDPTEERLRDEFGNTRVLHLPMQSIVRIEEVERKGQSAIRDAASGERVVTPFPLPAKPPR
>NZ_AP014940.1|WP_074872529.1|5815214_5815910_+|rhomboid-family-intramembrane-serine-protease
MFVAIPSRERARLRWATPLLFALLWISFIVSAVVLPDPEQRRLMVEWGALSGGLSSPEAWWNAIRDGSALRLFSALFLHADWAHLLGNLVFLLIFGLPAERAMGPWRLLALFLFGGAVANLAAVIAIATPDRLIIGASGAVSALIGAYLALFPSAKLGVVVPLGVFLQFVKVPAPLLIGVWALLQVVFTFIGPAFGAVAWSAHLAGFAFGGAFALIARAGIARRLRRKRGY
>NZ_AP014940.1|WP_096382164.1|5813570_5814950_-|porin
MQPSHRYIRLTAIALGVAGVISFGSASATGFQIRENSVKNQGRAFAGSAVAEKDASVVSNNPAAMVNLDTTTVRVDVTAIDLTAKFSGGGTAAAGSPLARPLTGGNGGDPGDITAVPAMSIVVPLSGSFEKLTLGAQLSAPFGLKTEYENGWVGRYNALESEVKTIDLTLSAAVKLTDRFSVGAGFIYERAEATLTNAVDFGSAICRVSPAACLTPNPVAAPFGPQKNDGTVKVKGDDNGIGWILGFQWKPTDRLSIGYSHRSEIDHDLEGTVTFTKPGNVSALLGAAGITQYNTGPGGAKLTTPSTDTLSVSYAFNEQFRMMFDAQKTDWHSLQSVNIVRANGTPVASEQFQWDDSMMYALGAEYDLNDRFTLRGGVAKDETPTNDTHRTPRLPDNDRTLYSVGLTWNANEHISVDAAYTRIQIDSPDVNVVSTSGSTLVGKFKGHADLFGIAAQYKF
>NZ_AP014940.1|WP_172437343.1|5812717_5813446_-|MarR-family-transcriptional-regulator
MSDPAYHLRQTALGLERLAGLLRAQQWREPDEHALHPAQRALLELLGEDKRGWRVGELAQRLGVSAASASDTIAALEARELVRRARDPDDGRAVRVHPSRRGLAWLRRSHARGGTGERLLATLAPDDLAAFSRSLQLLILQAQRDGLATGLRTCAGCEFFRPFAGGGESPHYCALVGAAFGDAQLRVDCAEQRPRGMDVGMSAADAVAQRFRAGAGGDNDSHNDKTTRSGRTPPRRHSASAE
>NZ_AP014940.1|WP_074872537.1|5812400_5812637_-|thioredoxin-family-protein
MRQKAVFFHAGCPVCVAAEQQVAEAIDRQRFEVEVVHLGEASARIAEARAAGVASVPALVMQGQVFHINYGAALSDLG
>NZ_AP014940.1|WP_096382155.1|5811644_5812349_-|MOSC-domain-containing-protein
MQASDTGVEVAALLRGRAVPYTRPGSRSGIDKRPLRGRVRIGETGLDGDEQGDLRVHGGPDKAVHHYPREHYRLWREELGVHALLEAPGAFGENLSSEGLTEAQVCLGDRYRFGGALLEVSQARQPCWKLNDRFGVADMARRMQANGRTGWYYRVLETGEAEAGDRLILLERPWPRWSLQRIATMLFVRTLEREELQAALALPLVPSWRKLVEARLARGEVEDWSRRIDGPSKA
>NZ_AP014940.1|WP_096382150.1|5811357_5811612_-|DUF2164-domain-containing-protein
METIRFDDQEKALLVAKLQRYFTEELKQPIGRFDAEFLLDFLSEELGAYYYNRGVADAQAVLTAKAADLADAVWQLERPTEFKR
>NZ_AP014940.1|WP_096382186.1|5822311_5824132_+|M28-family-peptidase
MDLPHAPAAGRPWRFHTLSRPNPLFAATSLVVATLALSACNKPPADGAAPAQPGSDAAATAPAAADHAFDAAINAADFAQHVKVLASDEFEGRAPGSAGEDKTVQYLEAQFKRLGLKPGNGDSYFQTVPMVETTADESTVLKLDVKGQARELKFGTDMVVGTRTGQPEVKVEASDLVFVGYGVNAPEQQWNDYAGVDVKGKTVVMFVNDPGFHGQDATLFEGKRMTYYGRWTYKFEEAARQGAKAALIVHDDAGASYGWDVVKNSWSGAQFDLPAKDDPEPRLPVQGWITADTARKLFADLGQNLDQLYQAAGKRGFKAIPLQATASVDLKSKISEKSSRNVIARLDGAKRPDEAIVYMAHWDHLGHHSEEGGHEGHPAAAKGEGHDTIYNGAVDNASGVAGILEIAEAFSKQTPPPDRSLLFLAVTLEESGLLGSKYYVAHPTVPLDKTVAVINLDAMPIIGKSKDMTVVGFGSSELEDILKTVADGQGRVLHAENTPQDGFYFRSDHFNFAKAGVPALYAKGGDDLLDGGVEAGQKAQVDYRDKRYHKPADEFDPSWKLDGVVQDLDALYGVGKILAGNEQWPNWYSGNAFRAAHDKLMAPAKK
>NZ_AP014940.1|WP_096383819.1|5824290_5824680_+|MAPEG-family-protein
MTIAYWCLLAAALLPYMWTSLAKVYGQRYDNRDPRGWQARQENPRSKAAYAAHLNAFEAFPAFAAGVLGAQMAGVDTGWIDLLAIAFIVFRVLHGVFYLAGKPPLRSAAWAGGFLCVVALLVLAALAAI
>NZ_AP014940.1|WP_096382191.1|5824710_5824899_+|hypothetical-protein
MSKTPVQIHRVAGGDIALWIDDGQSIHMKLRGCDLDPIELNEDEAESFAQTLTRLAQQLRSL
>NZ_AP014940.1|WP_096382195.1|5824992_5825727_+|2OG-Fe-dioxygenase-family-protein
MSAPPTSDHDEFAHSLREQGFRFVAGAEMRGHLLEHGSLQDWDAFADSWNDLAPDVYLAQVGRHRRRRHAVFHALRDGAIERRPHQPHYQSLNYNSLQGDIERWFEPVRDDIAQGESLQTVLGFCRDFFSTLAPQTADWHIELHQFRIEAGPDHEGQPTPEGVHRDGVDYVLVLLIDRHNIVSGTTTIHDRDGSLLGSFTLTAPLDAALVDDARVFHGVTAVTPQDPTREAHRDVLVVTFKAAS
>NZ_AP014940.1|WP_096382200.1|5825826_5827071_-|right-handed-parallel-beta-helix-repeat-containing-protein
MHRRQFMSVPLAAGAAAVSAGVGLAGFPTTALAAAATPSERISVLDFIPVGLRAGVLDGTGTADLTAYIQAAIDTRPGVFLDVQFPTGVYRVDGTLRVLRSHIWLSGENATLLHGGAGDAIQFGDGINRWDRIQIGGFLMGKAQAASAGAMIRSRLCSTVIVRDCYFYGDNKIFDVMSFERGYMIYVHNVISERCLGTHVSISGTGPDGDRLVDLTVYDCRFDYGRTALSGNGYVEGIYFRRNICLRQHNISVSLNGTPQWTIPSVKLQENDFDGGDSIGVQVNYLSNFQFNDNWFSSLQDTALRIDAQAAGGTVSANQFYATPGRSAMEIGGGNVVITGNTISGGNQGLYLRGSSRNVVFTGNAITYMQGSAINLYENPSQVTIVGNNLIGNVGGISSGGTTLNVANNLIAAA
>NZ_AP014940.1|WP_096382204.1|5833556_5834768_-|tyrosine--tRNA-ligase
MSTSVQEALDLIARGADEIIKLEELEARLKLGRPLRIKAGFDPTAPDLHLGHTVLLNKMRQFQDLGHQVIFLIGDFTGMIGDPSGKNATRKALTREDVLANAETYAEQVFKVLDKSRTEVRFNSEWFGQMGAADMIRLAAQHTVARMLERDDFAKRYAGQQPIAIHEFLYPLVQGYDSVALKCDVELGGTDQKFNLLMGRGLQEHHGQPPQIVLTMPLLEGLDGVAKMSKSLGNYIGINEPAIDIVTKAMKIDDTLMWRWIDLLSFEISIAEAARLKQEIEAGQLNPRDLKLRLARELAARFHGAAAAETAVEGWNAAVRGEGDLSSLPLTDVTVPAEGLRIAALLTAAGLTPSNSEANRKLKERAVKVDGQVVEDAQLTFAPGFEGVLTVGKRTFARVRLVS
>NZ_AP014940.1|WP_096382208.1|5834960_5836454_+|M23-family-metallopeptidase
MTVPEQASSVGAERRERLKALREKALKRKVLARHLSDGFNGRWSGRQWVQVGLFATLGMMVAAVIPGFSQSTASVRAHEPRQSLALALPPLTLARLKGETGDSWQLVRVNRGQTLGSVFKDMDIPKSTMSQILEQPGAREALMRMKPGAELGFDIPVNGSLRTFRYDQDEGHRVELSIAGDKVTDKKVIARPSQVRTVVLSGKVGKSLFRSARKVGLTPANINTLTDDIFKYDIDFNEDVGGDDRFSVVVEQTWREGELISTGPILAATFTSDGKLHTGFRFDRGGKPEYFTGDGRPLKKSFIRMPIPYARLTSGFGSRRHPVLGSIRMHAGVDYAAGTGTPIMAAGDARVQFIGWKGGYGRAVILDHGRGYTTLYGHMSNFSKIKPGQRIPQGTVIGYVGASGLATGPHLHYEFRVNGVHRNPLSITMPPPEPLSGVALAQFRQQTAVALGRIRQVENIIYADAGPAPGAAPAVAAAATAKTVAVAKTKKKKTSRG
>NZ_AP014940.1|WP_096382212.1|5836645_5837824_+|anhydro-N-acetylmuramic-acid-kinase
MVDSSSIPADSRVATPGAGLYLGLISGTSADGIDAALVRFEAGAAPTRCELVLGRTYAWDAALRERLVALGQGGDARSLEELGTLDIQTAEAFAEAARALLEEAGVAAAEVAAIGSHGQTVRHRPAGAGFDGRHPFTWQIGDGAVIAERSGIATVADFRRRDVAAGGHGAPLMPAFHAALLGSAGEDRAALNLGGIANFTLLPARGEVRGFDTGPANCLMDAWALRHLGQAFDADGAFAAQGQVDAALLARLLDEPWFALAPPKSTGREQFHLDWVDARLGGGERPQDVQATLLELSAVTIAQALRAQQPATRRVLACGGGVRNGALLARLAALLPQATVETTAAYGLDPDFVEAMGFAWLARQTLAGLPGNLPSVTGARGLRVLGTLHPAA
>NZ_AP014940.1|WP_145960217.1|5838554_5839967_-|AmpG-family-muropeptide-MFS-transporter
MTSEAGASNEPAAAPARPVKKGWRLVLSNLGQPKVLTMLLLGFSSGIPIYLVGNTLGYWMRENGIELSMIGFLSWVGLAYSLKFVWAPLVDKIDAPLLGRWLGRRRGWMLLSQFVAAAALVGMALVEPRQGQLLLGGVALDQLTVFGALALVVAFASATQDIVIDAWRIESADNGEQQGLLTSTSTLGYRGALLVTDSLILILAAHAGWQLSYELMALLLGVGVIATLRAREPRASEIAQAAPHPALFTARGLFDAVIGPFVAFFRQHGRMALLILLAISLYRLPDFLLGPMANPFYADLKMDKETVGAVRGSFGLVATIAGVAAAGLTAVRFGFIPTLIAGAVLGPASNLAFAYLALHGSDSTVFTAAMVIDNFCNGYAGVALVGYMSSLTNIGYTATQYALLSSFYALLGKLLKGLSGVAVTELAAGRTLLEGYALFFVGTALVGLPAVVLCIALALRRPAPADLSRT
>NZ_AP014940.1|WP_096382217.1|5839956_5840730_-|exodeoxyribonuclease-III
MRIISFNANGLRSATTKGFFDWFKTQHADVLCVQETKAQEHQLSGPEFLPDGYRAFFRDAITKKGYSGVAIYAKREPDEVRTALGWAPFDDEGRYIEARFGNLSVVSFYIPSGSSGDLRQGFKFEVMEWLKPILDQWLASGRDYVLCGDWNIVRSRLDIKNWTSNQKNSGCLPPERDWLNGVCADDSGWVDAYRALNAEGQDYTWWSNRGAARANDVGWRIDYQFATPSLRAKLRGCSILKDPRFSDHAPFTVDYDL

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Crispr_ID: NZ_AP014940_18

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_18

5837938-5838073

Orphan

Consensus_repeat	Method
GGCGCCGTGGTTCGGGTTGACGCGGTCGCGGCTTGCGCC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP014940_18

>merge|NZ_AP014940|18|5837938-5838073|CRISPRCasFinder
GGCGCCGTGGTTCGGGTTGACGCGGTCGCGGCTTGCGCCGCTCCTACAGGGAGTTATCGGGGCATCCGGAAATCTGGCGGGTTGGGCTTTGGGAGGCGGCGCCGTGGTTCGGGTTGGCGCGGTCGCGGCTTGCGCC

>NZ_AP014940|18|17|5837938-5838073|CRISPRCasFinder
GGCGCCGTGGTTCGGGTTGACGCGGTCGCGGCTTGCGCC	GCTCCTACAGGGAGTTATCGGGGCATCCGGAAATCTGGCGGGTTGGGCTTTGGGAGGC
GGCGCCGTGGTTCGGGTTGGCGCGGTCGCGGCTTGCGCC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_096382177.1\|5819711_5821247_-\|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase	unknown	unknown	gnl\|CDD\|235463
NZ_AP014940.1\|WP_096382237.1\|5849900_5850833_+\|SPOR-domain-containing-protein	unknown	unknown	gnl\|CDD\|225629
NZ_AP014940.1\|WP_096382195.1\|5824992_5825727_+\|2OG-Fe-dioxygenase-family-protein	unknown	unknown	gnl\|CDD\|370779
NZ_AP014940.1\|WP_096382182.1\|5821481_5822147_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|226123
NZ_AP014940.1\|WP_096382217.1\|5839956_5840730_-\|exodeoxyribonuclease-III	unknown	unknown	gnl\|CDD\|197336
NZ_AP014940.1\|WP_074870911.1\|5841362_5842019_+\|orotate-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|234771
NZ_AP014940.1\|WP_145960217.1\|5838554_5839967_-\|AmpG-family-muropeptide-MFS-transporter	unknown	unknown	gnl\|CDD\|341039
NZ_AP014940.1\|WP_096382208.1\|5834960_5836454_+\|M23-family-metallopeptidase	unknown	unknown	gnl\|CDD\|366703
NZ_AP014940.1\|WP_172437344.1\|5840796_5841366_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_AP014940.1\|WP_096382227.1\|5842156_5842804_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_074871389.1\|5845470_5845929_-\|dUTP-diphosphatase	unknown	unknown	gnl\|CDD\|234802
NZ_AP014940.1\|WP_096382212.1\|5836645_5837824_+\|anhydro-N-acetylmuramic-acid-kinase	unknown	unknown	gnl\|CDD\|236579
NZ_AP014940.1\|WP_096383823.1\|5842927_5845147_-\|phosphomannomutase/phosphoglucomutase	unknown	unknown	gnl\|CDD\|100091
NZ_AP014940.1\|WP_096382200.1\|5825826_5827071_-\|right-handed-parallel-beta-helix-repeat-containing-protein	unknown	unknown	gnl\|CDD\|379079
NZ_AP014940.1\|WP_074870919.1\|5847380_5848055_+\|DNA-repair-protein-RadC	unknown	unknown	gnl\|CDD\|178801
NZ_AP014940.1\|WP_096383819.1\|5824290_5824680_+\|MAPEG-family-protein	unknown	unknown	gnl\|CDD\|226211
NZ_AP014940.1\|WP_096382186.1\|5822311_5824132_+\|M28-family-peptidase	unknown	unknown	gnl\|CDD\|349910
NZ_AP014940.1\|WP_096382232.1\|5848211_5849900_+\|arginine--tRNA-ligase	unknown	unknown	gnl\|CDD\|234964
NZ_AP014940.1\|WP_096382191.1\|5824710_5824899_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096382204.1\|5833556_5834768_-\|tyrosine--tRNA-ligase	unknown	unknown	gnl\|CDD\|235645

