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_CP054139	Mucilaginibacter sp. G2-14 chromosome, complete genome	9 crisprs	cas3,csa3,PrimPol,PD-DExK,DEDDh,WYL,RT	0	0	2	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP054139_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP054139_1

407396-407494

Orphan

Consensus_repeat	Method
GCAAACAAATTGAACGATTGTGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP054139_1

>merge|NZ_CP054139|1|407396-407494|CRISPRCasFinder
GCTATGGATTTGAACGCTGGTGCAAACAAATTGAACGATTGTGCACATCTGCCGCACCCATACGGCTAAGCAGGTAACATCACAATTGAACGATTGCGC

>NZ_CP054139|1|1|407396-407494|CRISPRCasFinder
GCTATGGATTTGAACGCTGGTGC	AAACAAATTGAACGATTGTGCACATCTGCCGCACCCATACGGCTAAGCAGGTA
ACATCACAATTGAACGATTGCGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP054139.1\|WP_173413258.1\|400471_403030_-\|phospholipase-C,-phosphocholine-specific	unknown	unknown	gnl\|CDD\|274561
NZ_CP054139.1\|WP_173413259.1\|403031_403328_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|132407
NZ_CP054139.1\|WP_173413251.1\|394477_396250_-\|ATP-binding-cassette-domain-containing-protein	unknown	unknown	gnl\|CDD\|224055
NZ_CP054139.1\|WP_173413257.1\|399437_400397_+\|pectin-esterase	unknown	unknown	gnl\|CDD\|366462
NZ_CP054139.1\|WP_173413260.1\|403368_407328_-\|response-regulator	unknown	unknown	gnl\|CDD\|223715
NZ_CP054139.1\|WP_173417690.1\|426601_430120_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_CP054139.1\|WP_173413269.1\|430394_431612_-\|FecR-domain-containing-protein	unknown	unknown	gnl\|CDD\|226235
NZ_CP054139.1\|WP_173413255.1\|398464_398884_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|381108
NZ_CP054139.1\|WP_173413261.1\|407616_408603_+\|family-43-glycosylhydrolase	unknown	unknown	gnl\|CDD\|350105
NZ_CP054139.1\|WP_173413263.1\|413554_415276_+\|sulfatase-like-hydrolase/transferase	unknown	unknown	gnl\|CDD\|293749
NZ_CP054139.1\|WP_173413268.1\|424830_426588_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|369630
NZ_CP054139.1\|WP_173413264.1\|415309_418123_+\|family-43-glycosylhydrolase	unknown	unknown	gnl\|CDD\|350105
NZ_CP054139.1\|WP_173413266.1\|421148_423254_-\|SMP-30/gluconolactonase/LRE-family-protein	unknown	unknown	gnl\|CDD\|271323
NZ_CP054139.1\|WP_173413267.1\|423437_424517_-\|SGNH/GDSL-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|317058
NZ_CP054139.1\|WP_173413253.1\|397074_397572_-\|lipocalin-family-protein	unknown	unknown	gnl\|CDD\|381213
NZ_CP054139.1\|WP_173413254.1\|397958_398276_+\|thioredoxin	unknown	unknown	gnl\|CDD\|200072
NZ_CP054139.1\|WP_173413262.1\|408702_411723_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_CP054139.1\|WP_173413252.1\|396320_396884_-\|ribosome-recycling-factor	unknown	unknown	gnl\|CDD\|178850
NZ_CP054139.1\|WP_173413256.1\|398997_399393_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173413265.1\|420118_421051_-\|phosphodiester-glycosidase-family-protein	unknown	unknown	gnl\|CDD\|378342

Protein	Function_ID	Function_description	E-value
NZ_CP054139.1\|WP_173413258.1\|400471_403030_-\|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].	1.28276e-150
NZ_CP054139.1\|WP_173413259.1\|403031_403328_-\|hypothetical-protein	gnl\|CDD\|132407	TIGR03364, putative_secreted_oxidoreductase, FAD dependent oxidoreductase TIGR03364. This clade of FAD dependent oxidoreductases (members of the pfam01266 family) is syntenically associated with a family of proposed phosphonatase-like enzymes (TIGR03351) and is also found (less frequently) in association with phosphonate transporter components. A likely role for this enzyme involves the oxidative deamination of an aminophosphonate differring slightly from 2-aminoethylphosphonate, possibly 1-hydroxy-2-aminoethylphosphonate (see the comments for TIGR03351). Many members of the larger FAD dependent oxidoreductase family act as amino acid oxidative deaminases.	1.84146e-16