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_096382177.1\|5819711_5821247_-\|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase	gnl\|CDD\|235463	PRK05434, PRK05434, 2,3-bisphosphoglycerate-independent phosphoglycerate mutase.	0
NZ_AP014940.1\|WP_096382237.1\|5849900_5850833_+\|SPOR-domain-containing-protein	gnl\|CDD\|225629	COG3087, FtsN, Cell division protein [Cell division and chromosome partitioning].	6.30914e-15
NZ_AP014940.1\|WP_096382195.1\|5824992_5825727_+\|2OG-Fe-dioxygenase-family-protein	gnl\|CDD\|370779	pfam10014, 2OG-Fe_Oxy_2, 2OG-Fe dioxygenase. This family contains 2-oxoglutarate (2OG) and Fe-dependent dioxygenases. It includes L-isoleucine dioxygenase (IDO).	1.40279e-84
NZ_AP014940.1\|WP_096382182.1\|5821481_5822147_+\|hypothetical-protein	gnl\|CDD\|226123	COG3595, COG3595, Uncharacterized conserved protein [Function unknown].	4.50727e-05
NZ_AP014940.1\|WP_096382217.1\|5839956_5840730_-\|exodeoxyribonuclease-III	gnl\|CDD\|197336	cd10281, Nape_like_AP-endo, Neisseria meningitides Nape-like subfamily of the ExoIII family purinic/apyrimidinic (AP) endonucleases. This subfamily includes Neisseria meningitides Nape and related proteins. These are Escherichia coli exonuclease III (ExoIII)-like AP endonucleases and belong to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds. AP endonucleases participate in the DNA base excision repair (BER) pathway. AP sites are one of the most common lesions in cellular DNA. During BER the damaged DNA is first recognized by DNA glycosylase. AP endonucleases then catalyze the hydrolytic cleavage of the phosphodiester bond 5' to the AP site, and this is followed by the coordinated actions of DNA polymerase, deoxyribose phosphatase, and DNA ligase. If left unrepaired, AP sites block DNA replication, and have both mutagenic and cytotoxic effects. AP endonucleases can carry out a variety of excision and incision reactions on DNA, including 3'-5' exonuclease, 3'-deoxyribose phosphodiesterase, 3'-phosphatase, and occasionally, nonspecific DNase activities. Different AP endonuclease enzymes catalyze the different reactions with different efficiences. Many organisms have two AP endonucleases, usually one is the dominant AP endonuclease, the other has weak AP endonuclease activity; for example, Neisseria meningitides Nape and NExo. Nape, found in this subfamily, is the dominant AP endonuclease. It exhibits strong AP endonuclease activity, and also exhibits 3'-5'exonuclease and 3'-deoxyribose phosphodiesterase activities.	2.34607e-143
NZ_AP014940.1\|WP_074870911.1\|5841362_5842019_+\|orotate-phosphoribosyltransferase	gnl\|CDD\|234771	PRK00455, pyrE, orotate phosphoribosyltransferase; Validated.	1.61235e-74
NZ_AP014940.1\|WP_145960217.1\|5838554_5839967_-\|AmpG-family-muropeptide-MFS-transporter	gnl\|CDD\|341039	cd17486, MFS_AmpG_like, AmpG and similar transporters of the Major Facilitator Superfamily. AmpG acts as an inner membrane permease in the beta-lactamase induction system and in peptidoglycan recycling. It transports meuropeptide from the periplasm into the cytosol in gram-negative bacteria, which is essential for the induction of the ampC encoding beta-lactamase. The AmpG family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.20753e-107
NZ_AP014940.1\|WP_096382208.1\|5834960_5836454_+\|M23-family-metallopeptidase	gnl\|CDD\|366703	pfam01551, Peptidase_M23, Peptidase family M23. Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.	4.58201e-43
NZ_AP014940.1\|WP_172437344.1\|5840796_5841366_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	6.55578e-11
NZ_AP014940.1\|WP_074871389.1\|5845470_5845929_-\|dUTP-diphosphatase	gnl\|CDD\|234802	PRK00601, dut, dUTP diphosphatase.	5.66909e-84
NZ_AP014940.1\|WP_096382212.1\|5836645_5837824_+\|anhydro-N-acetylmuramic-acid-kinase	gnl\|CDD\|236579	PRK09585, anmK, anhydro-N-acetylmuramic acid kinase; Reviewed.	0
NZ_AP014940.1\|WP_096383823.1\|5842927_5845147_-\|phosphomannomutase/phosphoglucomutase	gnl\|CDD\|100091	cd03089, PMM_PGM, The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.	0
NZ_AP014940.1\|WP_096382200.1\|5825826_5827071_-\|right-handed-parallel-beta-helix-repeat-containing-protein	gnl\|CDD\|379079	pfam13229, Beta_helix, Right handed beta helix region. This region contains a parallel beta helix region that shares some similarity with Pectate lyases.	3.06987e-10
NZ_AP014940.1\|WP_074870919.1\|5847380_5848055_+\|DNA-repair-protein-RadC	gnl\|CDD\|178801	PRK00024, PRK00024, DNA repair protein RadC.	6.60267e-109
NZ_AP014940.1\|WP_096383819.1\|5824290_5824680_+\|MAPEG-family-protein	gnl\|CDD\|226211	COG3686, COG3686, Predicted membrane protein [Function unknown].	5.80834e-29
NZ_AP014940.1\|WP_096382186.1\|5822311_5824132_+\|M28-family-peptidase	gnl\|CDD\|349910	cd05660, M28_like_PA, M28 Zn-peptidase containing a protease-associated (PA) domain insert. Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They have co-catalytic zinc ions; each zinc ion is tetrahedrally co-ordinated, with three amino acid ligands plus activated water; one aspartate residue binds both metal ions. This subfamily is composed of uncharacterized proteins containing a protease-associated (PA) domain insert which may participate in substrate binding and/or promote conformational changes, influencing the stability and accessibility of the site to substrate.	7.0577e-109
NZ_AP014940.1\|WP_096382232.1\|5848211_5849900_+\|arginine--tRNA-ligase	gnl\|CDD\|234964	PRK01611, argS, arginyl-tRNA synthetase; Reviewed.	0
NZ_AP014940.1\|WP_096382204.1\|5833556_5834768_-\|tyrosine--tRNA-ligase	gnl\|CDD\|235645	PRK05912, PRK05912, tyrosyl-tRNA synthetase; Validated.	0

>NZ_AP014940.1|WP_096382212.1|5836645_5837824_+|anhydro-N-acetylmuramic-acid-kinase
MVDSSSIPADSRVATPGAGLYLGLISGTSADGIDAALVRFEAGAAPTRCELVLGRTYAWDAALRERLVALGQGGDARSLEELGTLDIQTAEAFAEAARALLEEAGVAAAEVAAIGSHGQTVRHRPAGAGFDGRHPFTWQIGDGAVIAERSGIATVADFRRRDVAAGGHGAPLMPAFHAALLGSAGEDRAALNLGGIANFTLLPARGEVRGFDTGPANCLMDAWALRHLGQAFDADGAFAAQGQVDAALLARLLDEPWFALAPPKSTGREQFHLDWVDARLGGGERPQDVQATLLELSAVTIAQALRAQQPATRRVLACGGGVRNGALLARLAALLPQATVETTAAYGLDPDFVEAMGFAWLARQTLAGLPGNLPSVTGARGLRVLGTLHPAA
>NZ_AP014940.1|WP_096382208.1|5834960_5836454_+|M23-family-metallopeptidase
MTVPEQASSVGAERRERLKALREKALKRKVLARHLSDGFNGRWSGRQWVQVGLFATLGMMVAAVIPGFSQSTASVRAHEPRQSLALALPPLTLARLKGETGDSWQLVRVNRGQTLGSVFKDMDIPKSTMSQILEQPGAREALMRMKPGAELGFDIPVNGSLRTFRYDQDEGHRVELSIAGDKVTDKKVIARPSQVRTVVLSGKVGKSLFRSARKVGLTPANINTLTDDIFKYDIDFNEDVGGDDRFSVVVEQTWREGELISTGPILAATFTSDGKLHTGFRFDRGGKPEYFTGDGRPLKKSFIRMPIPYARLTSGFGSRRHPVLGSIRMHAGVDYAAGTGTPIMAAGDARVQFIGWKGGYGRAVILDHGRGYTTLYGHMSNFSKIKPGQRIPQGTVIGYVGASGLATGPHLHYEFRVNGVHRNPLSITMPPPEPLSGVALAQFRQQTAVALGRIRQVENIIYADAGPAPGAAPAVAAAATAKTVAVAKTKKKKTSRG
>NZ_AP014940.1|WP_096382204.1|5833556_5834768_-|tyrosine--tRNA-ligase
MSTSVQEALDLIARGADEIIKLEELEARLKLGRPLRIKAGFDPTAPDLHLGHTVLLNKMRQFQDLGHQVIFLIGDFTGMIGDPSGKNATRKALTREDVLANAETYAEQVFKVLDKSRTEVRFNSEWFGQMGAADMIRLAAQHTVARMLERDDFAKRYAGQQPIAIHEFLYPLVQGYDSVALKCDVELGGTDQKFNLLMGRGLQEHHGQPPQIVLTMPLLEGLDGVAKMSKSLGNYIGINEPAIDIVTKAMKIDDTLMWRWIDLLSFEISIAEAARLKQEIEAGQLNPRDLKLRLARELAARFHGAAAAETAVEGWNAAVRGEGDLSSLPLTDVTVPAEGLRIAALLTAAGLTPSNSEANRKLKERAVKVDGQVVEDAQLTFAPGFEGVLTVGKRTFARVRLVS
>NZ_AP014940.1|WP_096382200.1|5825826_5827071_-|right-handed-parallel-beta-helix-repeat-containing-protein
MHRRQFMSVPLAAGAAAVSAGVGLAGFPTTALAAAATPSERISVLDFIPVGLRAGVLDGTGTADLTAYIQAAIDTRPGVFLDVQFPTGVYRVDGTLRVLRSHIWLSGENATLLHGGAGDAIQFGDGINRWDRIQIGGFLMGKAQAASAGAMIRSRLCSTVIVRDCYFYGDNKIFDVMSFERGYMIYVHNVISERCLGTHVSISGTGPDGDRLVDLTVYDCRFDYGRTALSGNGYVEGIYFRRNICLRQHNISVSLNGTPQWTIPSVKLQENDFDGGDSIGVQVNYLSNFQFNDNWFSSLQDTALRIDAQAAGGTVSANQFYATPGRSAMEIGGGNVVITGNTISGGNQGLYLRGSSRNVVFTGNAITYMQGSAINLYENPSQVTIVGNNLIGNVGGISSGGTTLNVANNLIAAA
>NZ_AP014940.1|WP_096382195.1|5824992_5825727_+|2OG-Fe-dioxygenase-family-protein
MSAPPTSDHDEFAHSLREQGFRFVAGAEMRGHLLEHGSLQDWDAFADSWNDLAPDVYLAQVGRHRRRRHAVFHALRDGAIERRPHQPHYQSLNYNSLQGDIERWFEPVRDDIAQGESLQTVLGFCRDFFSTLAPQTADWHIELHQFRIEAGPDHEGQPTPEGVHRDGVDYVLVLLIDRHNIVSGTTTIHDRDGSLLGSFTLTAPLDAALVDDARVFHGVTAVTPQDPTREAHRDVLVVTFKAAS
>NZ_AP014940.1|WP_096382191.1|5824710_5824899_+|hypothetical-protein
MSKTPVQIHRVAGGDIALWIDDGQSIHMKLRGCDLDPIELNEDEAESFAQTLTRLAQQLRSL
>NZ_AP014940.1|WP_096383819.1|5824290_5824680_+|MAPEG-family-protein
MTIAYWCLLAAALLPYMWTSLAKVYGQRYDNRDPRGWQARQENPRSKAAYAAHLNAFEAFPAFAAGVLGAQMAGVDTGWIDLLAIAFIVFRVLHGVFYLAGKPPLRSAAWAGGFLCVVALLVLAALAAI
>NZ_AP014940.1|WP_096382186.1|5822311_5824132_+|M28-family-peptidase
MDLPHAPAAGRPWRFHTLSRPNPLFAATSLVVATLALSACNKPPADGAAPAQPGSDAAATAPAAADHAFDAAINAADFAQHVKVLASDEFEGRAPGSAGEDKTVQYLEAQFKRLGLKPGNGDSYFQTVPMVETTADESTVLKLDVKGQARELKFGTDMVVGTRTGQPEVKVEASDLVFVGYGVNAPEQQWNDYAGVDVKGKTVVMFVNDPGFHGQDATLFEGKRMTYYGRWTYKFEEAARQGAKAALIVHDDAGASYGWDVVKNSWSGAQFDLPAKDDPEPRLPVQGWITADTARKLFADLGQNLDQLYQAAGKRGFKAIPLQATASVDLKSKISEKSSRNVIARLDGAKRPDEAIVYMAHWDHLGHHSEEGGHEGHPAAAKGEGHDTIYNGAVDNASGVAGILEIAEAFSKQTPPPDRSLLFLAVTLEESGLLGSKYYVAHPTVPLDKTVAVINLDAMPIIGKSKDMTVVGFGSSELEDILKTVADGQGRVLHAENTPQDGFYFRSDHFNFAKAGVPALYAKGGDDLLDGGVEAGQKAQVDYRDKRYHKPADEFDPSWKLDGVVQDLDALYGVGKILAGNEQWPNWYSGNAFRAAHDKLMAPAKK
>NZ_AP014940.1|WP_096382182.1|5821481_5822147_+|hypothetical-protein
MTRTRLSFCLSALIVLSSGAAYASDDVSKVNGSITVDAGQTRGDLDTVNGSIRIGDNASVDEAKTVNGSISVGNNSRANRLETVNGSIRAGTKLTASGGLETVNGGIFVDRGGRLGGDVSTVNGSIGLVATELNGGIDTVNGDVTVGVDSHVTGGIKYTKPNGISFRQQRDPVVIIGPNARVDGPLVFERPVKLYVHASAKTGAIRGATAVAFTGTTPPGQ
>NZ_AP014940.1|WP_096382177.1|5819711_5821247_-|2,3-bisphosphoglycerate-independent-phosphoglycerate-mutase
MSATSCPKPVVLLILDGWGHRDDPADNALAQAELPNWRALLASQAHTLIHTEGRHVGLPDGQMGNSEVGHMNLGAGRIVYQDLTRIDAAIEDGSFYANDELRAACAAAKAAGTTLHLLGLLSPGGVHSHERHIFAMIELARREGVAKVAVHAFLDGRDMPPKSAAPSLQRLQQACDEAGNARIASIGGRYYAMDRDKRWDRQLRAWDAIVEAKSEHHAATALEGLDAAYARGETDEFVAPTVIGDAQPMADGDAVVFMNFRADRARQLTAAFVDPNFDGYEARKPKLSRFVCLTEYDARLPAPVAFGPDDLRNTLGELLAAHGLTQLRIAETEKYAHVTFFFSGGREEPYAGESRILVPSPKVATYDLQPEMSCPEVTAKLVETIRTQAVDVAICNIANPDMVGHTGDLQAAIQAAQAVDKAIGAIAAAVQDVHGALLITADHGNLEMMRDASTGQPHTAHTVGPVPLVYIGPRKASLRAGGALRDVAPTILDLLGLPQPEEMTGRSLLEG
>NZ_AP014940.1|WP_145960217.1|5838554_5839967_-|AmpG-family-muropeptide-MFS-transporter
MTSEAGASNEPAAAPARPVKKGWRLVLSNLGQPKVLTMLLLGFSSGIPIYLVGNTLGYWMRENGIELSMIGFLSWVGLAYSLKFVWAPLVDKIDAPLLGRWLGRRRGWMLLSQFVAAAALVGMALVEPRQGQLLLGGVALDQLTVFGALALVVAFASATQDIVIDAWRIESADNGEQQGLLTSTSTLGYRGALLVTDSLILILAAHAGWQLSYELMALLLGVGVIATLRAREPRASEIAQAAPHPALFTARGLFDAVIGPFVAFFRQHGRMALLILLAISLYRLPDFLLGPMANPFYADLKMDKETVGAVRGSFGLVATIAGVAAAGLTAVRFGFIPTLIAGAVLGPASNLAFAYLALHGSDSTVFTAAMVIDNFCNGYAGVALVGYMSSLTNIGYTATQYALLSSFYALLGKLLKGLSGVAVTELAAGRTLLEGYALFFVGTALVGLPAVVLCIALALRRPAPADLSRT
>NZ_AP014940.1|WP_096382217.1|5839956_5840730_-|exodeoxyribonuclease-III
MRIISFNANGLRSATTKGFFDWFKTQHADVLCVQETKAQEHQLSGPEFLPDGYRAFFRDAITKKGYSGVAIYAKREPDEVRTALGWAPFDDEGRYIEARFGNLSVVSFYIPSGSSGDLRQGFKFEVMEWLKPILDQWLASGRDYVLCGDWNIVRSRLDIKNWTSNQKNSGCLPPERDWLNGVCADDSGWVDAYRALNAEGQDYTWWSNRGAARANDVGWRIDYQFATPSLRAKLRGCSILKDPRFSDHAPFTVDYDL
>NZ_AP014940.1|WP_172437344.1|5840796_5841366_+|GNAT-family-N-acetyltransferase
MTLDPDIAAAAGERPAPPEVRVGVVSPMLAPAVRALQVAPEQLQFVGDTAYNLEQTRLDPNSEAMAVLAGERVVGFYRLDFSVEAIAGRALGEPSVGLRAYAIDRREQGRGYGTAAMRACIEDLRRRHPQRRLLALTVNVRNQAAIAVYLKAGFYDTGELYHGGSAGPQHLMLYRLAAAPSPSPTATAP
>NZ_AP014940.1|WP_074870911.1|5841362_5842019_+|orotate-phosphoribosyltransferase
MTDHRTRFLQLALKADALRFGEFTLKSGRVSPYFFNAGRFDSGAALAELAQCYADAVQSHGLDFDLLFGPAYKGIPLATALGCEYARRGRDLPLAFNRKEAKSHGEGGMLIGAPLAGRRVLIVDDVITAGTAIREALGLIADAGGTVAGIVIALDRQEAVDPAQSRRSAAETVAIEHGLPVVAIAGLDDLLAFTGASAEFAAQRERLLAYRAAYGRQA
>NZ_AP014940.1|WP_096382227.1|5842156_5842804_+|hypothetical-protein
MKAIHTLIAGAVVLALAAPLASAQDASKKKLYCWDEGGRKVCGDALPAHAVDSARTEISAKSGLATAQVGRAMSAEERTAAEQAARAARSAATAAEAQKRRDRAMAESYATEDDLRKSFQERIVLLDETVKASQLGIEGRRQTVLSLLRKAGEAELNGKPVGSGLAENIRGQHDELLHQQDVLKQQVLERSLADQDLATALERYNALKAKNAAGG
>NZ_AP014940.1|WP_096383823.1|5842927_5845147_-|phosphomannomutase/phosphoglucomutase
MAWAGVQQHLDSSRRADLIQVRDAAVSNAHNALGVEHKRLRDRLAAAPMQAALQAGDFKAASAELGKDWPGASHGEVLPADLAAEYAALPKSGYGRLGAMEAAIVADKPMAAIVRDGGKPVLALAAPARAGEQLVGVAYVQLPLQRVSQGVEQADIGDSSYLALRQGGFSAIERGDAALNNGAEAMAAAIPGSDLRVAAAVPDIAGGPLGMGALPCFIAAVVLTLLAFVLARLRQRLGRSSGPVEEEGPVQTLAETMSAPIADANAINVSDNTLEAAPRPLAVDNGIFRAYDIRGVVGQSLDPGIAELIGHAIGSVMHDQGLTEIVVGRDGRLSGPSLMAGLIAGLRKAGRNVVDIGLAPTPVTYFGAYHLRAGSCVSLTGSHNPPDYNGFKIVVGGETLSGDAITDLYRRIVGGRLHTAAEPGTLAERDISEDYVQRIASDIQIDRPLKVVVDAGNGVAGDIGPRVLAAIGAEVTPLYCEIDGEFPNHHPDPSEPHNLVDLIKMVQRLDADLGIAFDGDGDRLGVVTRDGQNIFPDRLLMLFAADVLERNPGAMIIYDVKCTGRLPGHILRHGGSPLMWKTGHSLIKAKMRETDAELAGEMSGHFFFKERWYGFDDGIYSAARLLEILAAQADTPTRTLNELPNGVATPEIKVDAPEGDPHSFVERFRNEASFEGARLSTIDGLRVDFPDGWGLVRASNTTPILVMRFDADNQAAMERIQGLFRAQLHAIKPDLALPF
>NZ_AP014940.1|WP_074871389.1|5845470_5845929_-|dUTP-diphosphatase
MHHTLELKILDPRFGNEWPLPAYATPASAGLDLRAALEQELVLQPGDAALLPSGLAVHVGDPAMCAVVLPRSGLGHKHGIVLGNGTGLIDADYQGPLLISVWNRGREAYTIQPGDRVAQLVVLPIVRASLQVVEQFQASERGEGGFGHTGVR
>NZ_AP014940.1|WP_074870919.1|5847380_5848055_+|DNA-repair-protein-RadC
MRIQEWPSAERPREKLLAGGAGALSDAELLALILGSGVRGHDAVGTARRLLAEHGPLASLLEQPPARLLRMRGIGTARACALKAALELAARSQMADLERGGAVTDPPSAGRYLAQRLRGRPHEVFAAMFLNSRHAVIGFEELFQGTVDGAEVHPRVLVRRAMHHNAAAVIVGHNHPSGHAEPSASDRAVTQRLKQALALIDVRLIDHFVIGDGKPVSMAIRGWV
>NZ_AP014940.1|WP_096382232.1|5848211_5849900_+|arginine--tRNA-ligase
MKTTLHALVAQAIDALRAAGTVPADLSTPDFVIERPKNRGQGDFSTNAAMLLAKPARANPRELAQKLVEALPANGDIGKVEIAGPGFINFHVDEAAWRRQIGEVFAQGANYGRNDSGAGRRAGVEFVSANPTGPLHVGHGRAGVIGDCIARVLDANGWDVAREFYYNDAGVQINNLALSVQARARGLKPGDEGWPESAYNGDYIADVARAYLDGATVECENRSITGKGDIDDLDAIRQFAVASLRREQNEDLAAFGVGFDVYFLESSLYETDKVEETVRELIAHGHTYEEGGALWLRSTDFGDDKDRVMRKSDGSYTYFVPDVAYHLSKWQRGYLRAITELGSDHHGSLARVRAGLQALDAGIPQGWPEYVLHQMVTVMRSGEEVKLSKRAGSYLTLRDLIDEAGRDAVRWFLIARKPDSQLTFDIDLARSQSMDNPVYYVQVSHARMHGLMRQLSERGLSYDQADGLAQPLDLNDVAAHELIVTILRYPDVVAAAGRDLEPHQTAAYLLELAQAFQTYYNDHQFLVDDAAQRHARLVLAMATRQVLANGMELLGIHAPEVM
>NZ_AP014940.1|WP_096382237.1|5849900_5850833_+|SPOR-domain-containing-protein
MAARRGKSQAKRNHQSNDGLPGWVWGVLGLLLGVLLILVVPKYLKSDGKGDGFFRPQPNPDAQPAAVSAEEESVAPEGNAKPARTEAAQAKAGKPDKGGKPKDGPEYDFYTLLPGREVEMSDAELAATEAAEEQRRAAQQRRAGQTAAAHPNPDAAQPRTAAQTQAPATANLPKPVDTIAPAPSRPPTQVATATPPSSTVTPKPPTVSATQGGAGTPAAAATTASAAAAAVSDNTRYLLQAGAFQASGQAEEMKAKIAMLGLGARVESAQIGDKTVYRVRMGPYGTAGDLADAKRKLADGGLPGMAIKVQ

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Crispr_ID: NZ_AP014940_19

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_19

5890658-5890763

Orphan

Consensus_repeat	Method
TTCCGGCTTTCGCCGGAATGACGGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP014940_19

>merge|NZ_AP014940|19|5890658-5890763|CRISPRCasFinder
TTCCGGCTTTCGCCGGAATGACGGCGGCGTGGGGGCGCGGGCTTCGGGAGACCATGGCGGAGCCGCGTCGCTGCGGTTGGATTCCGGCTTTCGCCGGAATGACGGC

>NZ_AP014940|19|18|5890658-5890763|CRISPRCasFinder
TTCCGGCTTTCGCCGGAATGACGGC	GGCGTGGGGGCGCGGGCTTCGGGAGACCATGGCGGAGCCGCGTCGCTGCGGTTGGA
TTCCGGCTTTCGCCGGAATGACGGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_096382331.1\|5881428_5881671_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096382345.1\|5891067_5891712_-\|1-acyl-sn-glycerol-3-phosphate-acyltransferase	unknown	unknown	gnl\|CDD\|153250
NZ_AP014940.1\|WP_096382327.1\|5880302_5881082_+\|PhzF-family-phenazine-biosynthesis-protein	unknown	unknown	gnl\|CDD\|223461
NZ_AP014940.1\|WP_096383825.1\|5883245_5884868_-\|malate-synthase-A	unknown	unknown	gnl\|CDD\|236432
NZ_AP014940.1\|WP_096382357.1\|5897477_5899163_-\|ubiquinone-biosynthesis-regulatory-protein-kinase-UbiB	unknown	unknown	gnl\|CDD\|235310
NZ_AP014940.1\|WP_096382315.1\|5874196_5876725_-\|putative-peptide-modification-system-cyclase	unknown	unknown	gnl\|CDD\|275303
NZ_AP014940.1\|WP_172437345.1\|5893164_5893947_-\|pseudouridylate-synthase	unknown	unknown	gnl\|CDD\|211333
NZ_AP014940.1\|WP_096382318.1\|5876748_5877798_-\|GGDEF-domain-containing-protein	unknown	unknown	gnl\|CDD\|143635
NZ_AP014940.1\|WP_096382322.1\|5878113_5880192_+\|S9-family-peptidase	unknown	unknown	gnl\|CDD\|224423
NZ_AP014940.1\|WP_074870986.1\|5891758_5892163_-\|aminoacyl-tRNA-hydrolase	unknown	unknown	gnl\|CDD\|181730
NZ_AP014940.1\|WP_096382362.1\|5899302_5899962_-\|SCP2-sterol-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|225706
NZ_AP014940.1\|WP_096382341.1\|5889482_5890202_+\|GntR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224715
NZ_AP014940.1\|WP_096383827.1\|5886167_5888744_-\|collagenase	unknown	unknown	gnl\|CDD\|366791
NZ_AP014940.1\|WP_096382354.1\|5894049_5896827_+\|insulinase-family-protein	unknown	unknown	gnl\|CDD\|223685
NZ_AP014940.1\|WP_096382376.1\|5903040_5903943_-\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|179147
NZ_AP014940.1\|WP_096382350.1\|5892373_5893042_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096382372.1\|5901369_5903031_-\|AMP-binding-protein	unknown	unknown	gnl\|CDD\|236443
NZ_AP014940.1\|WP_096382337.1\|5884878_5885982_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|223656
NZ_AP014940.1\|WP_096382367.1\|5900176_5901163_-\|NAD-dependent-epimerase/dehydratase-family-protein	unknown	unknown	gnl\|CDD\|187552
NZ_AP014940.1\|WP_096382333.1\|5881782_5883084_-\|isocitrate-lyase	unknown	unknown	gnl\|CDD\|237893

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_096382327.1\|5880302_5881082_+\|PhzF-family-phenazine-biosynthesis-protein	gnl\|CDD\|223461	COG0384, COG0384, Predicted epimerase, PhzC/PhzF homolog [General function prediction only].	1.11726e-69
NZ_AP014940.1\|WP_096382345.1\|5891067_5891712_-\|1-acyl-sn-glycerol-3-phosphate-acyltransferase	gnl\|CDD\|153250	cd07988, LPLAT_ABO13168-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ABO13168. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are uncharacterized phospholipid/glycerol acyltransferases such as the Acinetobacter baumannii ATCC 17978 locus ABO13168 putative acyltransferase, and similar proteins.	9.51815e-70
NZ_AP014940.1\|WP_096382362.1\|5899302_5899962_-\|SCP2-sterol-binding-domain-containing-protein	gnl\|CDD\|225706	COG3165, COG3165, Uncharacterized protein conserved in bacteria [Function unknown].	5.34241e-41
NZ_AP014940.1\|WP_096383825.1\|5883245_5884868_-\|malate-synthase-A	gnl\|CDD\|236432	PRK09255, PRK09255, malate synthase; Validated.	0
NZ_AP014940.1\|WP_096382357.1\|5897477_5899163_-\|ubiquinone-biosynthesis-regulatory-protein-kinase-UbiB	gnl\|CDD\|235310	PRK04750, ubiB, putative ubiquinone biosynthesis protein UbiB; Reviewed.	0
NZ_AP014940.1\|WP_096382315.1\|5874196_5876725_-\|putative-peptide-modification-system-cyclase	gnl\|CDD\|275303	TIGR04510, mod_pep_cyc, putative peptide modification system cyclase. Members of this family show homology to mononucleotidyl cyclases and to tetratricopeptide repeat (TPR) proteins. Members occur in next to two other markers of ribosomal peptide modification systems. One is a dehydrogenase related to SagB proteins from thiazole/oxazole modification systems. The other is the putative precursor, related to the nitrile hydratase-related leader peptide (NHLP) and nitrile hydratase alpha subunit families. These systems occur in many species of Xanthomonas and Stenotrophomonas, among others.	0
NZ_AP014940.1\|WP_172437345.1\|5893164_5893947_-\|pseudouridylate-synthase	gnl\|CDD\|211333	cd02563, PseudoU_synth_TruC, tRNA pseudouridine isomerase C. Pseudouridine synthases catalyze the isomerization of specific uridines in an tRNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. TruC makes psi65 in tRNAs. This psi residue is not universally conserved.	1.87497e-76
NZ_AP014940.1\|WP_096382318.1\|5876748_5877798_-\|GGDEF-domain-containing-protein	gnl\|CDD\|143635	cd01949, GGDEF, Diguanylate-cyclase (DGC) or GGDEF domain. Diguanylate-cyclase (DGC) or GGDEF domain: Originally named after a conserved residue pattern, and initially described as a domain of unknown function 1 (DUF1). This domain is widely present in bacteria, linked to a wide range of non-homologous domains in a variety of cell signaling proteins. The domain shows homology to the adenylyl cyclase catalytic domain. This correlates with the functional information available on two GGDEF-containing proteins, namely diguanylate cyclase and phosphodiesterase A of Acetobacter xylinum, both of which regulate the turnover of cyclic diguanosine monophosphate. Together with the EAL domain, GGDEF might be involved in regulating cell surface adhesion in bacteria.	1.4187e-45
NZ_AP014940.1\|WP_096382322.1\|5878113_5880192_+\|S9-family-peptidase	gnl\|CDD\|224423	COG1506, DAP2, Dipeptidyl aminopeptidases/acylaminoacyl-peptidases [Amino acid transport and metabolism].	2.09427e-84
NZ_AP014940.1\|WP_074870986.1\|5891758_5892163_-\|aminoacyl-tRNA-hydrolase	gnl\|CDD\|181730	PRK09256, PRK09256, aminoacyl-tRNA hydrolase.	1.5762e-60
NZ_AP014940.1\|WP_096382376.1\|5903040_5903943_-\|alpha/beta-fold-hydrolase	gnl\|CDD\|179147	PRK00870, PRK00870, haloalkane dehalogenase; Provisional.	1.11746e-39
NZ_AP014940.1\|WP_096382341.1\|5889482_5890202_+\|GntR-family-transcriptional-regulator	gnl\|CDD\|224715	COG1802, GntR, Transcriptional regulators [Transcription].	6.92567e-39
NZ_AP014940.1\|WP_096383827.1\|5886167_5888744_-\|collagenase	gnl\|CDD\|366791	pfam01752, Peptidase_M9, Collagenase. This family of enzymes break down collagens.	8.42016e-145
NZ_AP014940.1\|WP_096382354.1\|5894049_5896827_+\|insulinase-family-protein	gnl\|CDD\|223685	COG0612, PqqL, Predicted Zn-dependent peptidases [General function prediction only].	3.84265e-74
NZ_AP014940.1\|WP_096382372.1\|5901369_5903031_-\|AMP-binding-protein	gnl\|CDD\|236443	PRK09274, PRK09274, peptide synthase; Provisional.	0
NZ_AP014940.1\|WP_096382337.1\|5884878_5885982_+\|LysR-family-transcriptional-regulator	gnl\|CDD\|223656	COG0583, LysR, Transcriptional regulator [Transcription].	6.50732e-53
NZ_AP014940.1\|WP_096382367.1\|5900176_5901163_-\|NAD-dependent-epimerase/dehydratase-family-protein	gnl\|CDD\|187552	cd05241, 3b-HSD-like_SDR_e, 3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs. Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	3.45147e-76
NZ_AP014940.1\|WP_096382333.1\|5881782_5883084_-\|isocitrate-lyase	gnl\|CDD\|237893	PRK15063, PRK15063, isocitrate lyase; Provisional.	0