NZ_CP054139.1\|WP_173413251.1\|394477_396250_-\|ATP-binding-cassette-domain-containing-protein	gnl\|CDD\|224055	COG1132, MdlB, ABC-type multidrug transport system, ATPase and permease components [Defense mechanisms].	5.61091e-137
NZ_CP054139.1\|WP_173413257.1\|399437_400397_+\|pectin-esterase	gnl\|CDD\|366462	pfam01095, Pectinesterase, Pectinesterase.	2.28679e-83
NZ_CP054139.1\|WP_173413255.1\|398464_398884_+\|hypothetical-protein	gnl\|CDD\|381108	cd17557, REC_Rcp-like, phosphoacceptor receiver (REC) domain of cyanobacterial phytochrome response regulator Rcp and similar domains. This family is composed of response regulators (RRs) that are members of phytochrome-associated, light-sensing two-component signal transduction pathways such as Synechocystis sp. Rcp1, Tolypothrix sp. RcpA, and Agrobacterium tumefaciens bacteriophytochrome response regulator AtBRR. They are stand-alone RRs containing only a REC domain with no output/effector domain. The REC domain itself functions as an effector domain. Also included in this family us Methanosaeta harundinacea methanogenesis regulatory protein FilR2, also a stand-alone RR. REC domains function as phosphorylation-mediated switches within response regulators, but some also transfer phosphoryl groups in multistep phosphorelays.	2.44092e-10
NZ_CP054139.1\|WP_173417690.1\|426601_430120_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_CP054139.1\|WP_173413269.1\|430394_431612_-\|FecR-domain-containing-protein	gnl\|CDD\|226235	COG3712, FecR, periplasmic ferric-dicitrate binding protein FecR, regulates iron transport through sigma-19 [Inorganic ion transport and metabolism, Signal transduction mechanisms].	7.84936e-24
NZ_CP054139.1\|WP_173413260.1\|403368_407328_-\|response-regulator	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	2.6374e-41
NZ_CP054139.1\|WP_173413261.1\|407616_408603_+\|family-43-glycosylhydrolase	gnl\|CDD\|350105	cd08991, GH43_HoAraf43-like, Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (HoAraf43;Hore_20580). This glycosyl hydrolase family 43 (GH43) subgroup includes Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (EC 3.2.1.55) (HoAraf43;Hore_20580). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. This GH43_ HoAraf43-like subgroup includes enzymes that have been annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.	7.16062e-16
NZ_CP054139.1\|WP_173413263.1\|413554_415276_+\|sulfatase-like-hydrolase/transferase	gnl\|CDD\|293749	cd16025, PAS_like, Bacterial Arylsulfatase of Pseudomonas aeruginosa and related proteins. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. The sulfatases are essential for human metabolism. At least eight human monogenic diseases are caused by the deficiency of individual sulfatases.	0