>NZ_AP014940.1|WP_096382341.1|5889482_5890202_+|GntR-family-transcriptional-regulator
MSILPRSLSDQAFEVVRERILSTQIPPLAPIRQELLAEELGISKIPLREALSRLEEQGLLSSHPNRGFFVPPLTSTEAEEVFALRLKIEPEAAAQACLIACETGQEQARAAFLAWEQADHGDPNASVRCNRAFHLALVTPGGRQITAQLVERLQVLAERYVRKHLEPVGREARAANEHLGILQAWLQRDAALVDQLLSTHILSTLHDLRAQLEHIPSTAPMLPDFRRAPRRRREPTEAT
>NZ_AP014940.1|WP_096383827.1|5886167_5888744_-|collagenase
MPSAFEPAATAVSSAASTAAVGSAAASASAPTPGHRAASAPFAASRSAGGAARKQPATERQLFGEHRQPRALAPTQRAPQQPLLPDRADSAYDGASLRRDPLKRPSRLSFARTAKAAAACDPNAFGALSGTALAAAVRAAAPDCVNELFGLSGSQAYATFREAQMVSVADALAASARAYDGSNAGGTLQLVLFLRAGYYVQYYDSAVGSYGAALRNAVRPALDAFAANANFGRIDDVHGEILAEYVTLIDSSAENARYLYVVKRLLDSYDSRFDAYYWMKVAINNAYTVTFRGHQDTAFRTLVQSDNSIVDTLYNFANRNFALLGTDRAYLVSNAGREMARFLQYDGALKTLARARAKALIDRSAITGTTARLWVGVGEMAQYYDAGNCAYYGQCDFVARLQAAALPIRHTCSATLTLRAQQMSASELASACATVAGQEAYFHRELATGGVPVAGDNNASLEMAVFDSSDDYGIYAGAIFGIDTNNGGMYLEGDPSAPGNQARFIAYEAEWLRPTFEIWNLTHEYVHYLDGRFDMWGDFQAAMQQKTVWWVEGFAEYLSYQYRNVANDGAIAEAARGTYALSTVYANDYDSGTNRVYRWGYLAVRFMFEQRRAQVNAILAKFRPGDYSGYATYMAGIGQSNDAAFKAWLPCVADPAGSGCTGTPNQPPTANFSVAASGLSVSFTDTSSDSDGRIVARSWSFGDGSSSTAANPSKTYAAGGSYTVTLTVTDDRGATATATRSISVSEPGLPECSGGDARTLGRNCSRSNAAASAGNYAYFYLYLPAGVSQLRIDTAGGSGNADLYVSAGNWPSRDSYQYRSAKAGNAESVTIANPPAGYVYVAVHAASAFSGVKVSARY
>NZ_AP014940.1|WP_096382337.1|5884878_5885982_+|LysR-family-transcriptional-regulator
MLRLLWGRTAPSERVPGPRPCGGVLYLTIKFFQCISFAELIYGIHVTSTRSLSPRFAYKSDKLKPLRAFCQTARLGSVSRAAEALYLSQPAVTLQLQALEREMGVRLLERSGRRLSLTREGEALYELARPLVEGLDGLEGVFRERIRGLDAGELNVAAGSSTILYLLPKIVEAFRAAHPEVRLTLHNVTGAGGLDLLRSDGVDLAVGSMLDVPGDLSYAPVYRFEPMLIAPRDHPLAKLETLTLQDLSPYGLILPPQRLTTYRMVDLVFQQNRVPYTVALEVGGWEVIKQYVAMGLGISIVTAICLTEADRARLSARSLAEYFPSRSYGVVVRKGKYLSPQARAFTELIQPALFERGDYYATGQSDR
>NZ_AP014940.1|WP_096383825.1|5883245_5884868_-|malate-synthase-A
MTQWQDPRPGQRGPGEGIELSGRAAGQEQVLTPAALEFLADLHRRFEPARQARLAARRERQAFFDAGGLPDFRADTAAIRAGRWRVAPLPTALLDRRVEITGPVDPKMVINALNSGAKVYMADFEDSTAPTWANLIAGQRALAATVAGTLEFAAPDTGKRYALKPFEEQAVLMVRPRGWHLDEKHLRIDGAPVSGGLFDLGLFAFHNAAALAAKDRGPYFYLPKLQSMEEAQLWNDALEHIERELELEPGSIKVTVLIETLPAVFEMDEILHALRTRIAGLNCGRWDYVFSYIKTFRAHRDKILPERGQVTMTQPFLRAYSELLIQTCHKRGAHAMGGMAAQIPINGDEAANEAALAKVRADKLREVTAGHDGTWVAHPALIPLAMRIFDERMPTPHQQHVLREDVLIIAEDLIKPSFGTITRAGFEGNVEVCVRYLAAWLDGNGCVPIHWLMEDAATAEIARTQLWQWLHAPSLFLDDGTPVDFALLERALIGLPSKLAGDAKLPGAGKLDQAIALLDELTHAPTLAEFLTTPAYERLH
>NZ_AP014940.1|WP_096382333.1|5881782_5883084_-|isocitrate-lyase
MSHTLPTAEQLRHEWATDPRWNGITRPYSAEDVVRLRGTVPVEHSIAKLGANKLWKSLHTEDFVNALGALTGNQAMQQVKAGLKAIYLSGWQVAADANIAGEMYPDQSLYPANSVPQVVRRINNTLLRADQIQCAEGTGDTDFLQPIVADAEAGFGGVLNAFELMKGMIEAGASGVHFEDQLASVKKCGHMGGKVLVPTREAVEKLVAARLAADVMGVPTLIVARTDAEAADLLTADIDPNDQPFTTGERTVEGFYKTRNGLDQAISRGLAYAPYADLVWCETGKPDLEFARKFAEAIHAQFPGKLLAYNCSPSFNWKKNLDDATIAKFQKEIASYGYKFQFITLAGFHSLNYGMFNLAHGYARRQMSAFVELQEAEFAAAEKGFTAVKHQREVGTGYFDAVTQTIQGGQSSTVALKGSTEEEQFHESKKAAA
>NZ_AP014940.1|WP_096382331.1|5881428_5881671_+|hypothetical-protein
MKLSIFCAALALGLGLSGAAAARDNSPQAQDTQASAALYWHCIYQSEFGGIYEFTQRGRCLLVVDSDIYGQLTLIDAYQA
>NZ_AP014940.1|WP_096382327.1|5880302_5881082_+|PhzF-family-phenazine-biosynthesis-protein
MKLKLLQIDAFAERVFAGNPAAVCALERWLPDETLQAIAAENHLSETAYYLRRDDDEFDLRWFTPAVEVDLCGHATLATAFAIFRERPDAELLRFRTRSGELRVRRSEHGLSMDFPLTRPRPIPAPDGLLAALGVTRAQVLDADDYIVVVEDEAQVEALAPDLHALRGFERRGVAVTAPGRDFDFVSRWFGPRVGVDEDPVTGSAHTWLAPYWAQRLGKTVLRARQGGARRGTLVCEVLGERVVLSGNAVLYLSGEIEF
>NZ_AP014940.1|WP_096382322.1|5878113_5880192_+|S9-family-peptidase
MPARPHRRPSPAGLALALLAALAVAPAFAAAPAASEVELIPRSALFGNPERSNAQLSPDGRYLSWLAPLRGVMNVWVAPADDPAQARAVTDDAARGIRNYVWSYRSGTLLYLRDSGGDENFHLYAVDVARPGAARDLTAYPKTRANLVRLAHRHPERILVGMNDRDAKWHDLYEVDLASGARKLVLENKDRLSGYLADGDLKIGRATRTREDGNGELLAADGRGGWKVVDTIPFEDSQTTEYEGYSDDGRTLYLTDARGRDTAALYAVDADGKRSLLLEDARADVGARLSDPVSDKVQAASVYYLRQQWKALDPAIGQDLQWLQKKLGDGEVSVASRSLDDRAWVVNYSAAEKPGATYLFRRGENERALTRLFSSRPALDGKPLVPMWPVEIPARDGKTLVSYLTLPKSADPNGDGKPDKPVPLVLFVHGGPWARDYYGYHPYAQWLANRGYASLRVNYRGSTGFGKAFVNAGDGEWAGKMHDDLIDAAGWAVERGVTKKEDVAIMGGSYGGYATLVGLTFTPDAFKCGVDIVGPSNLETLLKTIPPYWASLFEQFARRMGDPRTEAGRKQLAARSPITRVDKIDKPLLIGQGANDPRVNQAESDQIVEAMRKKNIPVTYVLFPDEGHGFARPENSMAFNAVAEGFLAQCLGGRAQPIGNDFKGSSISVPAGADGVKGLESALKTHKQEVKK
>NZ_AP014940.1|WP_096382318.1|5876748_5877798_-|GGDEF-domain-containing-protein
MNRDMAAPSVGRETDNSTATAAPTDVAMAVLTPGEFELFAEIGRPRRVEAGQVLFRRGELGTTMFVIARGAIVLDFGDDLVTKRLGVREFFGELGLLIGDHARSADAIAATDGLLVELRHEEFQRLVDRDPSLVSYFLRRAIMRVVLNEQSLIRRLRRRNQDLEAALDSLYATTHQLNQTEELVRTDDLTGLYNRRGLTLHLQETRAAGMADTIGLVLVDCDRFKQVNDEHGHLAGDRVLQSVANILRSVAGTEDIACRLGGDEFCLLVAAHTRQDVMRFADFIVHTVHGLLLIPQSPPTICPVSVGACLVSAKRDWNDWYAQADAALYQAKRLGGNRVHWQDAELSAV
>NZ_AP014940.1|WP_096382315.1|5874196_5876725_-|putative-peptide-modification-system-cyclase
MNDAHRPDADGPQLRTLLLTDLCDSTTLVERIGDGPAAELFREHDRLVLALQQRWRGRLIDRSDGLLLLFERPIDGLGFALDYARGLREIGAARKFELKARAGLHVGEVLTWRNSDEAVRVGAKPVEVEGLAKPMAGRLMATARPGQILLSAVAEPLAHRAARELGERGQQLLWKSHGRWRFKGVPEPQEIYEVGEPGIAPLRAPPNGPKAWRDVPLWRRPAALVAEVALLAMIGGGAWFATRPQPAIAFNQRDWVVVGDLRNLTGQSVLDDSLEQAFRISLEQSRYVNVLSDLKTRDTLERMQRKNDTVLDRAIASEIALRDGARAVILPTVAEVGGRVRVSAEVIDPHTQTTVYAESADGHGKESTLGSIDTVTAALREKLGEAMKSIERDSEPLPKVATKNLDALRAYALGLKAYGERRHPEAQRYFDQAIALDPEFALAYLAALRVHVGDADNRSAKPYLEKAVALRSHLAPRDALYLDAWSAEYGPQPATRAPAQWKLLAGLYPDYYAGHYNYAWAAFANNRYSESLSFAKAAAAPQNPLRSSAIELVGRAQLAQGDAKAALASFEQGEKIGRYGPNRRRAAALATLRRFDEARAVLAQLSDDTTTSGLTNNLERISVAVDQGRWDEAQKIAARAEREAVHGTPVLANQFALIRLTVESLSGRPLQTAAVLAIGRKAAAQAGDEADPLRNEQAYVALSAAYLGQRHGQAEVARQLLPVLEPLAKRIGDPLVTQLLIIVQAGQLRLDGKPQDAIALLRPLVRGDELFQVHSALRAAYAAAGQDQDAQVEERWLVQNRGRAYIETAGSQALQVVNVADTGLGERAKAETVARTVARTQR
>NZ_AP014940.1|WP_096382345.1|5891067_5891712_-|1-acyl-sn-glycerol-3-phosphate-acyltransferase
MDGAANAKLQHPPGAPDGSVALPLPPNVPRVKPSRLARWTGRTILRLGGWRMVGQFPDVPRAVLIGIPHSSNWDGVWAFAAKAAMGLNVNIIAKESLFKVPVVGFMLRRFGVIPINRSAAHGVIDQAVAMIKGAEKFWLGIAPEGTRKRVEKWKAGFWKIAKNADVPVVLAYFHYPDKVIGIGPAFHLGEDMDADMQRIREYCRPFIGKNRGTV
>NZ_AP014940.1|WP_074870986.1|5891758_5892163_-|aminoacyl-tRNA-hydrolase
MAITIPEAELVERFVRSTGPGGQNVNKVATAVELRFDVAQSPSLPEAVRERLLAKRDRRVTNDGVLVISAQRFRTQERNREDARERLAAFVDSGLRAPKPRVATKPSRAAKERRLGAKRDRGQTKRARSQREWD
>NZ_AP014940.1|WP_096382350.1|5892373_5893042_+|hypothetical-protein
MQRPLRPSATLWPAVLALAVLSAAAPAASAQAIPQRYDPANVNSQLNDPAFQRRMARAARSTAETLVGRPANATDNRILGQFDQVQSQALQQMQNAFSRMPQDQQVDARALQTLSQTPEGRLVLEQLAAEQRRAPSAYGAQNRGPQSEYDQLFQQAYPDGMQGPAPSVSSRNGYAPRSSVGGALGGALLQDITNAAIQRSIGPRVQVQGNTYYYEDRPRRRP
>NZ_AP014940.1|WP_172437345.1|5893164_5893947_-|pseudouridylate-synthase
MEPDYPPRRLPARTHPMSNSDATHTSETAAAGLPVLYADQALAIIDKPAGLMVHDSALARGETDFAADRLREQFGRPIFLVHRLDRATSGCLLLAFDRDTASALGKVLMSREVEKDYLAVCRGWPAQDAFEVDHDLDGGPGKPLKKPAQTRFAVLAQTELALPSAGFATSRYALLRAQPLTGRFRQIRRHLKHLSHHLIGDTSHGDGRHNRSFRMLGIHRMLLHAQRLAFVHPHSGQRIEATAPADAEFAKALALFEPAD
>NZ_AP014940.1|WP_096382354.1|5894049_5896827_+|insulinase-family-protein
MSAPQRLAVPLALALSLALAGARAEPARPPQGVVAGPCAQGICEYRLGNGLRVLLFPDASQPTVTVNLVYRVGSAQENYGETGMAHLLEHMMFKGTPEHRDIPAEMKKRGINFNANTAQDYTNYYGSFPADEGTLDWLLTLEADRMLHSDVAKADLDSEMTVVRNEMESGENNAFNVLDERTRSTAYLWHHYGQSTIGARSDVEHVPIERLRAYYRTWYRPDNATLVVAGRIDPQRTLDTVARRFGGLAKPAQPIPVFYTREPAQDGEREVVIRRVGDLRLLMAAYHTPAITHADAAPLAVLRELLGRTPGGRLHKALVETGLAESVGAGADTFRDPGLFNAQIALAKGGDAAKAQQVLLAQLEGIAQRPIDAAEVEAARQRILNAYEQADANVSGIAMSLTDSIAVGDWRLYFQFRDAVEKVDADAVNRVARAYLRASNRTLGRFEPEEKPDRVEVPQAPDAAEALKSYVAKRGVDAGEQFDPSPANIQARTRTLTIDTGVGAGLKLALLPKKTRGNTVTFSANFRFGDADSLRGRDVAASLAGAQLMRGGGGLSREQIDARFQALKTSARVGGDLQSASIGLQTRRDQLADAVALAAKLLREPAFPEAEFEQYRRQAITGLEAQRQEPDALAGQALARHFDPWPAGHPLHARSLDESLAAIRALKLEELRAFHREFYGSAEGEIAVVGDFDPDALERQLRTLFAAWKPGHAFAPIATRYTAVAPEQRRLDAPDKANGVLLARANLSLKETDPDYPALVAANYILGGGMKSRLIDRLRQKDGLSYSAGSRLDADDSRDGRDDDGNWSMQAIAAPQNLDKVERATREELTRLVESGVAADELRDAVSGLLTRREQARASDGNVAGLLSRNLFFGRTMQSTADLDAKLKALTVESVNAAIKRHLKPQDFSVYLAGDFDAAKKASGK
>NZ_AP014940.1|WP_096382357.1|5897477_5899163_-|ubiquinone-biosynthesis-regulatory-protein-kinase-UbiB
MKSAARAWRIGRVLLRYRLDALLDDTPVERWLKLARPFVPRASAEVEAMSRGARLRLALQELGPIFVKFGQILSTRRDLVPPDIAAELTLLQDRVKPFDGETARRIVEGALERRIDEAFDRFDIEPLASASIAQVHAARLPAQGERPAREVVVKVLRPDIEGKIAGDIALLKAMAVLVDRTHPSADKIRPRAIVAEIESTLAAELDLQREGANASVLRRFWADSDDMYVPEVIWTHTSERALTLERVYGIPSDDIAALDAAGIDRRALAAKGVRVFYTQVFRDNFFHADAHAGNIWVDSDPARRNNPRFIALDFGIMGQLSDEDQYYLAENFMAIFNRDYRRIAELHVQAGWMPAHIRIDELEAATRAVCEPYFTRPLSEISLAEVLLKLFRTAQRYELTLQPQLILLQKTLLNIEGVGRLLDPKLDIWAVARPVLQRILLDRYSPQRLAGEFRKRLPELVTRAPEMPRLLHAWLSQQVAGQHELKMRSGDIVELNRTIKDAVRRTVSAILGTGLLIVSAVLYGLESGGPRFWSVPASSWIAGLGGVWALLAAWPRRRWFK
>NZ_AP014940.1|WP_096382362.1|5899302_5899962_-|SCP2-sterol-binding-domain-containing-protein
MNDSASPLDALKPLAGRALEAALNRALALDPDTRAGLSALDGRSIALHLAEPPLAARILVAGERLEVGPVRSSDEPDLSVRSTLGAIFAQLPNLLGAARNEQAAPVGKLRIEGDADLARRLQRLAERFDPDWQQPFTAVFGDLVGVQIANAVAGALRHARDAAGAFASNAAEYLTEESRDLVPRAELDAFHDDVDALRDDVERAAARVARLHARAGGRA
>NZ_AP014940.1|WP_096382367.1|5900176_5901163_-|NAD-dependent-epimerase/dehydratase-family-protein
MKILVTGGGGFLGQALCRGLVARGHEVVSFNRGHYPALDPLGVTQIQGDLADRDAVVAAAQGCEAIFHNAAKAGAWGSYESYHQANVVGTENVLAACRAHGIGKLIYTSTPSVTHRATNPVEGGSAETVPYGDGFKAAYATTKTIAEKAVLAANSPQLATVALRPRLIWGVGDNQLLPRLVQRANSGRLRFVGTGENRIDTTYIDNAAQAHFDAFEHLAPGAACAGKAYFISNGDPRTVRETLNGLLGAVGAPTVNKTLPFRAAYVIGAICEGLWTLLPLKGEPPMTRFLAEQLSTTHWYDMGPAKRDFGYVPQVSFDEGLARVKAAQ
>NZ_AP014940.1|WP_096382372.1|5901369_5903031_-|AMP-binding-protein
MDASDAVCNIAASLPRLAAQSPQRVAMRCPGTRGPDGLARYDVELTYAELDRRSDAIAAGLAQRGIVRGTRTAVMVRPSPEFFLLMFALFKAGAVPVLIDPGIDKRALRQCLDEAAPEAFIGIPLAHIARVVLGWAKSARIRITTGARAFLADDTLARVERAGEGAGSQLADTKAEEVAAIVFTSGSTGVPKGVVFRHRHFVAQIEMMGEAFGIAPGGVDLPTFPPFALFDPALGLTSVIPDMDPTRPAQADPAKLHDALRRFGCDQLFGSPALMKVLADYGQPLPTLRRVTSAGAPVPPDTVAKLRELMHEDAQFWTPYGATECLPVAVIEGRELQSTRAATEAGAGTCVGRAVARNQVRIVRISDEAIEQWSDELLVPAGTVGEITVAGPTATDAYFNRDGMTRLAKIRERTAQGERIVHRMGDVGYLDEQGRLWFCGRKGHRVETASGPLYTEQVEPVFNTHAKVRRTALVGTGAQGQQRPLLWVELHQPRVGNRERERILAELREIGANHAHTAGIERFRFHPGFPVDIRHNAKIGREKLALQARAIGD
>NZ_AP014940.1|WP_096382376.1|5903040_5903943_-|alpha/beta-fold-hydrolase
MTSSSRFPDYPFQPQHFEVRPGIGLSYLDQGPRDGEVVVMLHGNPSWSYYWRKLVLGLHDRYRCIVPDHVGMGLSDKPGDERYEYTLQSRVDDVEKLLQHLGISGPMTLAVHDWGGGIGFGWGLKHSDQIKRLVITNTGAFPLPAAKPLPKRLRLGRDSAIGTGLIRGLNAFAGGAARLGVSKAMPADVRRAYVAPYDSWANRIATSRFVQDIPLGEGDKAWPLVQAMGRKLPEYADRPAFIGWGLGDFVFDHHFLKGFTDALPQAEVHAFQDAGHYVLEDKAAELVPAIRAFLDRNPLG

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Crispr_ID: NZ_AP014940_20

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_20

5897216-5897322

Orphan

Consensus_repeat	Method
CGGCGGAGCTACGTCGCTGCGGTTGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP014940_20

>merge|NZ_AP014940|20|5897216-5897322|CRISPRCasFinder
CGGCGGAGCTACGTCGCTGCGGTTGGATTCCGGCTTTCGCCGGAATGACGGCGTGGGGGGTTGCGGGGCTTCGGGGTGTGGCGGCGGAGCTGCGTCGCTGCGGTTGG

>NZ_AP014940|20|19|5897216-5897322|CRISPRCasFinder
CGGCGGAGCTACGTCGCTGCGGTTGG	ATTCCGGCTTTCGCCGGAATGACGGCGTGGGGGGTTGCGGGGCTTCGGGGTGTGG
CGGCGGAGCTGCGTCGCTGCGGTTGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_096382384.1\|5905493_5908022_+\|sodium:solute-symporter	unknown	unknown	gnl\|CDD\|271386
NZ_AP014940.1\|WP_096382345.1\|5891067_5891712_-\|1-acyl-sn-glycerol-3-phosphate-acyltransferase	unknown	unknown	gnl\|CDD\|153250
NZ_AP014940.1\|WP_096382362.1\|5899302_5899962_-\|SCP2-sterol-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|225706
NZ_AP014940.1\|WP_096383825.1\|5883245_5884868_-\|malate-synthase-A	unknown	unknown	gnl\|CDD\|236432
NZ_AP014940.1\|WP_096382390.1\|5908155_5909049_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|176118
NZ_AP014940.1\|WP_096382357.1\|5897477_5899163_-\|ubiquinone-biosynthesis-regulatory-protein-kinase-UbiB	unknown	unknown	gnl\|CDD\|235310
NZ_AP014940.1\|WP_096382380.1\|5904562_5905417_+\|CoA-ester-lyase	unknown	unknown	gnl\|CDD\|225184
NZ_AP014940.1\|WP_096382367.1\|5900176_5901163_-\|NAD-dependent-epimerase/dehydratase-family-protein	unknown	unknown	gnl\|CDD\|187552
NZ_AP014940.1\|WP_172437345.1\|5893164_5893947_-\|pseudouridylate-synthase	unknown	unknown	gnl\|CDD\|211333
NZ_AP014940.1\|WP_172437346.1\|5911938_5913222_+\|beta-lactamase-family-protein	unknown	unknown	gnl\|CDD\|365903
NZ_AP014940.1\|WP_074870986.1\|5891758_5892163_-\|aminoacyl-tRNA-hydrolase	unknown	unknown	gnl\|CDD\|181730
NZ_AP014940.1\|WP_096382376.1\|5903040_5903943_-\|alpha/beta-fold-hydrolase	unknown	unknown	gnl\|CDD\|179147
NZ_AP014940.1\|WP_096382341.1\|5889482_5890202_+\|GntR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224715
NZ_AP014940.1\|WP_096383827.1\|5886167_5888744_-\|collagenase	unknown	unknown	gnl\|CDD\|366791
NZ_AP014940.1\|WP_096382354.1\|5894049_5896827_+\|insulinase-family-protein	unknown	unknown	gnl\|CDD\|223685
NZ_AP014940.1\|WP_096382395.1\|5909396_5911691_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657
NZ_AP014940.1\|WP_096382350.1\|5892373_5893042_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096382337.1\|5884878_5885982_+\|LysR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|223656
NZ_AP014940.1\|WP_096382372.1\|5901369_5903031_-\|AMP-binding-protein	unknown	unknown	gnl\|CDD\|236443
NZ_AP014940.1\|WP_096382333.1\|5881782_5883084_-\|isocitrate-lyase	unknown	unknown	gnl\|CDD\|237893

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_096382384.1\|5905493_5908022_+\|sodium:solute-symporter	gnl\|CDD\|271386	cd11495, SLC5sbd_NIS-like_u3, uncharacterized subgroup of the Na(+)/iodide (NIS) cotransporter subfamily; putative solute-binding domain. Proteins belonging to the same subfamily as this uncharacterized subgroup include i) NIS, which transports I-, and other anions including ClO4-, SCN-, and Br-, ii) SMVT, which transports biotin, pantothenic acid and lipoate, and iii) the Na(+)/monocarboxylate cotransporters SMCT1 and 2. SMCT1 is a high-affinity transporter while SMCT2 is a low-affinity transporter. This subgroup belongs to the solute carrier 5 (SLC5) transporter family.	4.09537e-174
NZ_AP014940.1\|WP_096382345.1\|5891067_5891712_-\|1-acyl-sn-glycerol-3-phosphate-acyltransferase	gnl\|CDD\|153250	cd07988, LPLAT_ABO13168-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ABO13168. Lysophospholipid acyltransferase (LPLAT) superfamily member: acyltransferases of de novo and remodeling pathways of glycerophospholipid biosynthesis which catalyze the incorporation of an acyl group from either acylCoAs or acyl-acyl carrier proteins (acylACPs) into acceptors such as glycerol 3-phosphate, dihydroxyacetone phosphate or lyso-phosphatidic acid. Included in this subgroup are uncharacterized phospholipid/glycerol acyltransferases such as the Acinetobacter baumannii ATCC 17978 locus ABO13168 putative acyltransferase, and similar proteins.	9.51815e-70
NZ_AP014940.1\|WP_096382362.1\|5899302_5899962_-\|SCP2-sterol-binding-domain-containing-protein	gnl\|CDD\|225706	COG3165, COG3165, Uncharacterized protein conserved in bacteria [Function unknown].	5.34241e-41
NZ_AP014940.1\|WP_096383825.1\|5883245_5884868_-\|malate-synthase-A	gnl\|CDD\|236432	PRK09255, PRK09255, malate synthase; Validated.	0
NZ_AP014940.1\|WP_096382390.1\|5908155_5909049_+\|LysR-family-transcriptional-regulator	gnl\|CDD\|176118	cd08427, PBP2_LTTR_like_2, The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator, contains the type 2 periplasmic binding fold. LysR-transcriptional regulators comprise the largest family of prokaryotic transcription factor. Homologs of some of LTTRs with similar domain organizations are also found in the archaea and eukaryotic organisms. The LTTRs are composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The genes controlled by the LTTRs have diverse functional roles including amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to a name a few. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.	1.53288e-78
NZ_AP014940.1\|WP_096382357.1\|5897477_5899163_-\|ubiquinone-biosynthesis-regulatory-protein-kinase-UbiB	gnl\|CDD\|235310	PRK04750, ubiB, putative ubiquinone biosynthesis protein UbiB; Reviewed.	0
NZ_AP014940.1\|WP_096382380.1\|5904562_5905417_+\|CoA-ester-lyase	gnl\|CDD\|225184	COG2301, CitE, Citrate lyase beta subunit [Carbohydrate transport and metabolism].	4.38968e-62
NZ_AP014940.1\|WP_096382367.1\|5900176_5901163_-\|NAD-dependent-epimerase/dehydratase-family-protein	gnl\|CDD\|187552	cd05241, 3b-HSD-like_SDR_e, 3beta-hydroxysteroid dehydrogenases (3b-HSD)-like, extended (e) SDRs. Extended SDR family domains belonging to this subgroup have the characteristic active site tetrad and a fairly well-conserved NAD(P)-binding motif. 3b-HSD catalyzes the NAD-dependent conversion of various steroids, such as pregnenolone to progesterone, or androstenediol to testosterone. This subgroup includes an unusual bifunctional 3b-HSD/C-4 decarboxylase from Arabidopsis thaliana, and Saccharomyces cerevisiae ERG26, a 3b-HSD/C-4 decarboxylase, involved in the synthesis of ergosterol, the major sterol of yeast. It also includes human 3 beta-HSD/HSD3B1 and C(27) 3beta-HSD/ [3beta-hydroxy-delta(5)-C(27)-steroid oxidoreductase; HSD3B7]. C(27) 3beta-HSD/HSD3B7 is a membrane-bound enzyme of the endoplasmic reticulum, that catalyzes the isomerization and oxidation of 7alpha-hydroxylated sterol intermediates, an early step in bile acid biosynthesis. Mutations in the human NSDHL (NAD(P)H steroid dehydrogenase-like protein) cause CHILD syndrome (congenital hemidysplasia with ichthyosiform nevus and limb defects), an X-linked dominant, male-lethal trait. Mutations in the human gene encoding C(27) 3beta-HSD underlie a rare autosomal recessive form of neonatal cholestasis. Extended SDRs are distinct from classical SDRs. In addition to the Rossmann fold (alpha/beta folding pattern with a central beta-sheet) core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids. Extended SDRs are a diverse collection of proteins, and include isomerases, epimerases, oxidoreductases, and lyases; they typically have a TGXXGXXG cofactor binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid sythase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.	3.45147e-76
NZ_AP014940.1\|WP_172437345.1\|5893164_5893947_-\|pseudouridylate-synthase	gnl\|CDD\|211333	cd02563, PseudoU_synth_TruC, tRNA pseudouridine isomerase C. Pseudouridine synthases catalyze the isomerization of specific uridines in an tRNA molecule to pseudouridines (5-ribosyluracil, psi). No cofactors are required. TruC makes psi65 in tRNAs. This psi residue is not universally conserved.	1.87497e-76
NZ_AP014940.1\|WP_172437346.1\|5911938_5913222_+\|beta-lactamase-family-protein	gnl\|CDD\|365903	pfam00144, Beta-lactamase, Beta-lactamase. This family appears to be distantly related to pfam00905 and PF00768 D-alanyl-D-alanine carboxypeptidase.	1.84728e-55
NZ_AP014940.1\|WP_074870986.1\|5891758_5892163_-\|aminoacyl-tRNA-hydrolase	gnl\|CDD\|181730	PRK09256, PRK09256, aminoacyl-tRNA hydrolase.	1.5762e-60
NZ_AP014940.1\|WP_096382376.1\|5903040_5903943_-\|alpha/beta-fold-hydrolase	gnl\|CDD\|179147	PRK00870, PRK00870, haloalkane dehalogenase; Provisional.	1.11746e-39
NZ_AP014940.1\|WP_096382341.1\|5889482_5890202_+\|GntR-family-transcriptional-regulator	gnl\|CDD\|224715	COG1802, GntR, Transcriptional regulators [Transcription].	6.92567e-39
NZ_AP014940.1\|WP_096383827.1\|5886167_5888744_-\|collagenase	gnl\|CDD\|366791	pfam01752, Peptidase_M9, Collagenase. This family of enzymes break down collagens.	8.42016e-145
NZ_AP014940.1\|WP_096382354.1\|5894049_5896827_+\|insulinase-family-protein	gnl\|CDD\|223685	COG0612, PqqL, Predicted Zn-dependent peptidases [General function prediction only].	3.84265e-74
NZ_AP014940.1\|WP_096382395.1\|5909396_5911691_+\|TonB-dependent-receptor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	8.60803e-48
NZ_AP014940.1\|WP_096382337.1\|5884878_5885982_+\|LysR-family-transcriptional-regulator	gnl\|CDD\|223656	COG0583, LysR, Transcriptional regulator [Transcription].	6.50732e-53
NZ_AP014940.1\|WP_096382372.1\|5901369_5903031_-\|AMP-binding-protein	gnl\|CDD\|236443	PRK09274, PRK09274, peptide synthase; Provisional.	0
NZ_AP014940.1\|WP_096382333.1\|5881782_5883084_-\|isocitrate-lyase	gnl\|CDD\|237893	PRK15063, PRK15063, isocitrate lyase; Provisional.	0

>NZ_AP014940.1|WP_096382354.1|5894049_5896827_+|insulinase-family-protein
MSAPQRLAVPLALALSLALAGARAEPARPPQGVVAGPCAQGICEYRLGNGLRVLLFPDASQPTVTVNLVYRVGSAQENYGETGMAHLLEHMMFKGTPEHRDIPAEMKKRGINFNANTAQDYTNYYGSFPADEGTLDWLLTLEADRMLHSDVAKADLDSEMTVVRNEMESGENNAFNVLDERTRSTAYLWHHYGQSTIGARSDVEHVPIERLRAYYRTWYRPDNATLVVAGRIDPQRTLDTVARRFGGLAKPAQPIPVFYTREPAQDGEREVVIRRVGDLRLLMAAYHTPAITHADAAPLAVLRELLGRTPGGRLHKALVETGLAESVGAGADTFRDPGLFNAQIALAKGGDAAKAQQVLLAQLEGIAQRPIDAAEVEAARQRILNAYEQADANVSGIAMSLTDSIAVGDWRLYFQFRDAVEKVDADAVNRVARAYLRASNRTLGRFEPEEKPDRVEVPQAPDAAEALKSYVAKRGVDAGEQFDPSPANIQARTRTLTIDTGVGAGLKLALLPKKTRGNTVTFSANFRFGDADSLRGRDVAASLAGAQLMRGGGGLSREQIDARFQALKTSARVGGDLQSASIGLQTRRDQLADAVALAAKLLREPAFPEAEFEQYRRQAITGLEAQRQEPDALAGQALARHFDPWPAGHPLHARSLDESLAAIRALKLEELRAFHREFYGSAEGEIAVVGDFDPDALERQLRTLFAAWKPGHAFAPIATRYTAVAPEQRRLDAPDKANGVLLARANLSLKETDPDYPALVAANYILGGGMKSRLIDRLRQKDGLSYSAGSRLDADDSRDGRDDDGNWSMQAIAAPQNLDKVERATREELTRLVESGVAADELRDAVSGLLTRREQARASDGNVAGLLSRNLFFGRTMQSTADLDAKLKALTVESVNAAIKRHLKPQDFSVYLAGDFDAAKKASGK
>NZ_AP014940.1|WP_172437345.1|5893164_5893947_-|pseudouridylate-synthase
MEPDYPPRRLPARTHPMSNSDATHTSETAAAGLPVLYADQALAIIDKPAGLMVHDSALARGETDFAADRLREQFGRPIFLVHRLDRATSGCLLLAFDRDTASALGKVLMSREVEKDYLAVCRGWPAQDAFEVDHDLDGGPGKPLKKPAQTRFAVLAQTELALPSAGFATSRYALLRAQPLTGRFRQIRRHLKHLSHHLIGDTSHGDGRHNRSFRMLGIHRMLLHAQRLAFVHPHSGQRIEATAPADAEFAKALALFEPAD
>NZ_AP014940.1|WP_096382350.1|5892373_5893042_+|hypothetical-protein
MQRPLRPSATLWPAVLALAVLSAAAPAASAQAIPQRYDPANVNSQLNDPAFQRRMARAARSTAETLVGRPANATDNRILGQFDQVQSQALQQMQNAFSRMPQDQQVDARALQTLSQTPEGRLVLEQLAAEQRRAPSAYGAQNRGPQSEYDQLFQQAYPDGMQGPAPSVSSRNGYAPRSSVGGALGGALLQDITNAAIQRSIGPRVQVQGNTYYYEDRPRRRP
>NZ_AP014940.1|WP_074870986.1|5891758_5892163_-|aminoacyl-tRNA-hydrolase
MAITIPEAELVERFVRSTGPGGQNVNKVATAVELRFDVAQSPSLPEAVRERLLAKRDRRVTNDGVLVISAQRFRTQERNREDARERLAAFVDSGLRAPKPRVATKPSRAAKERRLGAKRDRGQTKRARSQREWD
>NZ_AP014940.1|WP_096382345.1|5891067_5891712_-|1-acyl-sn-glycerol-3-phosphate-acyltransferase
MDGAANAKLQHPPGAPDGSVALPLPPNVPRVKPSRLARWTGRTILRLGGWRMVGQFPDVPRAVLIGIPHSSNWDGVWAFAAKAAMGLNVNIIAKESLFKVPVVGFMLRRFGVIPINRSAAHGVIDQAVAMIKGAEKFWLGIAPEGTRKRVEKWKAGFWKIAKNADVPVVLAYFHYPDKVIGIGPAFHLGEDMDADMQRIREYCRPFIGKNRGTV
>NZ_AP014940.1|WP_096382341.1|5889482_5890202_+|GntR-family-transcriptional-regulator
MSILPRSLSDQAFEVVRERILSTQIPPLAPIRQELLAEELGISKIPLREALSRLEEQGLLSSHPNRGFFVPPLTSTEAEEVFALRLKIEPEAAAQACLIACETGQEQARAAFLAWEQADHGDPNASVRCNRAFHLALVTPGGRQITAQLVERLQVLAERYVRKHLEPVGREARAANEHLGILQAWLQRDAALVDQLLSTHILSTLHDLRAQLEHIPSTAPMLPDFRRAPRRRREPTEAT
>NZ_AP014940.1|WP_096383827.1|5886167_5888744_-|collagenase
MPSAFEPAATAVSSAASTAAVGSAAASASAPTPGHRAASAPFAASRSAGGAARKQPATERQLFGEHRQPRALAPTQRAPQQPLLPDRADSAYDGASLRRDPLKRPSRLSFARTAKAAAACDPNAFGALSGTALAAAVRAAAPDCVNELFGLSGSQAYATFREAQMVSVADALAASARAYDGSNAGGTLQLVLFLRAGYYVQYYDSAVGSYGAALRNAVRPALDAFAANANFGRIDDVHGEILAEYVTLIDSSAENARYLYVVKRLLDSYDSRFDAYYWMKVAINNAYTVTFRGHQDTAFRTLVQSDNSIVDTLYNFANRNFALLGTDRAYLVSNAGREMARFLQYDGALKTLARARAKALIDRSAITGTTARLWVGVGEMAQYYDAGNCAYYGQCDFVARLQAAALPIRHTCSATLTLRAQQMSASELASACATVAGQEAYFHRELATGGVPVAGDNNASLEMAVFDSSDDYGIYAGAIFGIDTNNGGMYLEGDPSAPGNQARFIAYEAEWLRPTFEIWNLTHEYVHYLDGRFDMWGDFQAAMQQKTVWWVEGFAEYLSYQYRNVANDGAIAEAARGTYALSTVYANDYDSGTNRVYRWGYLAVRFMFEQRRAQVNAILAKFRPGDYSGYATYMAGIGQSNDAAFKAWLPCVADPAGSGCTGTPNQPPTANFSVAASGLSVSFTDTSSDSDGRIVARSWSFGDGSSSTAANPSKTYAAGGSYTVTLTVTDDRGATATATRSISVSEPGLPECSGGDARTLGRNCSRSNAAASAGNYAYFYLYLPAGVSQLRIDTAGGSGNADLYVSAGNWPSRDSYQYRSAKAGNAESVTIANPPAGYVYVAVHAASAFSGVKVSARY
>NZ_AP014940.1|WP_096382337.1|5884878_5885982_+|LysR-family-transcriptional-regulator
MLRLLWGRTAPSERVPGPRPCGGVLYLTIKFFQCISFAELIYGIHVTSTRSLSPRFAYKSDKLKPLRAFCQTARLGSVSRAAEALYLSQPAVTLQLQALEREMGVRLLERSGRRLSLTREGEALYELARPLVEGLDGLEGVFRERIRGLDAGELNVAAGSSTILYLLPKIVEAFRAAHPEVRLTLHNVTGAGGLDLLRSDGVDLAVGSMLDVPGDLSYAPVYRFEPMLIAPRDHPLAKLETLTLQDLSPYGLILPPQRLTTYRMVDLVFQQNRVPYTVALEVGGWEVIKQYVAMGLGISIVTAICLTEADRARLSARSLAEYFPSRSYGVVVRKGKYLSPQARAFTELIQPALFERGDYYATGQSDR
>NZ_AP014940.1|WP_096383825.1|5883245_5884868_-|malate-synthase-A
MTQWQDPRPGQRGPGEGIELSGRAAGQEQVLTPAALEFLADLHRRFEPARQARLAARRERQAFFDAGGLPDFRADTAAIRAGRWRVAPLPTALLDRRVEITGPVDPKMVINALNSGAKVYMADFEDSTAPTWANLIAGQRALAATVAGTLEFAAPDTGKRYALKPFEEQAVLMVRPRGWHLDEKHLRIDGAPVSGGLFDLGLFAFHNAAALAAKDRGPYFYLPKLQSMEEAQLWNDALEHIERELELEPGSIKVTVLIETLPAVFEMDEILHALRTRIAGLNCGRWDYVFSYIKTFRAHRDKILPERGQVTMTQPFLRAYSELLIQTCHKRGAHAMGGMAAQIPINGDEAANEAALAKVRADKLREVTAGHDGTWVAHPALIPLAMRIFDERMPTPHQQHVLREDVLIIAEDLIKPSFGTITRAGFEGNVEVCVRYLAAWLDGNGCVPIHWLMEDAATAEIARTQLWQWLHAPSLFLDDGTPVDFALLERALIGLPSKLAGDAKLPGAGKLDQAIALLDELTHAPTLAEFLTTPAYERLH
>NZ_AP014940.1|WP_096382333.1|5881782_5883084_-|isocitrate-lyase
MSHTLPTAEQLRHEWATDPRWNGITRPYSAEDVVRLRGTVPVEHSIAKLGANKLWKSLHTEDFVNALGALTGNQAMQQVKAGLKAIYLSGWQVAADANIAGEMYPDQSLYPANSVPQVVRRINNTLLRADQIQCAEGTGDTDFLQPIVADAEAGFGGVLNAFELMKGMIEAGASGVHFEDQLASVKKCGHMGGKVLVPTREAVEKLVAARLAADVMGVPTLIVARTDAEAADLLTADIDPNDQPFTTGERTVEGFYKTRNGLDQAISRGLAYAPYADLVWCETGKPDLEFARKFAEAIHAQFPGKLLAYNCSPSFNWKKNLDDATIAKFQKEIASYGYKFQFITLAGFHSLNYGMFNLAHGYARRQMSAFVELQEAEFAAAEKGFTAVKHQREVGTGYFDAVTQTIQGGQSSTVALKGSTEEEQFHESKKAAA
>NZ_AP014940.1|WP_096382357.1|5897477_5899163_-|ubiquinone-biosynthesis-regulatory-protein-kinase-UbiB
MKSAARAWRIGRVLLRYRLDALLDDTPVERWLKLARPFVPRASAEVEAMSRGARLRLALQELGPIFVKFGQILSTRRDLVPPDIAAELTLLQDRVKPFDGETARRIVEGALERRIDEAFDRFDIEPLASASIAQVHAARLPAQGERPAREVVVKVLRPDIEGKIAGDIALLKAMAVLVDRTHPSADKIRPRAIVAEIESTLAAELDLQREGANASVLRRFWADSDDMYVPEVIWTHTSERALTLERVYGIPSDDIAALDAAGIDRRALAAKGVRVFYTQVFRDNFFHADAHAGNIWVDSDPARRNNPRFIALDFGIMGQLSDEDQYYLAENFMAIFNRDYRRIAELHVQAGWMPAHIRIDELEAATRAVCEPYFTRPLSEISLAEVLLKLFRTAQRYELTLQPQLILLQKTLLNIEGVGRLLDPKLDIWAVARPVLQRILLDRYSPQRLAGEFRKRLPELVTRAPEMPRLLHAWLSQQVAGQHELKMRSGDIVELNRTIKDAVRRTVSAILGTGLLIVSAVLYGLESGGPRFWSVPASSWIAGLGGVWALLAAWPRRRWFK
>NZ_AP014940.1|WP_096382362.1|5899302_5899962_-|SCP2-sterol-binding-domain-containing-protein
MNDSASPLDALKPLAGRALEAALNRALALDPDTRAGLSALDGRSIALHLAEPPLAARILVAGERLEVGPVRSSDEPDLSVRSTLGAIFAQLPNLLGAARNEQAAPVGKLRIEGDADLARRLQRLAERFDPDWQQPFTAVFGDLVGVQIANAVAGALRHARDAAGAFASNAAEYLTEESRDLVPRAELDAFHDDVDALRDDVERAAARVARLHARAGGRA
>NZ_AP014940.1|WP_096382367.1|5900176_5901163_-|NAD-dependent-epimerase/dehydratase-family-protein
MKILVTGGGGFLGQALCRGLVARGHEVVSFNRGHYPALDPLGVTQIQGDLADRDAVVAAAQGCEAIFHNAAKAGAWGSYESYHQANVVGTENVLAACRAHGIGKLIYTSTPSVTHRATNPVEGGSAETVPYGDGFKAAYATTKTIAEKAVLAANSPQLATVALRPRLIWGVGDNQLLPRLVQRANSGRLRFVGTGENRIDTTYIDNAAQAHFDAFEHLAPGAACAGKAYFISNGDPRTVRETLNGLLGAVGAPTVNKTLPFRAAYVIGAICEGLWTLLPLKGEPPMTRFLAEQLSTTHWYDMGPAKRDFGYVPQVSFDEGLARVKAAQ
>NZ_AP014940.1|WP_096382372.1|5901369_5903031_-|AMP-binding-protein
MDASDAVCNIAASLPRLAAQSPQRVAMRCPGTRGPDGLARYDVELTYAELDRRSDAIAAGLAQRGIVRGTRTAVMVRPSPEFFLLMFALFKAGAVPVLIDPGIDKRALRQCLDEAAPEAFIGIPLAHIARVVLGWAKSARIRITTGARAFLADDTLARVERAGEGAGSQLADTKAEEVAAIVFTSGSTGVPKGVVFRHRHFVAQIEMMGEAFGIAPGGVDLPTFPPFALFDPALGLTSVIPDMDPTRPAQADPAKLHDALRRFGCDQLFGSPALMKVLADYGQPLPTLRRVTSAGAPVPPDTVAKLRELMHEDAQFWTPYGATECLPVAVIEGRELQSTRAATEAGAGTCVGRAVARNQVRIVRISDEAIEQWSDELLVPAGTVGEITVAGPTATDAYFNRDGMTRLAKIRERTAQGERIVHRMGDVGYLDEQGRLWFCGRKGHRVETASGPLYTEQVEPVFNTHAKVRRTALVGTGAQGQQRPLLWVELHQPRVGNRERERILAELREIGANHAHTAGIERFRFHPGFPVDIRHNAKIGREKLALQARAIGD
>NZ_AP014940.1|WP_096382376.1|5903040_5903943_-|alpha/beta-fold-hydrolase
MTSSSRFPDYPFQPQHFEVRPGIGLSYLDQGPRDGEVVVMLHGNPSWSYYWRKLVLGLHDRYRCIVPDHVGMGLSDKPGDERYEYTLQSRVDDVEKLLQHLGISGPMTLAVHDWGGGIGFGWGLKHSDQIKRLVITNTGAFPLPAAKPLPKRLRLGRDSAIGTGLIRGLNAFAGGAARLGVSKAMPADVRRAYVAPYDSWANRIATSRFVQDIPLGEGDKAWPLVQAMGRKLPEYADRPAFIGWGLGDFVFDHHFLKGFTDALPQAEVHAFQDAGHYVLEDKAAELVPAIRAFLDRNPLG
>NZ_AP014940.1|WP_096382380.1|5904562_5905417_+|CoA-ester-lyase
MRSKLFVPGARPELFDKALAGAADALSFDLEDAVAPERKAAARVAVAAFLASTAAAASSKLMIVRVNAPGSEHFAADLAAVAREGTDLINLPKIESAAALHEAVAALERAETRNGVARPIGLLVNIETPRALLAAAAIAGAHPRVAGLQLGLADLFEAQGIARDDRANVHAALFAVRMAAAQAGVFALDGAYADLHDEAGYFDEALVAKRLGFLGKTCLHPRQVGLANRAFAASADELARARRIVTAAETAADGGRGVFVVDGRMIDRPFLKRAQALLATAERT
>NZ_AP014940.1|WP_096382384.1|5905493_5908022_+|sodium:solute-symporter
MSQQSQSLKPGRRAPAARSSLAGARRALWQPISAARALSLWMLLLLAALAAPLQAEPLTPLRSGELPALQTAAPPLGLAQLDGATVAVGSESAWRLDPGAAQWRALQWTPPPRLRAILGDGARAFALSADGALARLQADPARLQALPLPAAPEPLRDAAAAWSADTLYLAGLGADGAPRLYQRPLGDERAAWAAAPAWAAPGAPRTALFQTKSLFLVLADPAGGADRLLRWTPGQGGWSEAGRVPGQIAGAGRATGQAHLLIPVSASAHAPAQLKTFQTITGAWAELPGAQVPADALATAAWPDGLMWARADGAQTRFATAQIQSNKLRLHWLDWAVIVVYLAGMIGIGLYFYLREKRGSTDSFFVGGRSIPFWAAGISLYAANTSSISFIAIPAKAFETNWQYMANNIIAVGGLVFVAIWIVPLLRRLDLMSVFSYLETRFHPSIRMLASALCVFVQIGSRMSVILFLPALAIATITGISVFWSVLLMGGFTIVYTAMGGMKAVIWTDFVQVIVKMGGAIFAIGFMIWGLRGGLHQFWSTAMAEGKMHTFDFSFDLTKATVWGFLFLVLFEVVLTFPKDQVLMQRTLSTSSAREAGRSIWAFAAIMIPGGIVFYTIGTAMFVYYREHPERMNPLLPIDATFPMFIAAELPVGVTGLIIAGIFAAAMATLSGIMNSVATLISVDFYEKLHKGHSAQQSVRFAELMTVVVGLVGIGAALLLSKFDIHSLFDVSIELAGLLGGGFAGAYTLGMFTRRANWQGVAIGIGASVVLTLGIWTLRAVHPYYYLAISIALCIVIGYIASLFFPAPTQSLDGLTIYRDKPSSAPAGHLLPQAGEGTAKAD
>NZ_AP014940.1|WP_096382390.1|5908155_5909049_+|LysR-family-transcriptional-regulator
METQFLNTFVTIVDQGSMAAAARVLGITPAAVAQQIRTLEREIGAPLIARVGRTVSVTEEGARILPRTRELLRNIADLRSVATESEIAGELRLGACPTALAGILPDVLARMVETFPQINVFIKPGYSADLYHAVEQGDLDAAIVLQAPFPLPKTCEWQLLREEPLIVLAPAHLADRDPHELLATQPLIRYDRHQWGGRQAEEYLRAQRIVPRERFELNALNAIAVMVDRGLGVSLVPDWAQPWPEGLKLARIPLPDASAKRCIGIVWSRSSVRVRLVTVLLQESRKAMQQRSAPKPL
>NZ_AP014940.1|WP_096382395.1|5909396_5911691_+|TonB-dependent-receptor
MLKPLSAAIGSALLLSFAAGTATAQDAAADAAPAAPESETAAANRAAVNLDNVVVTGTRSPKAVDKIPGAITLVSKAELARSLVLTEDATAVLARTVPGYAESSQAMSNTGENLRGRVALRLFDGVPQGSPLREGTRNGTFTDMGIVGRIEVINGPSASEGIGAAGGIINYLSAAPTKEGNEFTVVSRYTTQFKDDSAGWKLGFNFARKAGNFDMLASASFLDRGITYDGSGRRIGMNTSGSLADTESRNLFLKAGYDFGEDGTQRIEGSVSHFNIEGKANYIQVLGCRPDERALCGETRTNTSERGKIFGSKAAINDFKQYQLTYTNSDFFGGTLTVNGYKADQEMRYLPENTIDRQDPLLGPIGQVWDQSEIVTNKKGLRTSWARPSLFAVEGLELRVGVDLVEDTAEQRLALTDRLWVPPMEYKSRAPWMQLSWDIGPVTLSGGLRREDGELHVNDYTTTWYRDRRHVGGGTLDYQENLTNFGAVWRVNEQWSVFGSYGEGFTLANVGIPLRNVQCSGDGGSIQTNGCPNDPPISVGDLLDLNAIVVKNTEFGFNWRGERGSLSASHYDSKSDYGQSLAIDPVTNDLVLLRAPVRIKGVELSADWRFNDAWRVSAVYSRTRGKTAFWTADAAGRFGAGGLNKPMGVLDINPDKLAWTVTWNFRPNADVSLGATTLFSRDLSGSDVRTFDNRAFSFNESTKGYTLFDLGFNYETERYGKFSLGIENLLDKQYILSWSQPPGGFQNYWAGRGRMISLSHTFKF
>NZ_AP014940.1|WP_172437346.1|5911938_5913222_+|beta-lactamase-family-protein
MGGPSGLTLSAQPSANPSPYAALHAFLDRATRPGGYLGAVSLIVRNGKIVDFQAYGQRDLARREPMRHDAIFRIYSMSKTVTSAAVMQLAERGLIDVEAPIERYLPELAHRRVVAGGTAAAPRLRPAQRPITVRHLLTHTAGFAAGLPGDETAAALTQGHDPHAARDLAGFVARLAQAPLAADPGTRFGYDGAATETLARLVEVVSGQTFDAYLREHLFAPLQMRDTGFVVASSERKRIADLTTTGDDGRLRLDDGPSQREPGAPLNAYPSGAGGLYSTACDYARFAQMLLDGGRIAERSGFAQCDGKRARGPGPRVLRADTVAAMLRNQLSMLDPPVHQFDPGEGFGFGGAVVIDPTKRSAPASLGQFGWPGAASTTYAIDPLRKTVAIALLQHLPRTGAAGDPPRLSRDFYRLAFAAADAAPSPP