NZ_CP054139.1\|WP_173413268.1\|424830_426588_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|369630	pfam07980, SusD_RagB, SusD family. This domain is found in bacterial cell surface proteins such SusD and SusD-like proteins, as as well RagB, outer membrane surface receptor antigen. Bacteroidetes, one of the two dominant bacterial phyla in the human gut, are Gram-negative saccharolytic microorganisms that utilize a diverse array of glycans. Hence, they express starch-utilization system (Sus) for glycan uptake. SusD has 551 amino acids, and is almost entirely alpha-helical, with 22 alpha-helices, eight of which form 4 tetra-trico peptide repeats (TPRs: helix-turn-helix motifs involved in protein-protein interactions). The four TPRs pack together to create a right-handed super-helix. This is predicted to mediate the formation of SusD and SusC porin complex at the cell surface. The interaction between SusC and TPR1/TPR2 region of SusD is predicted to be of functional importance since it allows SusD to be in position for oligosaccharide capture from other Sus lipoproteins and delivery of these glycans to the SusC porin. The non-TPR containing portion of SusD is where starch binding occurs. The binding site is a shallow surface cavity located on top of TPR1. SusD homologs such as SusD-like proteins have a critical role in carbohydrate acquisition. Both SusD and its homologs, contain about 15-20 residues at the N-terminus that might be a flexible linker region, anchoring the protein to the membrane and the glycan-binding domain. Other homologs to SusD have been examined in Porphyromonas gingivalis such as RagB, an immunodominant outer-membrane surface receptor antigen. Structural characterization of RagB shows substantial similarity with Bacteroides thetaiotaomicron SusD (i.e alpha-helices and TPR regions). Based on this structural similarity, functional studies suggest that, RagB binding of glycans occurs at pockets on the molecular surface that are distinct from those of SusD.	2.2073e-41
NZ_CP054139.1\|WP_173413264.1\|415309_418123_+\|family-43-glycosylhydrolase	gnl\|CDD\|350105	cd08991, GH43_HoAraf43-like, Glycosyl hydrolase family 43 protein such as Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (HoAraf43;Hore_20580). This glycosyl hydrolase family 43 (GH43) subgroup includes Halothermothrix orenii H 168 alpha-L-arabinofuranosidase (EC 3.2.1.55) (HoAraf43;Hore_20580). It belongs to the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. This GH43_ HoAraf43-like subgroup includes enzymes that have been annotated as having xylan-digesting beta-xylosidase (EC 3.2.1.37) and xylanase (endo-alpha-L-arabinanase, EC 3.2.1.8) activities. GH43 are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many GH43 enzymes display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.	1.4259e-40
NZ_CP054139.1\|WP_173413266.1\|421148_423254_-\|SMP-30/gluconolactonase/LRE-family-protein	gnl\|CDD\|271323	cd14953, NHL_like_1, Uncharacterized NHL-repeat domain in bacterial proteins. This bacterial family of NHL-repeat domains is found in a variety of domain architectures. 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.	4.65083e-111
NZ_CP054139.1\|WP_173413267.1\|423437_424517_-\|SGNH/GDSL-hydrolase-family-protein	gnl\|CDD\|317058	pfam14606, Lipase_GDSL_3, GDSL-like Lipase/Acylhydrolase family.	1.04666e-75
NZ_CP054139.1\|WP_173413253.1\|397074_397572_-\|lipocalin-family-protein	gnl\|CDD\|381213	cd19438, lipocalin_Blc-like, bacterial lipocalin Blc, Arabidopsis thaliana temperature-induced lipocalin-1, and similar proteins. Escherichia coli bacterial lipocalin (Blc, also known as YjeL) is an outer membrane lipoprotein involved in the storage or transport of lipids necessary for membrane maintenance under stressful conditions. Blc has a binding preference for lysophospholipids. This group includes eukaryotic lipocalins such as Arabidopsis thaliana temperature-induced lipocalin-1 (TIL) which is involved in thermotolerance, oxidative, salt, drought and high light stress