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Crispr_ID: NZ_AP014940_21

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_AP014940_21

6076143-6076245

Orphan

Consensus_repeat	Method
TTCCGGCTTTCGCCGGAATGACGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_AP014940_21

>merge|NZ_AP014940|21|6076143-6076245|CRISPRCasFinder
TTCCGGCTTTCGCCGGAATGACGGCGTGGGGGTTGCGGGCTTCGGGAGATCACAGCGGAGCCGCGTCGCTGCGGTTGGATTCCGGCTTTTGCCGGAATGACGG

>NZ_AP014940|21|20|6076143-6076245|CRISPRCasFinder
TTCCGGCTTTCGCCGGAATGACGG	CGTGGGGGTTGCGGGCTTCGGGAGATCACAGCGGAGCCGCGTCGCTGCGGTTGGA
TTCCGGCTTTTGCCGGAATGACGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_AP014940.1\|WP_096382776.1\|6077290_6078304_-\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224054
NZ_AP014940.1\|WP_096382789.1\|6081210_6081957_+\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|226927
NZ_AP014940.1\|WP_096382761.1\|6069850_6070315_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|236828
NZ_AP014940.1\|WP_096382793.1\|6081953_6083141_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|224582
NZ_AP014940.1\|WP_096382800.1\|6085942_6087286_+\|zinc-ribbon-domain-containing-protein	unknown	unknown	gnl\|CDD\|379090
NZ_AP014940.1\|WP_096382781.1\|6078538_6079285_+\|ferredoxin--NADP-reductase	unknown	unknown	gnl\|CDD\|99792
NZ_AP014940.1\|WP_172437352.1\|6063855_6064947_+\|hybrid-sensor-histidine-kinase/response-regulator	unknown	unknown	gnl\|CDD\|381093
NZ_AP014940.1\|WP_096382797.1\|6083436_6084474_-\|energy-transducer-TonB	unknown	unknown	gnl\|CDD\|367555
NZ_AP014940.1\|WP_096382747.1\|6062649_6063603_-\|aldo/keto-reductase	unknown	unknown	gnl\|CDD\|381307
NZ_AP014940.1\|WP_096382768.1\|6074130_6074982_+\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_096382744.1\|6061457_6062672_-\|DMT-family-transporter	unknown	unknown	gnl\|CDD\|223769
NZ_AP014940.1\|WP_074871258.1\|6076481_6077294_-\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|237896
NZ_AP014940.1\|WP_096382752.1\|6065740_6068287_-\|ATP-dependent-helicase-HrpB	unknown	unknown	gnl\|CDD\|273901
NZ_AP014940.1\|WP_074871270.1\|6084881_6085943_+\|SPFH-domain-containing-protein	unknown	unknown	gnl\|CDD\|372597
NZ_AP014940.1\|WP_096382784.1\|6079525_6081067_+\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|312032
NZ_AP014940.1\|WP_096382758.1\|6069034_6069829_+\|TatD-family-hydrolase	unknown	unknown	gnl\|CDD\|182449
NZ_AP014940.1\|WP_172437353.1\|6070641_6073731_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|238657
NZ_AP014940.1\|WP_096382755.1\|6068349_6068811_-\|hypothetical-protein	unknown	unknown	unknown
NZ_AP014940.1\|WP_074871438.1\|6087583_6088786_+\|MFS-transporter	unknown	unknown	gnl\|CDD\|225371
NZ_AP014940.1\|WP_096382772.1\|6075060_6075594_-\|hypothetical-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_AP014940.1\|WP_096382789.1\|6081210_6081957_+\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|226927	COG4555, NatA, ABC-type Na+ transport system, ATPase component [Energy production and conversion / Inorganic ion transport and metabolism].	7.50358e-115
NZ_AP014940.1\|WP_096382752.1\|6065740_6068287_-\|ATP-dependent-helicase-HrpB	gnl\|CDD\|273901	TIGR01970, ATP-dependent_RNA_helicase_HrpB, ATP-dependent helicase HrpB. This model represents HrpB, one of two related but uncharacterized DEAH-box ATP-dependent helicases in many Proteobacteria, but also in a few species of other lineages. The member from Rhizobium meliloti has been designated HelO. HrpB is typically about 800 residues in length, while its paralog HrpA (TIGR01967), also uncharacterized, is about 1300 amino acids long. Related characterized eukarotic proteins are RNA helicases associated with pre-mRNA processing. [Unknown function, Enzymes of unknown specificity].	0
NZ_AP014940.1\|WP_096382800.1\|6085942_6087286_+\|zinc-ribbon-domain-containing-protein	gnl\|CDD\|379090	pfam13248, zf-ribbon_3, zinc-ribbon domain. This family consists of a single zinc ribbon domain, ie half of a pair as in family DZR. pfam12773.	0.00218328
NZ_AP014940.1\|WP_096382781.1\|6078538_6079285_+\|ferredoxin--NADP-reductase	gnl\|CDD\|99792	cd06195, FNR1, Ferredoxin-NADP+ (oxido)reductase is an FAD-containing enzyme that catalyzes the reversible electron transfer between NADP(H) and electron carrier proteins such as ferredoxin and flavodoxin. Isoforms of these flavoproteins (i.e. having a non-covalently bound FAD as a prosthetic group) are present in chloroplasts, mitochondria, and bacteria in which they participate in a wide variety of redox metabolic pathways. The C-terminal domain contains most of the NADP(H) binding residues and the N-terminal domain interacts non-covalently with the isoalloxazine rings of the flavin molecule which lies largely in a large gap betweed the two domains. Ferredoxin-NADP+ reductase first accepts one electron from reduced ferredoxin to form a flavin semiquinone intermediate. The enzyme then accepts a second electron to form FADH2 which then transfers two electrons and a proton to NADP+ to form NADPH.	6.68464e-71
NZ_AP014940.1\|WP_172437352.1\|6063855_6064947_+\|hybrid-sensor-histidine-kinase/response-regulator	gnl\|CDD\|381093	cd17538, REC_D1_PleD-like, first (D1) phosphoacceptor receiver (REC) domain of response regulator PleD and similar domains. PleD contains a REC domain (D1) with the phosphorylatable aspartate, a REC-like adaptor domain (D2), and the enzymatic diguanylate cyclase (DGC) domain, also called the GGDEF domain according to a conserved sequence motif, as its output domain. The GGDEF-containing PleD response regulators are global regulators of cell metabolism in some important human pathogens. This model describes D1 of PleD and similar domains. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.	2.78859e-42
NZ_AP014940.1\|WP_096382797.1\|6083436_6084474_-\|energy-transducer-TonB	gnl\|CDD\|367555	pfam03544, TonB_C, Gram-negative bacterial TonB protein C-terminal. The TonB_C domain is the well-characterized C-terminal region of the TonB receptor molecule. This protein is bound to an inner membrane-bound protein ExbB via a globular domain and has a flexible middle region that is likely to help in positioning the C-terminal domain into the iron-transporter barrel in the outer membrane. TonB_C interacts with the N-terminal TonB box of the outer membrane transporter that binds the Fe3+-siderophore complex. The barrel of the transporter, consisting of 22 beta-sheets and an inside plug, binds the iron complex in the barrel entrance.	4.90389e-17
NZ_AP014940.1\|WP_096382747.1\|6062649_6063603_-\|aldo/keto-reductase	gnl\|CDD\|381307	cd19081, AKR_AKR9C1, AKR9C family of aldo-keto reductase (AKR). Haloferax volcanii aldo-keto reductase is a founding member of aldo-keto reductase family 9 member C1 (AKR9C1).	6.92335e-173
NZ_AP014940.1\|WP_096382744.1\|6061457_6062672_-\|DMT-family-transporter	gnl\|CDD\|223769	COG0697, RhaT, Permeases of the drug/metabolite transporter (DMT) superfamily [Carbohydrate transport and metabolism / Amino acid transport and metabolism / General function prediction only].	1.94224e-18
NZ_AP014940.1\|WP_074871258.1\|6076481_6077294_-\|ABC-transporter-permease	gnl\|CDD\|237896	PRK15066, PRK15066, inner membrane transport permease; Provisional.	2.17494e-157
NZ_AP014940.1\|WP_096382761.1\|6069850_6070315_-\|hypothetical-protein	gnl\|CDD\|236828	PRK11034, clpA, ATP-dependent Clp protease ATP-binding subunit; Provisional.	0.00692239
NZ_AP014940.1\|WP_074871270.1\|6084881_6085943_+\|SPFH-domain-containing-protein	gnl\|CDD\|372597	pfam13421, Band_7_1, SPFH domain-Band 7 family.	3.70067e-102
NZ_AP014940.1\|WP_096382784.1\|6079525_6081067_+\|alpha/beta-hydrolase	gnl\|CDD\|312032	pfam08386, Abhydrolase_4, TAP-like protein. This is a family of putative bacterial peptidases and hydrolases that bear similarity to a tripeptidyl aminopeptidase isolated from Streptomyces lividans. A member of this family is thought to be involved in the C-terminal processing of propionicin F, a bacteriocidin characterized from Propionibacterium freudenreichii.	5.95468e-18
NZ_AP014940.1\|WP_096382758.1\|6069034_6069829_+\|TatD-family-hydrolase	gnl\|CDD\|182449	PRK10425, PRK10425, 3'-5' ssDNA/RNA exonuclease TatD.	2.21623e-113
NZ_AP014940.1\|WP_172437353.1\|6070641_6073731_-\|TonB-dependent-receptor	gnl\|CDD\|238657	cd01347, ligand_gated_channel, TonB dependent/Ligand-Gated channels are created by a monomeric 22 strand (22,24) anti-parallel beta-barrel. Ligands apparently bind to the large extracellular loops. The N-terminal 150-200 residues form a plug from the periplasmic end of barrel. Energy (proton-motive force) and TonB-dependent conformational alteration of channel (parts of plug, and loops 7 and 8) allow passage of ligand. FepA residues 12-18 form the TonB box, which mediates the interaction with the TonB-containing inner membrane complex. TonB preferentially interacts with ligand-bound receptors. Transport thru the channel may resemble passage thru an air lock. In this model, ligand binding leads to closure of the extracellular end of pore, then a TonB-mediated signal facillitates opening of the interior side of pore, deforming the N-terminal plug and allowing passage of the ligand to the periplasm. Such a mechanism would prevent the free diffusion of small molecules thru the pore.	3.85355e-20
NZ_AP014940.1\|WP_096382793.1\|6081953_6083141_+\|ABC-transporter-permease	gnl\|CDD\|224582	COG1668, NatB, ABC-type Na+ efflux pump, permease component [Energy production and conversion / Inorganic ion transport and metabolism].	4.88348e-46
NZ_AP014940.1\|WP_074871438.1\|6087583_6088786_+\|MFS-transporter	gnl\|CDD\|225371	COG2814, AraJ, Arabinose efflux permease [Carbohydrate transport and metabolism].	5.60976e-102
NZ_AP014940.1\|WP_096382776.1\|6077290_6078304_-\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224054	COG1131, CcmA, ABC-type multidrug transport system, ATPase component [Defense mechanisms].	7.78726e-94