tolerance, and is needed for seed longevity by ensuring polyunsaturated lipids integrity. This group belongs to the lipocalin/cytosolic fatty-acid binding protein family which have a large beta-barrel ligand-binding cavity. Lipocalins are mainly low molecular weight extracellular proteins that bind principally small hydrophobic ligands, and form covalent or non-covalent complexes with soluble macromolecules, as well as membrane bound-receptors. They participate in processes such as ligand transport, modulation of cell growth and metabolism, regulation of immune response, smell reception, tissue development and animal behavior. Cytosolic fatty-acid binding proteins, also bind hydrophobic ligands in a non-covalent, reversible manner, and have been implicated in intracellular uptake, transport and storage of hydrophobic ligands, regulation of lipid metabolism and sequestration of excess toxic fatty acids, as well as in signaling, gene expression, inflammation, cell growth and proliferation, and cancer development.	3.34336e-42
NZ_CP054139.1\|WP_173413254.1\|397958_398276_+\|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].	1.80187e-48
NZ_CP054139.1\|WP_173413262.1\|408702_411723_+\|SusC/RagA-family-TonB-linked-outer-membrane-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_CP054139.1\|WP_173413252.1\|396320_396884_-\|ribosome-recycling-factor	gnl\|CDD\|178850	PRK00083, frr, ribosome recycling factor; Reviewed.	1.57739e-99
NZ_CP054139.1\|WP_173413265.1\|420118_421051_-\|phosphodiester-glycosidase-family-protein	gnl\|CDD\|378342	pfam09992, NAGPA, Phosphodiester glycosidase. This is a family conserved from bacteria to humans. The structure of a member from Bacteroides has been crystallized and modelled onto the luminal region of the human member of the family, the transmembrane glycoprotein N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase. There is some conservation of potentially functional residues, implying that in the bacterial members this family acts in some way as a phosphodiester glycosidase. The human protein is also present, so the eukaryotic members are likely to be catalyzing the second step in the formation of the mannose 6-phosphate targeting signal on lysosomal enzyme oligosaccharides.	7.88403e-41

>NZ_CP054139.1|WP_173413260.1|403368_407328_-|response-regulator
MKRITIFLFLLSLAPVFSIAQPYYFRHYQVEDGLPYNSVLCSLQDKQGFMWFGTRDGLCRFDGYLFKSYKYTPGNKFSLGNNYVYNLTQDDPYKLWIGTKNGLYRFDMKLERFELETRTAGKIIDGIVIDEKHNVWFIASGKLYCITHDGHFQTIEIANAQRLTAIARGSVNELWLATESGYVVRFASDTWSFKYYDVFANTPAITARRIEKIWKDGAGHLYIGTSNHGVKLLNIADITYKDILTFDEDHTEIMARAFCPDGNGHIWIGTESGIYIYDTTTGSIRNLRKNFYDPYSLSDNAVYTITKDSEKGMWISTYFGGVNYYSATGAQFEKFFPKDTPGSLHGNLVREFCQDTNGYLWVGTEDAGLNRLNLRDNTFTHVGFTGKPGSISYNNIHGLLSVGKELWVGTYQHGLDILDINSLKVIRHYGFGPGEHDLKTNFVNVLFKTRSGQIYLGTQLGLYRYNQTGDNFTHVNELGVCYVSSIIEDHSGKIWVGTFGNGVYTLSPQNEYWTHFEHQPDVQGTLTSNVVTDVYEDSSQRIWLCTENGGLCQYNIKQAGFTKYKLPAEFNDKYLFNVIEDNKRRLWVTSSGGLICMEPAQGNVHAFTKGDGLLNDQFNYRSAFKDSQGRLYFGSSKGFIRHWQQAPVNAQTRAQLYITGLQADHQTTDDTDDGQIQLPYAGHVTLGPGKTTFSIDFSALSYASPGTAIYSYKIDGLDKNWITLPANRRVYYTQVAPGDYVFKVRASVGDNGVQTPVRTLKISITPPFYAGLPATIFYMILVCVAIYFVYKLLHDRSEEKNRRKIAYLETQKEREIYQAKIDFFTHVTHEIRTPLSLIKAPLEKVMQADDIGTAKNDLMLVNRNTDRLLDLVDQLLSFRRTEIDGYSLNFNRTNISALLINLCALFREQAQQAKLDLQIDVTDSQLIAYIDHDAFNKILSNLLSNAIKYADSRMIVRLLKENEDEFCIIVKNDGPVLSPDTARKIFEPFVRGEQHSHKPGTGIGLPLAKALVDLHQGKLEYLAEQDQLNTFKLVIPLHQAVEMNIGPDNSGETSTATAPEIETEPTKPVVLIVEDQPDFREFIQSLLSEAYSVLTAGDAAHAKEILIKHSVQLIISDVMMPGIDGFEFCRQLKSDINFSHIPFILLTAKNNFASKIEGLDCGSDAFIEKPFSPRHLKMQIVNLLKNRDIVKEHYAHSPVANLKTMAHSKADSEFLHKLDTLIKVNLTKQDFDVEELAEQMNLSRPTLYRKVKAITDLSPAELVTVTRLKQAAEMLTTGDYKIYEIAEEVGFTSSAVLSRAFQKQFGVSPSVYISKTLKS