>NZ_AP014940.1|WP_096382772.1|6075060_6075594_-|hypothetical-protein
MRLTPLAAIASLALLAACTAPDKPKDATATPAADSAAATAPQPAVAADGPGPASAKIGADQVGKVSPVPAFKGFGEHWSIDIQATGEMNHKVDLTWGSGSEKASGSARYNGQPADAPNTLIVLSGELQTQAGAKPMTIEISKKECIDDGDNKHMHSVDVSVEGMDKLTGGCGDLAVY
>NZ_AP014940.1|WP_096382768.1|6074130_6074982_+|hypothetical-protein
MPTALAENRSPAFVPLALSTLVFVLSGAFVLVAALSSPAAQGTGLNVAQWLCSIGSLIGFVAALACVLTDRRGVPVRPWACILAALVLIFGLGVAWSLLQTPLMQSLAQRSGAQTLGAWAAGLGALKVVAVNLVALPLAWWLGGRGALPVVWTSRQRRAIGALVALSLGAGVALLVQTAAAAFTALGEGEQRAGMSVVGLAVGAVHGLTALIAPVRRGSGALPALWSSLLTPALIVLASLPAMLGGEHWELAARVIAVALALLLAPVASWLLVRWLHGRSTRA
>NZ_AP014940.1|WP_172437353.1|6070641_6073731_-|TonB-dependent-receptor
MLGICLALAVPAALAQQAAPAAKPAAAESKPASAPTDLDRLVVTGSRIRRAGFDTLEPATVVSKDYIASRGITNVADALNEIPGFGVGITPEGGQATFGTGVNFVNRFGIGSARTLTLVNGRRFVTSAPTTLFGPAAPGLQVDLNAIPTALVERVENIAIGGAPTYGSDAIAGVVNVILRKNYEGVEAGASYGVTEQGDNERYNAWALVGANFDDGRGNVTFSFTYDDSKGVLQKERDFFRAGYFNAANPLAARMAALFPGRTPGNDGRYNPNIPFNTGNNDGIPNGVLIKDRRIWSTPFGGLISPVTGAFKPGTDNMVANGFGPGGNTVLAFDRSGNLVPYNQGIPFSATDASGGDGISLVDAGQVISDLKRMSVNTTARWALNDRVDVFMEGSFYSAESTELTDQWAYNSPLFGGASQMLRFPTTYALLTDQARAQLNALGVTAFNLSRASRDLITNNGSGTTELGRIVLGLEGDFDIGERTFYWEASANYGRSDSRAYGTSLNQQNFVNALNVVRVNGQVVCAGAPVAGVVVPGGVTAKPDPNCVPLDLFGEGRPSAAARQYVTTRTASQALQEQEVYNINVSSTLFDLWSGPLQYNIGFEHRKESGLFDPGSFLEQGLGRSVPITPLQGHYTTNEWFGEFVLPLVNPERNFIGLRKLDVIGKYRQVDNSINGKFDTYTYGLQWKPFEDLEIRGNFTRSLRSPSITEAFLPQATSFQFVTGDPCDSRFINSGANVANRQRNCQAFLNYYGLSNFTSNANGASIQGISGGNPNLRNESADSYTYGFTWAPSFAEGLTVTADYYNIKIKDVISSLTAADIATACFDASDFNAGDVPNANSFCSRIVRNAPGSAAGAGQATTFISGFVNGKSLTMEAYSTEIAYRFDTDRFGRFAFGLTGYFPKELTVDVTGVAPNPAAGEIGTSKRQYQISGAWEMGKWGLNLTGNYLSSAEFNVLNTPETRDILKVGDYWLFNGGVRYRLNDHAMLRLAVTNLFDKDPPFPAQTSADSFSTYDVLGRRYNLAFEWKF
>NZ_AP014940.1|WP_096382761.1|6069850_6070315_-|hypothetical-protein
MRTHFAAAAALALALCACAAHAQQPTFPAPAFRGGNVDWQVVLKTQQDLTVVYQLKVPEADKPQKGGLGQRNAAYGGYVLVGEIGVEKTAMTVKIAPVPLGKPCKLANGLMGDSYGRFTYSIDVIPQKAKPVSTKNDHKPWPAKWSGCGNFTLD
>NZ_AP014940.1|WP_096382758.1|6069034_6069829_+|TatD-family-hydrolase
MQLIDIGANLTHDSFDHDRDAVLQRARAAGVTRMVITGASREHSPKALELARQHPGELFATAGVHPHHASEYTAECDAEMRALLAHDEVVAVGECGLDYFRDFSPRPAQRRAFEMQLQSAVDTGKPLFLHQRDAHDDFVAMMKNFDGKLGPAVVHCFTGTREELFAYLDRDWYIGITGWLCDERRGLHLRELVKHIPAQRLMIETDAPYLLPRTVKPAPSHRRNEPMYLAHIIEELARDRGEDVAVAAARSTATATGFFRLPPQ
>NZ_AP014940.1|WP_096382755.1|6068349_6068811_-|hypothetical-protein
MRIATFCLAALLTLAGAVHAATPAKLDFPENAFNGGNTDPVWSIELKREDVGLVRYSLSSPRGVPIAAGTLKSVAPVLKLPVFGELKGEYGLAGTATIQQRSRPMQVLVGPSRAGAPCQDARGKKYAQAVFIAIGDASDPDKLYYGCGEYRKP
>NZ_AP014940.1|WP_096382752.1|6065740_6068287_-|ATP-dependent-helicase-HrpB
MNSPAFPIDPLLPQIRDSLAAHPRLVLDAPPGAGKTTQVPPALLDAPWLDGRRIVMLEPRRVAARAAANFMARQRGEAAGDTVGYRIRFENKVSARTRIEVVTEGILTRMIQDDPTLDGVGALLFDEFHERHLAADLGLALALDVQASLREDLRIVVMSATLDGERLAQFLDAPRLSSAGRSYPVQIGHYPARREEKLEHQLKRAIEHALATHPGDVLAFLPGQREIARADAALAGSEAARGVDVLALHGELPVEQQSRVLQPDPDGRRRVVLATNVAESSVTLPGVRVVIDSGLAREPRYDPNSGFARLDVVAIAQASADQRAGRAGRVADGWAYRLWPESQRLEPQRRPEMAQVELAGLALELAAWGDAGLRFLDAPPPGALAAARELLLRLGALEPGAGAQLAITAFGRRMLALGTHPRLAAMLLAPREAGERALACDLAALLEARDPLRSGGDALHARWQALAAFRAGRAPADASRSALAALDQASKQWRRRLRVDNPPPSSAPAHALGDLLLHAFPDRIARQHPSDPYRYQLANGRSAKLFDDSAVYGEPWLAISELRDDPRDARILRAAPLDEARLEREFPQRFVSEDRVVWDAAARGIAAVRERRFDRIVIDSRPLARPDPSRYADALIDAVRQLGLDALPWTPGLRQWRARVRGLREWMPELTQGDTPLPDLSDSALLERLDQWLKPALSGKTRLDALDEAGFGEALRSLCDWSWRQKLDALAPSRIVVPSGMERAIEYSYDDHALDGRGAAQAPVLAVKLQELFGLADTPRIADGRVPLTLHLLSPAGRPLQVTQDLRGFWERTYPEVKKEMKGRYPKHPWPDDPWTATATHRAKPRGT
>NZ_AP014940.1|WP_172437352.1|6063855_6064947_+|hybrid-sensor-histidine-kinase/response-regulator
MSTPATSTGRILVVDDQAANLRVVTALLSRQGYEVVAASTGDEALQLYAQSPPDLILLDVMMPGMDGFEVMDALRADSPLRVPVVFVTAAHDRDLLLRAFDAGVVDYVTKPFLPEELLARVNAHVGLKLTRDRLERVAREREELVNLVAHDLKNPLTSVLFASDLLINNGCKPERVPRYLQMIHESADDALGYIRHYLESQAGHRERAEHGARADLAETLDWLVRRYEMQLDARGIRVQVQPPANGSAQVAMDSRVLRQVSENLVTNAMKYAPGGDLTLAARNSAPGFWQLIVADRGPGIPVARQRELFKPFVRLHDNDIDDGLSSGLGLSLAKQIVVNAGGQLWYEERKHGGSRFIIELPEA
>NZ_AP014940.1|WP_096382747.1|6062649_6063603_-|aldo/keto-reductase
MNLRPLGRSSLSVAPLAFGGNVFGWSADEATSFALLDAFTEAGFALVDTADVYSAWVPGNQGGESERIIGRWLAQGGGRRERVVVATKVAKWAPRRGLAPATIQAAVDDSLRRLGTEVIDLYQAHEDDPTVPLEDTLGAFARLIEAGKVRAIGASNYSAARLAQALDVSERHGLPRYETLQPEYNLCDRAGFEAELEPLVRERGVGVIGYYSLASGFLTGKYRSRADLGKSRARGGAVEKYLDARGLRILAALDEVAAGHGATPAQVALAWLIARPSVTAPIASATSVAQLHELLAATRLNLRVDEIAALDAASAGG
>NZ_AP014940.1|WP_096382744.1|6061457_6062672_-|DMT-family-transporter
MRPAPAADRGRAGGRADAGRFDAARSDAVRPTARRSKARRSHRRVADPALALPCAADAPTFAIAFLPVPPPLANAAAAPAPSRDEPPVSPASSSTARRTGVALAASGAILFSAKAILAKLQYRYGVDSLQVLALRMAFSLPLFAALGVREHGRARARGALPTRRDWGLIVVLGVLGYYLSSLLDFWGLEYVPVSLERLILFLNPTIVLLIGLFAFKRRVAAREWTALAVSYAGVVLVMVENLRVEGEHVLFGSALVLGAAVSYALYLAMSGELIKRLGSLQLVAWAMIVSTAAVLIHYLIARPPSALFGLPWQVYALAAANAVFCTFLPVTFTMAAVGRLGAGTAAQFSVIGPVSLVFLGAWVLGEKITAIQLVGTAVVLGGVWLLSRPGANSVPLPAADKPSS
>NZ_AP014940.1|WP_074871258.1|6076481_6077294_-|ABC-transporter-permease
MSSEIQTADSAAISPARRNLTALGTIVRREVTRILRIWGQTLVPPAITMTLYFLIFGGLIGSRIGDMGGYSYMEFIVPGLVMMSVIQNSYGNISSSFFGAKFGRHVEELLVSPMPNWVILWGYVAGAVLRGLMVGAIVLLIAMCFTKVRIPHPLVTFTTVLLGATIFSLAGFINAVYAKKFDDVAIVPTFILTPLTYLGGVFYSVKLLPAWAEAATHANPIFYMVNAFRYGLLGSSDVPLWVAYALMLAFVVALSSLGLWLLKRGVGLRS
>NZ_AP014940.1|WP_096382776.1|6077290_6078304_-|ABC-transporter-ATP-binding-protein
MTQPTALATGPRQVSAAAVAAGAAVPALRVRDLRKTYDNKVQALKGVSLDVAEGDFFALLGPNGAGKSTLIGIVSSLVNLSDGAVEIFGTDLQRRRDEAMRLIGLVPQEINFNMFEKPLDILVNYAGFYGVPREQALVRAEEELKRAQLWDKADKMSRTLSGGMKRRLMIARAMMTRPRLLILDEPTAGVDIEIRRGMWKTLREINAAGTTIILTTHYLEEAESLCRNLAIIDQGRIVQQGPMKALLAMLDVEGFLLDIDGVLPAALPQIEGATLAAADDHTLDLEMPRAMDLNRVFAALGEAGIRVRSMRTKSNRLEELFVRMIAPPSAAATGSAA
>NZ_AP014940.1|WP_096382781.1|6078538_6079285_+|ferredoxin--NADP-reductase
MKQFPLKLVSRRMLAPTVGHYVFQRGDGEPLDYIPGQFIQVHFQYADGTATKRSYSLATIHDHALGPGEAVEIAVSYVPGGAATALFEGLGEGDAVQASGPFGRFCLMPADANRRYLLIATGTGVTPYRAMLPQLERQIRERGIEVVLLFGARTPAELLYGDEFRAFADRVPGFRFVPCFSRELPAEPHADVRHGYVQQFLAEFAPDAAGDIAYLCGNPNMVDACFEALKDYGLAVPQIRREKYVSSK
>NZ_AP014940.1|WP_096382784.1|6079525_6081067_+|alpha/beta-hydrolase
MPIDWKHPRPRCAAIALAAAFAALTLAGCGRGANAASADGGAVKRRYGSIAFEPCTLASPFATGTIPAQCARFKVPENHAEPNGRKIELNLAWLPATDSSAAEDDPVFFLAGGPGQAATSSWPLVDAAFRDVRKRRNIVLVDQRGTGKSAPLTCTEAVPQDDDGGDEAAQLAASVEAVRRCAQGLKVDARYFTTTDAIADLDAVRAAIGAAKVDLVGVSYGTRVAQQYAGRYPQRTRAVVLDGVAPNELVLGSEHARNLDAALAQQFKLCQQTPACRARFGADPREQLRQLMVRLQAQPVEVDYRDPSTGEPRRERVTAGHVAMLTRMFSYQPEAASLLPLVLSEADQGRYAPLLALSKMIGGQLSEELNYGMQLSVTCAEDADLFVNDPADKDTVLGNAMTDALKAQCAVWPTGTRPKDFHQPLRSNLPVLLLSGELDPVTPPRYGEQVLKNLPNGRHLVLRGQGHGALRVGCTPKLLGQFLESGDAKALDARCLDALGYVPPFVSFTGWEP
>NZ_AP014940.1|WP_096382789.1|6081210_6081957_+|ATP-binding-cassette-domain-containing-protein
MITAHDLHKSFKTKSGTVAAVQGVDFQARDGEITGLLGPNGAGKTTTLRMLYTLMRPDRGEVRVDGVDAAKDPAAVRRSLGVLPDARGVYKRLTARENIAYFGELHGLSRAQIEQRTAELARALDMGDILDRQTEGFSQGQRTKTAIARALVHDPRNVILDEPTNGLDVMTTRAMRGFLRGLREEGRCVIFSSHIMQEVAALCDRIVIVAKGQVVAAGTADELRAHTGEDNLEDAFVKAIGSDEGLHA
>NZ_AP014940.1|WP_096382793.1|6081953_6083141_+|ABC-transporter-permease
MKVNPFAAFWSVVRKELRDISRDRRTLAITLLMGPLLYPLLMLGMGSLAENRARTQLDSVLKVPVVGAERAPNLVKFLATQNIVAVPAPKDLDAAVQNQEHDVGLIVSPDFGKDWKAGQPALVEIVQDSTRRDADIPARRLHAALEGYSRQVGALRLLARGIAASVIQPVNVADRDVATAEAKRGLILSALLPYLLIMTSFAGGAFLIIDATAGERERQSLEPLLATPAPRAAIVSGKIAAACVLGLFSLLLTLLAFKLSAQMSSGVGRMLDVSLYAIGKMLLILLPMSFIGTALLTYLSAAAKSLKEAQSHVTWLMLLPLLPTFVLMVNPLKTQLWQFAVPFLAQNQLLLKVIRGETINGQTWAMYLACGFGLAALLWVAAVRRYNNERLAISG
>NZ_AP014940.1|WP_096382797.1|6083436_6084474_-|energy-transducer-TonB
MIANNDRHCSRLSAVKQVSAVFALGCALAACGKKEEAAPAAPEQAAPSASAPAANAGNAVSAKVSALSVEQLREAARKAYAENRLYAPAEDNAVEYYLALREKAPADAVASSALTDLLPMTVIATEQSIGREDFSEAQRLSALIERADPQHPAMARLKAAIASAQQAVTKRAEQEKLTAEDQARKQAELEKQRLAQQQQQQQQAAQQLAAQQAAERQAATRAAEQRAAEQRAAEQRPAPTAAAPERPAPAPTAPSAPAAAASDLRAVSTPAPRYPPDALRAGTSGEVQVEFTVGTDGSVTAARVVRANPPRVFDREAVNAVRKWRFQPVPAPVTTRRTIGFNPGG
>NZ_AP014940.1|WP_074871270.1|6084881_6085943_+|SPFH-domain-containing-protein
MSILGFIKGELLEVIEWTDDSRDTLSYRFPDDDKEIKNGAQLIVRESQQVQFVAAGQYADLFGPGKHTLKTENIPVLSTILGWKYGFQSPFKCDVYFLNTRLFTGNKWGTANPVMMRDADFGVVRLRAFGTYDFRIVDPPKFLKEVAGTDQNFRLDEFADTMRSRIVSVFTEALASAKVPALDVASRYTELGEALLPLINPAMTSKYGIEIASFVLENVSVPPEVEKAIDARSSMSAVGNLNDYVKFQMGSAMGQGGDASAAVPAQMAMGFGIAQEMMRGMQGAPQGNAAAAPAADAAPAGGLEVLTPEQAATALGVSVEDVMAAIAAGDLKARKIGNATRIAKSALEEFLRG
>NZ_AP014940.1|WP_096382800.1|6085942_6087286_+|zinc-ribbon-domain-containing-protein
MDNATVGKHPCPECGGDLQWNAGKQALACPYCGTVVPLASSPAGAGDGSAQIVEHDLEEALARIPPELPEPRAQGAAGNGAQEPDLAAVHATIERLARSPGGAPGTASSWSVAARSQDGEFELKGSQNGHALELLRSMAATPAEQRGYGAQRREVQCQSCHAISVFVDGKVADRCEFCGSPSIIDHESLGDAITPESLLPFKISDGQVRDAIRKWYGSRWFAPNRLKTAALTDTLKGVYLPYWTFDADVSARWSAEAGHYYYVTESYTENGQRKTREVQKIRWEPASGSLQLFFNDELVPGTVGVHADLLQKIGDFPTTTDLKPYSPEFVRGWTVERYQVDLRQAAQRGEAQMRERTRAACSAEVPGDTQRNLQVDAKLSRRTFKHVLVPVWLVSYTYGSRSYQVLANGYTGALAGERPYSWVKIFFAALAAVLALLVLLAVFGGTR
>NZ_AP014940.1|WP_074871438.1|6087583_6088786_+|MFS-transporter
MPLALLALTLGAFAIGTTEFVIVGLIPTLAADLGVDLPSAGLLVSLYALAVAIGAPLLTALTGRVPRKPLLIGLMALFTAGNVVAWLAPGYATLIVARVLTGLAHGVFFSVGSIIATSLVPKEKAASAIATMFSGMTVAFVTGIPLGTFLGQHFGWRATFLAVAGFGLIALIGSALFVPRRIAHSAPAPLRQQAALLLQPRLLLVYAMTAVGYGGSLIAFTFLAPILQDIAGFGPNMVGAVLLAYGVSVAIGNVWGGRLADRHGPVKALKTIFALLAAVLLALSFTMHSQWLVVLTALAWGAVAFGNVPGLQVYVVKQAQRYAPQAVDTAAGFNIAAFNLGVAGGAWAGGQVVAHLGLAHTPWIAALVVFAAFGLTALSGRLDRRDGVAERAEGIAVAAH

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity
NZ_AP014940_12	12.1\|4931140\|53\|NZ_AP014940\|CRISPRCasFinder	4931140-4931192	53	NZ_AP014940.1	5741502-5741554	1	0.981
NZ_AP014940_21	21.1\|6076167\|55\|NZ_AP014940\|CRISPRCasFinder	6076167-6076221	55	NZ_AP014940.1	4804946-4805000	2	0.964
NZ_AP014940_21	21.1\|6076167\|55\|NZ_AP014940\|CRISPRCasFinder	6076167-6076221	55	NZ_AP014940.1	4805185-4805239	2	0.964

1. spacer 12.1|4931140|53|NZ_AP014940|CRISPRCasFinder matches to position: 5741502-5741554, mismatch: 1, identity: 0.981

agctgggggttgtgaggcttcgggaggttacggcggagctgcgtcgcttcggt	CRISPR spacer
agctgggggttgtgaggcttcgggaggttacggcggagctgcttcgcttcggt	Protospacer
****************************************** **********

2. spacer 21.1|6076167|55|NZ_AP014940|CRISPRCasFinder matches to position: 4804946-4805000, mismatch: 2, identity: 0.964

cgtgggggttgcgggcttcgggagatcacagcggagccgcgtcgctgcggttgga	CRISPR spacer
cgtgggggttgcgggcttcgggaggtcacggcggagccgcgtcgctgcggttgga	Protospacer
************************.****.*************************

3. spacer 21.1|6076167|55|NZ_AP014940|CRISPRCasFinder matches to position: 4805185-4805239, mismatch: 2, identity: 0.964

cgtgggggttgcgggcttcgggagatcacagcggagccgcgtcgctgcggttgga	CRISPR spacer
cgtgggggttgcgggcttcgggaggtcacggcggagccgcgtcgctgcggttgga	Protospacer
************************.****.*************************