>NZ_CP054139.1|WP_173413259.1|403031_403328_-|hypothetical-protein
MQKQVDTPRLFHISEEPGIYMGRSAIIIIDYLRTFVNFKNWELLQSWHGIYPKMTNGETELIMNIEPGVTVINGVGGNGMTLSFGLCKQLMPGNFDKN
>NZ_CP054139.1|WP_173413258.1|400471_403030_-|phospholipase-C,-phosphocholine-specific
MDNRRDFLKKAALLAGAASLPGLIPESIQKAMAINAAPGSTYLDAEHIVILMQENRSFDHCYGSLKGVRGFNDPKAIDLPNKNKVWLQSNAAGKTYTPFRLDIKGTKATWMHSLPHSWQNQVDARNDGRYDQWLNVKRSGTKAYADMPLTMGYHTREDIPFYYALADAFTVCDQNFCSSLTGTNPNRLHFWTGTIRAEQNENSRAHVWNDDMDYGTLNWTTFPERLEERGVSWKCYQNEVAIDTGFKGEEDAWLSNFQDNPLEFFGQYHIHLYDLHVRALEKGAADLKESIPQLQKQMADLPAGDAKTQELKAKLAKMQAEATSVNTQLENIRKKPFDSLTEQQKSLHRKAFDTNRNAPDHRELVDLEYDDNGTKRMLKIPKGDVLHQFRADVDSGKLPTVSWISAPENFSDHPTSAWFGAWYVSEVIDILTKNPEVWKKTIFILAYDENDGYFDHVPPFVAPHSHKAGTGKVTPGMDTRVEFVTLEQEQARKGFPEKYDRESPIGLGFRVPLVIASPWSKGGWVNSEVFDHTSTLQFLEKFISHKTGKPIKETNISDWRRTICGDLTSVFRSGDAAPLHSPAPVPRKEFLAGIHQAKFKKLPDNYHELTTDEITTFNSTPHASPYMPKQEAGIKPSCSIPYQLQVDGRLSADKKSFEIKFDNKNEVFGKATAGAPFNVYAPGNYMQMGKDQLAPLRTWAYGLKPGTDLADQWPLHEFEHDNYHLRVYGPNGFYREFMGNAEDPQLAITLEYQRSRLNKNTLTGNVSLRLNNLSGKDYTVEINHHGYHNNNIKQVVKGKTQGEPLIIDLQKNHGWYDFSVKVNGHNSFAVRYAGRVETGKSSFTDPVMGGVV
>NZ_CP054139.1|WP_173413257.1|399437_400397_+|pectin-esterase
MKKTLIPLLLCACAINTIAQKKIIVSPDGSGNYKTVQEAFNAVPLNNKKPVIIFVKNGTYREKLHLDSTKNFVELIGESRFNTTLIYDDHTGKTAPDGKVISTPTSYSFLIKADNFKAHDITFTNDAGFTAGQAVAVECQGDKAVFYNCRFTGNQDILFLNSAKSRQYYKDCYIEGTTDFIFGAATAWFENCHIHSKKNSHVTAASTPQDHLYGFVFNDCTLTGDSTLHMVSLGRPWRPYAWVVYMHCYIGQQIKAEGWSNWNQTESYKTARYAEFENYGPGASAKGRVNWARQLTATDAAKITLANVFPGWDPLAELR
>NZ_CP054139.1|WP_173413256.1|398997_399393_+|hypothetical-protein
MSQPVHPDYIKASNLILITLVLSVISSFFTPNIGIVTPLMKIGVVILSIIINGLIAYFIRRGSETVKYILLILLLFGLASIPMMISLFKTRPVSSIISLVLMAIQVWVIVILFKIPKHNISYKPERGPDAV
>NZ_CP054139.1|WP_173413255.1|398464_398884_+|hypothetical-protein
MKDLNIMMIDDNPIDHLIVQRICEKESLFGRIKHYYHPAEPLELLKTIGNNIAQLPDIILLDLHIPIISGWEMLDHFADIQRIAGKRIDVHVLSDSLDHADRIRSQSYSFVRNFFVKPLTSLALREMHQYYAQFAVLPV
>NZ_CP054139.1|WP_173413254.1|397958_398276_+|thioredoxin
MALEITDANFEELVLKSDKPVLVDFWAEWCGPCRMVGPVVEEIAKEYDGKAVVGKVNVDNNPGISMKFGIRNIPALLFFKNGEIVDKQIGAVPKSVLADKLVKQL
>NZ_CP054139.1|WP_173413253.1|397074_397572_-|lipocalin-family-protein
MKAICTLLIFFYTALAAPVNKPVDKVDLSRFAGKWYSLYSIPTIYDKGSRETTTTYTLNKDGYYNVFTACKKGDDDKIYTSKLFPEKDGDGEMKAQFLWPFKVDYWVIELDDDYQYVVVGHPEHKFLFIMSRKPFIDKKLYDEIVTRCKAKGYAVDKLTSQQHHG
>NZ_CP054139.1|WP_173413252.1|396320_396884_-|ribosome-recycling-factor
MSELIKKQLTDAKSLMEKAVDHCDNELGKIRAGKANPAMLDGIVVDYYGSPTPLSQVGSVNTPDAKTIVIQPWEKSLLGPIEKAIMEANLGVNPQNDGVIIRINVPPLTEERRRDLVKKAKSEGENGKVTVRNIRKDINDKIRKLKAEGVSEDEMKTGEAEVQKLVDAYITKVDQLIAAKEKDIMTV
>NZ_CP054139.1|WP_173413251.1|394477_396250_-|ATP-binding-cassette-domain-containing-protein
MKLLLSYLKEHRWLVALALVLAAFNIGFSLLDPMITGNIVDNYMIPKNGKNLSYDYRLHGALKWIGLAIGAAMVSRIAKNFQDYFTNIIIQKTGAKMYADGLKHSLELPYQVFEDQRSGETLGILQKVRTDSEKFITSFINTLFISLVGMLFVIFYSISVNYKVTLVYFAALPVIGFVSSALSKRIKNIQRTIVAETTSLAGSTTESLRNIELIKSLGLVKQEIERLNKTTYKILNLELKKVKYVRSMSFIQGTTVNFVRSCMVLVLLILIFKGSLTPGNYFKFLFYSFFLFNPLQELGNVIQSWREAQVSLGNFEAILNTPIDKKPAKPVLIEQVKTLTFNNVSFKHLTANRNALNHINFQVNSGETIAFVGPSGSGKTTLVKLLVGLYQPLEGDISYNKVQSSEIDLDQLREKIGFVTQDTQLFSGTIRENLLFVRPEATDEECMNVLHRAACQSLLARADKGLDTMIGEGGVKVSGGEKQRLSIARALLRRPDILVFDEATSSLDSITEEEITETIKDVSDQTDHITILIAHRLSTIMHADNIYVLEKGHIIESGKHTDLIQQKGLYYAMWRQQIGEKMTPEVAELP
>NZ_CP054139.1|WP_173413261.1|407616_408603_+|family-43-glycosylhydrolase
MMTKFTWLILFCCIPFCLLAQEKPKMYYTDTSSTGIKIAKDPVVVKFKGWYWMYYSKQAFQNTADGMQGWNIGIAQSRDLYHWKKVAEIKPDAAYEQHGLCAPGATVRGGKIHLFYQTYGNGPKDAICHAWSADGINFTRDATNPVFSPKGEWTNGRAIDAEVYHYNNQYFLFFATRDKAGEIQKQGVATASNNTNFSRGEWKQATDDAILAPQLPWEGKCIEGASIIKRNNKLYMFYAGSYNNMPQQIGVAESADGIHWRRVSDKPFLANGKPGSWNYSESGHPGIFEDDDGQTYLFFQGNNNHGKSWYLSNVKIGWNSEGPYLMPE
>NZ_CP054139.1|WP_173413262.1|408702_411723_+|SusC/RagA-family-TonB-linked-outer-membrane-protein
MRYKPLLVKMMATAVLLLIAISFTEHVLAQTAKAPVTITGKIVDEQTGETLPGVTVKVKNTTRMTSTNLAGVYSIAINNPQEVLVFTFVGYEPQERAAGSLKTINISLKPTASNLNEVVVVGYGTQKKQFLTGSVARANLEAFHDAPDANFVQMLQGTVVGLNIGQVNVAGQTPAIQVRGASTLNGNTTVLIILDGIQYNGDLQSINPDDIATIDVLKDASATAVYGAQAANGVILITTKKGKQGKTRVTASSSYATQTPTQNLKPLDPDAYQEHVRMLYYQQAYLAPDYTTPDPTFNLNLHLDAASRANAAAGNSYDWWGNSTHLGHMYDNKVSISGGTDQINYLMSYNNTNQQGFIVNDLFKRQSVRVNLETKIAPWWTAGVQSFATFVNKDGAEPTLADIIRFSPFVVPFNASGDLLQNPDNTVGLNPFLSQYVDDIERNDYFFANFYTDIKFPFMKGLSYRINYGNNYRDTKQYRSSKYAQNGLGEAYKNNTFYNDYTLDNILTYQRDFGKHSIETTLLYGSIERKNQNTNADARQFTQLTLGYDGIQQGAIQLVSSSAYKEALAYQMGRVNYKYDNKYLLTGTVRRDGFSGFAQNNKWGIFPSLSAGWIVTNEKFLKLPWLNYLKLRGGYGISGNQTNRYASLSTVSSSAAYVFGDVSTPAFGQQQTAIGNSNLRWEKTTGKSLGIDFEVLHSRLTGSVDMYDNITTDLLYNVAIPYATGYSIIATNIGKLQNRGLEISLTSKNISSKDFDWTSTVNFSTNSNKILSLLGQDNNHDGVEDDLIASNLFINRSIGTVYGYQTAGIYQLADKDIRTGYFPGNYRIVDQNGDNLITPTDDRVVLGRTEPAYRVSLLNTLRYSNFTLTFFLNSIQGGKNGYLGASSVPLVLNDNTVRWNYLSALNYWQPNNPGGTQPFSVTAPAIAPTIYSDRSFVRLQDVTLSYRVPKKLTDKLHLQNLSVFASGKNLATWTKWKGWDPETNQALIPDGRPVLKGASFGLNVSF
>NZ_CP054139.1|WP_173413263.1|413554_415276_+|sulfatase-like-hydrolase/transferase
MLKLSTLKKGCVALSIVTLAFNASAQNKENRRPNIVLIMADDMGYSDIGCYGGEIKTPNIDNLAKNGLRFSQFYNTSRCCPTRASLLTGLYSHQAGIGDMTFDQKQPGYRGYLTENTVTIAEVLKKAGYQTGMVGKWHVSNTFLGQKDEHLKWLNHQSYKPFFSPVEQYPVNRGFEKYYGTIWGVNDYFDPFSLVNGTEPVKTVPKDFYYTDAINDTASAYIKQFSKTGKPFFLYVANTAPHWPLHALPEDIKKYEDTYKAGWDAIREARYKKLIAEGVFPADKNILSKRWKPNRKWEDNPTKDWDAHTMAVRAAMIDRMDQGIGRIIKTLKETGQLDNTLIIFLSDNGASSDDAQKYLPGNDRPGETRTGQKIIYPANKDVNAGPETTFASADEMWSNVANVPFRYWKTEPFEGGICTPMIAYWPAGLKTPKGSVTTQMGHVMDFMATFAELAGTTYPTEFEGRKITPTSGISLVPILKGKKRQGHDYLFFEHIGRRAVIHGDWKLLALNNAPWELYNLKEDRSEMHDLITEHPDIAENLTKAWQEWANSHNVLPKPVKAEANKQPADMSND
>NZ_CP054139.1|WP_173413264.1|415309_418123_+|family-43-glycosylhydrolase
MTFLNTIRLTALINILLFTANALFAQNNPVIDNVPDVGVINFNGKYYLAGVNTNGGFYISDDLVHWKGPEHVFTMANDWTKGKPFGDNQIHAADIRYINGRFHFYWSVNYWGGQNTTVQIGHAVADNIMGPYIEPDKKNWFDERIDPHLLVDSDSSLYFYTVKFTDGNTIWGQQMRDPWTHRGSPKLLFNSLPLTWERMDNSVTEGPEVIKYRSRYYLMYNANHTGNTYGNYALGVAEADEPLGFNSANKYPHPVVQQNLTDDPSKQRRVFSSSLDGFTNWKYTFNQPGESWNTPAFTDTEWKKGDKGFGNQVLKGSTRINPQTMWRTNDIWVRKHFKIPWALSGQLQLMVNHTGPTEVFMDGQLIYNGVAANYTTVNLLPQLVNELKTGEHVLVIHGEKAERGANIDVDLIENLASPGDDILYNPGQPNLLKGPNGFEWWLVYFAIKNGGKKGQFINRVLFNDHELTVDGPTSNKTTGYHPDPALPIFGDSFEDENIKDRWSLQSGKWRVRNGELMQEGNTGKSLALIKSRASSNYLFKIGVNPTTLKTANAGIIAYYTDALNFLEIGIDQAKGAWYSRLVRDGKEIIVINKLSPVFNFNVYHSLSVYKNGNTVEFQIDDQPAPGKHQIITLFDEPGLPGIFTQATTATFDGAIYTPGWDEYNAGITGWGNAVNRKQATGEWGVTEKGITINKTQGESTVYKGDLLNSYEFATQIYSNGAGTAGIFPVYTDENNYVKAAIDFQHNSLIVSGKLNGAAIPGKTILLKRKMVRYPDQRYSDHSNKVYTLKANTSISNIEIVKFPVDNKQLLTINLFDSLKVEYHHHDEWRPLNFEKIPTGIQAVDQIKFPLITADALRIRSSGFNTRMPAVYKIYTDEDGTSDYNLRAVKLKDKLLLFLDNGLIADIDGTWPPSQVGLFGTDAGACFNGLMLFEKRDN
>NZ_CP054139.1|WP_173413265.1|420118_421051_-|phosphodiester-glycosidase-family-protein
MKKYYLLLSALLFSIHLFAQTDSANLAHAQWKLKKINAKVYWKTTHLTNHSLFGANENINVIIIPAHTKSVRLVVGYSDSLETTSQQAMRNNALAGINGSFFKMRGADPDDHPELNHVPKLEPSKLPYNRAGTYLRKDGQLIAPNKIAAKQTTRRRPQLGVLALSDNGAAILKPDTLNFEWENTLAARDIMTSGPLLMLNGKNMAISTDDFSQKRHPRTAVGKLADGSTMLLVVDGRFEESAGMSLIELQQTMRWLGCVTALNLDGGGSSAMYIKGQPEHGIVNYPSDNKKFDHAGEREVANTVLIVPVH
>NZ_CP054139.1|WP_173413266.1|421148_423254_-|SMP-30/gluconolactonase/LRE-family-protein