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity
NZ_AP014940_3	3.1\|1312981\|25\|NZ_AP014940\|CRISPRCasFinder	1312981-1313005	25	NZ_CP049158	Caballeronia sp. SBC1 plasmid pSBC1_2, complete sequence	1729179-1729203	2	0.92
NZ_AP014940_3	3.1\|1312981\|25\|NZ_AP014940\|CRISPRCasFinder	1312981-1313005	25	NZ_CP049318	Caballeronia sp. SBC2 plasmid pSBC2-2, complete sequence	1733847-1733871	2	0.92
NZ_AP014940_3	3.1\|1312981\|25\|NZ_AP014940\|CRISPRCasFinder	1312981-1313005	25	NC_013502	Rhodothermus marinus DSM 4252 plasmid pRMAR01, complete sequence	100002-100026	4	0.84
NZ_AP014940_3	3.1\|1312981\|25\|NZ_AP014940\|CRISPRCasFinder	1312981-1313005	25	NC_015970	Rhodothermus marinus SG0.5JP17-172 plasmid pRHOM17201, complete sequence	22906-22930	4	0.84
NZ_AP014940_7	7.1\|3309717\|28\|NZ_AP014940\|CRISPRCasFinder	3309717-3309744	28	NC_012718	Burkholderia glumae BGR1 plasmid bglu_2p, complete sequence	66485-66512	4	0.857
NZ_AP014940_7	7.1\|3309717\|28\|NZ_AP014940\|CRISPRCasFinder	3309717-3309744	28	NZ_CP009433	Burkholderia glumae LMG 2196 = ATCC 33617 plasmid pBIN_1, complete sequence	7597-7624	4	0.857
NZ_AP014940_7	7.1\|3309717\|28\|NZ_AP014940\|CRISPRCasFinder	3309717-3309744	28	NZ_CP039340	Ralstonia solanacearum strain UW386 plasmid pUW386, complete sequence	1823535-1823562	4	0.857
NZ_AP014940_7	7.1\|3309717\|28\|NZ_AP014940\|CRISPRCasFinder	3309717-3309744	28	NZ_CP045091	Burkholderia glumae strain GX plasmid pWSGX3, complete sequence	37223-37250	4	0.857
NZ_AP014940_7	7.1\|3309717\|28\|NZ_AP014940\|CRISPRCasFinder	3309717-3309744	28	NZ_LR134463	Tsukamurella tyrosinosolvens strain NCTC13231 plasmid 21, complete sequence	144168-144195	5	0.821
NZ_AP014940_7	7.1\|3309717\|28\|NZ_AP014940\|CRISPRCasFinder	3309717-3309744	28	NZ_CP023740	Methylosinus trichosporium OB3b plasmid pOB3b3, complete sequence	45835-45862	5	0.821
NZ_AP014940_7	7.1\|3309717\|28\|NZ_AP014940\|CRISPRCasFinder	3309717-3309744	28	NZ_CP029602	Streptomyces sp. WAC 01438 plasmid unnamed1, complete sequence	41077-41104	6	0.786
NZ_AP014940_7	7.1\|3309717\|28\|NZ_AP014940\|CRISPRCasFinder	3309717-3309744	28	NZ_CP034352	Streptomyces sp. W1SF4 plasmid p2, complete sequence	248554-248581	6	0.786
NZ_AP014940_7	7.1\|3309717\|28\|NZ_AP014940\|CRISPRCasFinder	3309717-3309744	28	NZ_CP024986	Streptomyces lavendulae subsp. lavendulae strain CCM 3239 plasmid pSA3239, complete sequence	140930-140957	6	0.786
NZ_AP014940_7	7.1\|3309717\|28\|NZ_AP014940\|CRISPRCasFinder	3309717-3309744	28	NC_024970	Streptomyces aureofaciens strain CCM3239 plasmid pSA3239, complete sequence	100120-100147	6	0.786
NZ_AP014940_7	7.1\|3309717\|28\|NZ_AP014940\|CRISPRCasFinder	3309717-3309744	28	NZ_KJ396772	Streptomyces lavendulae subsp. lavendulae strain CCM3239 plasmid pSA3239, complete sequence	100120-100147	6	0.786
NZ_AP014940_7	7.1\|3309717\|28\|NZ_AP014940\|CRISPRCasFinder	3309717-3309744	28	NZ_LT703509	Mycobacterium chimaera strain Mycobacterium chimaera MC045 isolate Mycobacterium chimaera plasmid 5	7145-7172	6	0.786
NZ_AP014940_7	7.1\|3309717\|28\|NZ_AP014940\|CRISPRCasFinder	3309717-3309744	28	NZ_CP015274	Mycobacterium chimaera strain ZUERICH-1 plasmid unnamed 2, complete sequence	23294-23321	6	0.786
NZ_AP014940_7	7.1\|3309717\|28\|NZ_AP014940\|CRISPRCasFinder	3309717-3309744	28	NZ_CP019223	Mycobacterium chimaera strain CDC 2015-22-71 plasmid pDHQP20152271_2, complete sequence	28102-28129	6	0.786
NZ_AP014940_7	7.1\|3309717\|28\|NZ_AP014940\|CRISPRCasFinder	3309717-3309744	28	NZ_CP045965	Mycobacterium chimaera strain AUSMDU00007395 plasmid pAUSMDU00007395_02, complete sequence	14555-14582	6	0.786
NZ_AP014940_7	7.1\|3309717\|28\|NZ_AP014940\|CRISPRCasFinder	3309717-3309744	28	NZ_CP049158	Caballeronia sp. SBC1 plasmid pSBC1_2, complete sequence	928904-928931	7	0.75
NZ_AP014940_7	7.1\|3309717\|28\|NZ_AP014940\|CRISPRCasFinder	3309717-3309744	28	NZ_CP049318	Caballeronia sp. SBC2 plasmid pSBC2-2, complete sequence	933584-933611	7	0.75
NZ_AP014940_7	7.1\|3309717\|28\|NZ_AP014940\|CRISPRCasFinder	3309717-3309744	28	NZ_CP013381	Burkholderia sp. Bp5365 strain MSMB43 plasmid pMSMB43, complete sequence	295951-295978	7	0.75
NZ_AP014940_7	7.1\|3309717\|28\|NZ_AP014940\|CRISPRCasFinder	3309717-3309744	28	NZ_CP009547	Burkholderia sp. 2002721687 plasmid pBTU, complete sequence	127025-127052	7	0.75
NZ_AP014940_17	17.2\|5821638\|36\|NZ_AP014940\|CRT	5821638-5821673	36	NZ_CP018944	Escherichia coli strain Ecol_224 plasmid pEC224_4, complete sequence	11422-11457	8	0.778
NZ_AP014940_17	17.6\|5821860\|36\|NZ_AP014940\|CRT	5821860-5821895	36	KX557288	Rhodococcus phage ChewyVIII, complete genome	33845-33880	8	0.778

1. spacer 3.1|1312981|25|NZ_AP014940|CRISPRCasFinder matches to NZ_CP049158 (Caballeronia sp. SBC1 plasmid pSBC1_2, complete sequence) position: , mismatch: 2, identity: 0.92

tttcgtccccgttcgccgcagcttt	CRISPR spacer
tttcgtccccgttcgccgcagccgt	Protospacer
**********************. *

2. spacer 3.1|1312981|25|NZ_AP014940|CRISPRCasFinder matches to NZ_CP049318 (Caballeronia sp. SBC2 plasmid pSBC2-2, complete sequence) position: , mismatch: 2, identity: 0.92

tttcgtccccgttcgccgcagcttt	CRISPR spacer
tttcgtccccgttcgccgcagccgt	Protospacer
**********************. *

3. spacer 3.1|1312981|25|NZ_AP014940|CRISPRCasFinder matches to NC_013502 (Rhodothermus marinus DSM 4252 plasmid pRMAR01, complete sequence) position: , mismatch: 4, identity: 0.84

tttcgtccccgttcgccgcagcttt	CRISPR spacer
tttcgtccccgtccgccgcagcggg	Protospacer
************.*********

4. spacer 3.1|1312981|25|NZ_AP014940|CRISPRCasFinder matches to NC_015970 (Rhodothermus marinus SG0.5JP17-172 plasmid pRHOM17201, complete sequence) position: , mismatch: 4, identity: 0.84

tttcgtccccgttcgccgcagcttt	CRISPR spacer
tttcgtccccgtccgccgcagcggg	Protospacer
************.*********

5. spacer 7.1|3309717|28|NZ_AP014940|CRISPRCasFinder matches to NC_012718 (Burkholderia glumae BGR1 plasmid bglu_2p, complete sequence) position: , mismatch: 4, identity: 0.857

gcggccggagccgtcgttgttgatcgtc	CRISPR spacer
cttgccggagccgtcgttgttgatcgcc	Protospacer
 . ***********************.*

6. spacer 7.1|3309717|28|NZ_AP014940|CRISPRCasFinder matches to NZ_CP009433 (Burkholderia glumae LMG 2196 = ATCC 33617 plasmid pBIN_1, complete sequence) position: , mismatch: 4, identity: 0.857

gcggccggagccgtcgttgttgatcgtc	CRISPR spacer
cttgccggagccgtcgttgttgatcgcc	Protospacer
 . ***********************.*

7. spacer 7.1|3309717|28|NZ_AP014940|CRISPRCasFinder matches to NZ_CP039340 (Ralstonia solanacearum strain UW386 plasmid pUW386, complete sequence) position: , mismatch: 4, identity: 0.857

gcggccggagccgtcgttgttgatcgtc	CRISPR spacer
cttgccggagccgtcgttgttgatcgcc	Protospacer
 . ***********************.*

8. spacer 7.1|3309717|28|NZ_AP014940|CRISPRCasFinder matches to NZ_CP045091 (Burkholderia glumae strain GX plasmid pWSGX3, complete sequence) position: , mismatch: 4, identity: 0.857

gcggccggagccgtcgttgttgatcgtc	CRISPR spacer
cttgccggagccgtcgttgttgatcgcc	Protospacer
 . ***********************.*

9. spacer 7.1|3309717|28|NZ_AP014940|CRISPRCasFinder matches to NZ_LR134463 (Tsukamurella tyrosinosolvens strain NCTC13231 plasmid 21, complete sequence) position: , mismatch: 5, identity: 0.821

gcggccggagccgtcgttgttgatcgtc	CRISPR spacer
gcggctgcagccgtcgttgttgagccgc	Protospacer
*****.* *************** *  *

10. spacer 7.1|3309717|28|NZ_AP014940|CRISPRCasFinder matches to NZ_CP023740 (Methylosinus trichosporium OB3b plasmid pOB3b3, complete sequence) position: , mismatch: 5, identity: 0.821

----gcggccggagccgtcgttgttgatcgtc	CRISPR spacer
cttcgcggc----gccgtcgttgttgatcgcc	Protospacer
    *****    *****************.*

11. spacer 7.1|3309717|28|NZ_AP014940|CRISPRCasFinder matches to NZ_CP029602 (Streptomyces sp. WAC 01438 plasmid unnamed1, complete sequence) position: , mismatch: 6, identity: 0.786

gcggccggagccgtcgttgttgatcgtc	CRISPR spacer
gcggccggagccgtcggtgttcatgaga	Protospacer
**************** **** ** .

12. spacer 7.1|3309717|28|NZ_AP014940|CRISPRCasFinder matches to NZ_CP034352 (Streptomyces sp. W1SF4 plasmid p2, complete sequence) position: , mismatch: 6, identity: 0.786

gcggccggagccgtcgttgttgatcgtc	CRISPR spacer
gcggccggagccgtcgtggtggaggtcc	Protospacer
***************** ** **   .*

13. spacer 7.1|3309717|28|NZ_AP014940|CRISPRCasFinder matches to NZ_CP024986 (Streptomyces lavendulae subsp. lavendulae strain CCM 3239 plasmid pSA3239, complete sequence) position: , mismatch: 6, identity: 0.786

gcggccggagccgtcgttgttgatcgtc	CRISPR spacer
gcggccggagccgtcgtggtggagatcc	Protospacer
***************** ** **   .*

14. spacer 7.1|3309717|28|NZ_AP014940|CRISPRCasFinder matches to NC_024970 (Streptomyces aureofaciens strain CCM3239 plasmid pSA3239, complete sequence) position: , mismatch: 6, identity: 0.786

gcggccggagccgtcgttgttgatcgtc	CRISPR spacer
gcggccggagccgtcgtggtggagatcc	Protospacer
***************** ** **   .*

15. spacer 7.1|3309717|28|NZ_AP014940|CRISPRCasFinder matches to NZ_KJ396772 (Streptomyces lavendulae subsp. lavendulae strain CCM3239 plasmid pSA3239, complete sequence) position: , mismatch: 6, identity: 0.786

gcggccggagccgtcgttgttgatcgtc	CRISPR spacer
gcggccggagccgtcgtggtggagatcc	Protospacer
***************** ** **   .*

16. spacer 7.1|3309717|28|NZ_AP014940|CRISPRCasFinder matches to NZ_LT703509 (Mycobacterium chimaera strain Mycobacterium chimaera MC045 isolate Mycobacterium chimaera plasmid 5) position: , mismatch: 6, identity: 0.786

gcggccggagccgtcgttgttgatcgtc	CRISPR spacer
gccgccggagccgtcgtcgttgacgcgc	Protospacer
** **************.*****.   *

17. spacer 7.1|3309717|28|NZ_AP014940|CRISPRCasFinder matches to NZ_CP015274 (Mycobacterium chimaera strain ZUERICH-1 plasmid unnamed 2, complete sequence) position: , mismatch: 6, identity: 0.786

gcggccggagccgtcgttgttgatcgtc	CRISPR spacer
gccgccggagccgtcgtcgttgacgcgc	Protospacer
** **************.*****.   *

18. spacer 7.1|3309717|28|NZ_AP014940|CRISPRCasFinder matches to NZ_CP019223 (Mycobacterium chimaera strain CDC 2015-22-71 plasmid pDHQP20152271_2, complete sequence) position: , mismatch: 6, identity: 0.786

gcggccggagccgtcgttgttgatcgtc	CRISPR spacer
gccgccggagccgtcgtcgttgacgcgc	Protospacer
** **************.*****.   *

19. spacer 7.1|3309717|28|NZ_AP014940|CRISPRCasFinder matches to NZ_CP045965 (Mycobacterium chimaera strain AUSMDU00007395 plasmid pAUSMDU00007395_02, complete sequence) position: , mismatch: 6, identity: 0.786

gcggccggagccgtcgttgttgatcgtc	CRISPR spacer
gccgccggagccgtcgtcgttgacgcgc	Protospacer
** **************.*****.   *

20. spacer 7.1|3309717|28|NZ_AP014940|CRISPRCasFinder matches to NZ_CP049158 (Caballeronia sp. SBC1 plasmid pSBC1_2, complete sequence) position: , mismatch: 7, identity: 0.75

gcggccggagccgtcgttgttgatcgtc	CRISPR spacer
ggcattggagccgtcgttgttgatcgga	Protospacer
*  ...********************

21. spacer 7.1|3309717|28|NZ_AP014940|CRISPRCasFinder matches to NZ_CP049318 (Caballeronia sp. SBC2 plasmid pSBC2-2, complete sequence) position: , mismatch: 7, identity: 0.75

gcggccggagccgtcgttgttgatcgtc	CRISPR spacer
ggcattggagccgtcgttgttgatcgga	Protospacer
*  ...********************

22. spacer 7.1|3309717|28|NZ_AP014940|CRISPRCasFinder matches to NZ_CP013381 (Burkholderia sp. Bp5365 strain MSMB43 plasmid pMSMB43, complete sequence) position: , mismatch: 7, identity: 0.75

gcggccggagccgtcgttgttgatcgtc	CRISPR spacer
cttgtcggagccgtcgttgttgaccgcg	Protospacer
 . *.******************.**.

23. spacer 7.1|3309717|28|NZ_AP014940|CRISPRCasFinder matches to NZ_CP009547 (Burkholderia sp. 2002721687 plasmid pBTU, complete sequence) position: , mismatch: 7, identity: 0.75

gcggccggagccgtcgttgttgatcgtc	CRISPR spacer
cttgtcggagccgtcgttgttgaccgcg	Protospacer
 . *.******************.**.

24. spacer 17.2|5821638|36|NZ_AP014940|CRT matches to NZ_CP018944 (Escherichia coli strain Ecol_224 plasmid pEC224_4, complete sequence) position: , mismatch: 8, identity: 0.778

cgcatcggcgacaacgccagcgtcgatgaagccaag	CRISPR spacer
ctgatcggcgacaacgccagcggtgatgaattcgcg	Protospacer
*  ******************* .****** .*. *

25. spacer 17.6|5821860|36|NZ_AP014940|CRT matches to KX557288 (Rhodococcus phage ChewyVIII, complete genome) position: , mismatch: 8, identity: 0.778

ggcctggtcgccaccgagctcaacggcggcatcgac	CRISPR spacer
gtcggtatcgccaccgagatcaacggcggtatcggc	Protospacer
* *   .*********** **********.****.*

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

1715713 : 1742165

Bacillus_phage(50.0%)

tail,plate

The bacterium proteins that are colored denote the protein is present at specific phage-related keywords (such as 'capsid', 'head', 'integrase', 'plate', 'tail', 'fiber', 'coat', 'transposase', 'portal', 'terminase', 'protease' or 'lysin' and 'tRNA')

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_096377207.1\|1715713_1719154_-\|plate	putative baseplate assembly protein	A0A1J0GW37	Streptomyces_phage	6.4e-12	35.1
WP_096377208.1\|1719150_1721679_-\|plate	putative baseplate assembly protein	NA	NA	NA	NA
WP_074872264.1\|1721721_1722078_-	GPW/gp25 family protein	NA	NA	NA	NA
WP_074872267.1\|1722098_1722464_-	hypothetical protein	NA	NA	NA	NA
WP_096377209.1\|1722474_1723017_-\|plate	baseplate assembly protein	A0A127AW40	Bacillus_phage	1.7e-07	35.6
WP_096377210.1\|1723058_1724189_-	hypothetical protein	NA	NA	NA	NA
WP_096377211.1\|1724192_1724516_-	hypothetical protein	NA	NA	NA	NA
WP_074872277.1\|1724552_1725215_-	hypothetical protein	NA	NA	NA	NA
WP_096377212.1\|1725222_1726077_-	DUF4157 domain-containing protein	NA	NA	NA	NA
WP_172437171.1\|1726073_1734434_-	DUF4157 domain-containing protein	NA	NA	NA	NA
WP_172437172.1\|1734430_1734709_-	hypothetical protein	NA	NA	NA	NA
WP_096377214.1\|1734705_1736784_-	ATP-binding protein	A0A109WUE1	Acidianus_tailed_spindle_virus	2.0e-08	34.9
WP_096377215.1\|1736798_1738091_-	DUF4255 domain-containing protein	NA	NA	NA	NA
WP_096377216.1\|1738087_1738948_-	hypothetical protein	NA	NA	NA	NA
WP_096377217.1\|1738944_1739712_-\|plate	phage baseplate protein	NA	NA	NA	NA
WP_074872293.1\|1739722_1740247_-\|tail	phage tail protein	NA	NA	NA	NA
WP_096377218.1\|1740278_1742165_-\|tail	phage tail sheath subtilisin-like domain-containing protein	J9PVC2	Bacillus_phage	8.3e-38	34.5

Anti-CRISPR protein detection

Acr ID	Acr position	Acr size	Homology with known anti	Neighbor HTH/AcRanker	Neighbor Aca	In prophage	Protospacer in prophage

Overview of predicted results

Overview of the results

Cas Category Instructions

Results visualization

1. NZ_AP014940

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CRISPR-Cas detection and classification

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Self-targeting detection

MGE targeting detection<

Prophage detection

Anti-CRISPR protein detection