MKNFIFLGIALAMCMFSCKKNQVADENGNTAAITGGGLKLKDMGIVASNDSAFTISTYAGNGTAAFSNGTSGNLLTASFDSPEGIVFDSGGNMFVADRDNQIIRKITTGGVISTFAGQQGVAGFADGTGTAAKFSTPIRLSIDAANNIYVADRDNAKIRKITSAGVVTTIAGSTAGSGATQFNWPVDVAVKSDGSILYVADSKNHRIQKITLSGGTYTTSLLAGQTTLGYANGTGSAAKFNFPAGVAIDASGNIIVADRMNNCIRKITSGGVVSLLAGIPGTVYDLDAPALQASFGEPYGVTVANDGCIYVCDINYHNVRRISNHGGFVATVAGYSTSGYADGTFNTRFNVPTSVAIDNSGNFYVTDVSNNRIRKMKPETRVIQYTEGWTPMDTSTYAGVKRYRYTGNRFWLPSTASNPIQNINIIDIDMSVNHFEFMHVDSFANQTTVSNIIGHPTSVIAALSGTFATGNHHGKFASYLRNNDVTYWKADAEEALYPDGYWHYHDGMFYVDATGTPGMEQSNMTQLPFSPTTRKYMMSGAPLLIKNSVPIEITSPTNWGVSNTTPPQTLRVIIAPRAIVALPIINKHVLLICIDGVENGIDCYASNGISAPGRYGMTTADATQFVQQFFHPSWAINMDGGGSASMYMMGATDGQTGGVSGGIPVISYPDWDSSCTISGMDYSRYGQQRKSMQDCIAVIAN
>NZ_CP054139.1|WP_173413267.1|423437_424517_-|SGNH/GDSL-hydrolase-family-protein
MKTLFKTVFVAIVFHYQVYAQVPKPVYTKATDLTIAGDIMPTQNPYHRVDTVKYPAMPAVVKRLLTQSAGKVICFTTNSKQLTAKWCSSGSKPYPNLTPIANKGLDLYIKKDGKWQFAGVGRPDGQCTEATLVSNMADGEKECLLYLPIYDEVGNVEIGTDAGASIKPIPFPFQKRVLVYGSSITQGASASRSGLAYPARLSRLTGLNFMNLGLSGSAKMEPAVIAMINDIQADAYVLDCIPNSSDVVVKERALNMINSIRAAHPGKPIIMVNSITREAGYIDTKVGNMVNAQNAAIDSIAKNLVKQHTKDFYYIDTKGFLGDDHEGSTDGIHPNDLGSYRFVEKIEPMIADILKKYFK
>NZ_CP054139.1|WP_173413268.1|424830_426588_-|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKKIYIALIGLVTLGAMGCKKNYLDVTPPDKIDAQVFFNNATDLQVYTNGFYDQVPVTSGLTYTVYTDDASSDNILPLQIVDRVKGARVVPVARGTGGWSFSSLRSINYFLANYGKCPDAAAKQKYGGIARYFRAYFYYDKVKTFGDVPLYTKVLTADDPDLYKPRDSRTVVMDTVLADINYAIANIPKTVALNNITGYTALALKARICLYEGTWRKYHGIANYQSMLNEAVSAADALISSGAYKLYTTGGANTAYRDLFARVDQDVTETILARDYSKLVQVNGVDYFMTSATGGAYGIPKDMINSYLMKDGTRFTDIPNYQTKQFYDEMQNRDPRLTQTTAGPDFAAYLETAREPVNLSITTTGYRVIKALSTRDQWVSNGGYSDFILFRYAEALLVYAEAKAELGTLTQADLDRSVNLLRARAGMPNMNMAAANATPDPFLLAQYPNVEKGANKGVILEIRRERRIEMFNEGLRWDDLMRWKEGKKLEQPMVGIYFPSLGSFDFNNDGKTDVYLHNGNASGAPAGTSSVVNVTQKALTNGTSGNFFPLKGITITFDENKDYLYPIPSEDITLNPKITQNPGWK
>NZ_CP054139.1|WP_173417690.1|426601_430120_-|SusC/RagA-family-TonB-linked-outer-membrane-protein
MKLTTLLLLITLVQVSAKSFGQRITLNENNVSLKRVIQDIEHQSGYVFFYDSKDVKQKVNVHISDASIEDVLAECLKNLPLSYKIADKTILLQQKNLPTAIAEAPPVPITVKGKITDNKGVPLIGATVSAKKANKAVVADVNGMFEIKDINSDEILIFSYTGYVTKQIPANDPGIANVVLEEDVKAMNEVVVVGYGTQKKENLTGAVSQISSTDIGYHATPNIANSLQGLLPGLNIQANTGNPGDKPDINIRGFNSVNGGSPLILIDGIQGDIDRVNPLDVETVSVLKDAASAAIYGARGSFGVILITTKKGKAGNTVVNYTNNIGRTTPIVRTDYISDPYEYGKIVDAFLSGYNGTTYTNYTDADYAKERQVADGTLAPFNEKQADGTYKFFGKTNWYDLLFRKWAPSQTHNLSISGGNDKLQGYLSGRSYNTGTIQAGVDASLIKYNIKGNLNFKANKWLDISDNIQVSTADMTEYGGSKAGYVTNGSGIYNGNTYYFLFPFMPSSIDGVPYDYNGYGEIAALGDKSSFQKTYSEQFVNTLSARLHPVKDLVVNIDYANTVNHVAVTTRENPITYLTTLKANLQTVGLNTLTEARNRNYYNALNVYGTYNKNLFNDTHHFKLLLGYNQEDFSSDNISAQQGNLLVSNLSSLNLGTNLIAANGSGSLWAIRGYFGRLNYDYKNKYLLEVNGRYDGSSRFPVTSRYGFFPSVSAGWYLSREDFFKPLEKTISSLKLRSSYGQLGNQNIDLYTFSQILSTGQTIWASNAVRFNYVGAPAPLPSVVTWENSKTIDVGADLGLFNDKFNVSFDWYEKNVSGMYVPGQPLPSVFGAPEPRENIASLRDRGFELQVSYNAGFDIAGSPFRLKSTISLYNFTGVITKYPNASGLMSAFYEGQKLGDIYGYHIDGQFQSDAEAAAYQAKFVNPATSLGQVYNYEINIVQNAQWKGLHAGDIKYVDVNGDGAINKGKNTLADHGDLVKIGNTMPKFPFGFNFAADWKNFDLMVAGTGVMHQDWYPTGDIYWGPYERPYLSFIRKDLIQNAWTPETPTNTYPQAVRGYASLGALRSLGEINDYYLTNVGYLRVKNLTLGYTLPVKLTQKVGIQKLRFYVSGENLFTWSFGHLTKYIDPETAGSGIDYSTPMNVSTSSSSIARAGESYPLGKVYSLGLSITL
>NZ_CP054139.1|WP_173413269.1|430394_431612_-|FecR-domain-containing-protein
MENHQLKEIFSRYLENRCTAGEVETLIGYFNTDNEAYLRLLIEQELESPEPDLNDEHLYTLTAEAFENIRQQIGKNNKPAEIRHINIPNHKKQRLWPRIAVAASLLLILSVTAYFITHQQQPNSKPNLVAKRLPQHDIAPGGNKAVLILANGQQINLTNAKNGRLAKEANMLINKTADGKVVYQSDKQNKAATELAYNTLKTPRGGKYDLTLADGTRVWLNAASSITYPSAFNGPDRQVEITGEAYFEVVHNAAKPFRVKVAGQTIEDLGTHFNINAYADEPAIKTTLLEGSIRVSNSTGNLVLKPGQQAVIKADQNITIDAGADMEEAIAWHQGLFKFNEASTEMVMRQLSRWYDVDVSYEGKIPPRQFSGKIYRNASALKVSDILSYKQIHFRLEGRKIIVMP

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Crispr_ID: NZ_CP054139_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP054139_2

664163-664265

Orphan

Consensus_repeat	Method
CTGCACATCTGCACATTAAAAAG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP054139_2

>merge|NZ_CP054139|2|664163-664265|CRISPRCasFinder
CTGCATATCTGCACATCTGCAAATTAAAAAAACCAGCATTTGAACATCTGTGTAATAAGCAAATCAAAACATTTGCACATCTGCACACCTGCACATCTGCACA

>NZ_CP054139|2|2|664163-664265|CRISPRCasFinder
CTGCATATCTGCACATCTGCAAA	TTAAAAAAACCAGCATTTGAACATCTGTGTAATAAGCAAATCAAAACATTTGCACAT
CTGCACACCTGCACATCTGCACA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP054139.1\|WP_173413470.1\|675448_676705_+\|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme	unknown	unknown	gnl\|CDD\|99747
NZ_CP054139.1\|WP_173413467.1\|671175_672078_+\|cell-division-protein-FtsQ	unknown	unknown	gnl\|CDD\|224505
NZ_CP054139.1\|WP_173413459.1\|659670_660075_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173413469.1\|673652_675302_+\|cell-division-protein-FtsZ	unknown	unknown	gnl\|CDD\|236468
NZ_CP054139.1\|WP_173413452.1\|651651_652293_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173413460.1\|660071_662204_+\|PASTA-domain-containing-protein	unknown	unknown	gnl\|CDD\|223839
NZ_CP054139.1\|WP_173413458.1\|658771_659674_+\|16S-rRNA-(cytosine(1402)-N(4))-methyltransferase-RsmH	unknown	unknown	gnl\|CDD\|234597
NZ_CP054139.1\|WP_173413466.1\|669824_671183_+\|UDP-N-acetylmuramate--L-alanine-ligase	unknown	unknown	gnl\|CDD\|234757
NZ_CP054139.1\|WP_173413453.1\|652382_654275_+\|RecQ-family-ATP-dependent-DNA-helicase	unknown	unknown	gnl\|CDD\|223588
NZ_CP054139.1\|WP_173413457.1\|658302_658779_+\|division/cell-wall-cluster-transcriptional-repressor-MraZ	unknown	unknown	gnl\|CDD\|224912
NZ_CP054139.1\|WP_173413454.1\|654381_654894_+\|fasciclin-domain-containing-protein	unknown	unknown	gnl\|CDD\|367095
NZ_CP054139.1\|WP_173413461.1\|662200_663664_+\|UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,-6-diaminopimelate-ligase	unknown	unknown	gnl\|CDD\|234660
NZ_CP054139.1\|WP_173413456.1\|657236_657839_+\|DUF2807-domain-containing-protein	unknown	unknown	gnl\|CDD\|371327
NZ_CP054139.1\|WP_173413465.1\|668548_669643_+\|undecaprenyldiphospho-muramoylpentapeptide-beta-N-acetylglucosaminyltransferase	unknown	unknown	gnl\|CDD\|234825
NZ_CP054139.1\|WP_173413463.1\|665723_667067_+\|UDP-N-acetylmuramoyl-L-alanine--D-glutamate-ligase	unknown	unknown	gnl\|CDD\|223842
NZ_CP054139.1\|WP_173413464.1\|667221_668415_+\|FtsW/RodA/SpoVE-family-cell-cycle-protein	unknown	unknown	gnl\|CDD\|274232
NZ_CP054139.1\|WP_173413468.1\|672084_673434_+\|cell-division-protein-FtsA	unknown	unknown	gnl\|CDD\|273483
NZ_CP054139.1\|WP_173413471.1\|677036_678320_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173413462.1\|664358_665600_+\|phospho-N-acetylmuramoyl-pentapeptide--transferase	unknown	unknown	gnl\|CDD\|234638
NZ_CP054139.1\|WP_173413455.1\|654972_656694_-\|M28-family-peptidase	unknown	unknown	gnl\|CDD\|349895

Protein	Function_ID	Function_description	E-value
NZ_CP054139.1\|WP_173413470.1\|675448_676705_+\|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme	gnl\|CDD\|99747	cd06454, KBL_like, KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.	5.32124e-106
NZ_CP054139.1\|WP_173413467.1\|671175_672078_+\|cell-division-protein-FtsQ	gnl\|CDD\|224505	COG1589, FtsQ, Cell division septal protein [Cell envelope biogenesis, outer membrane].	0.00150026
NZ_CP054139.1\|WP_173413468.1\|672084_673434_+\|cell-division-protein-FtsA	gnl\|CDD\|273483	TIGR01174, Cell_division_protein_FtsA, cell division protein FtsA. This bacterial cell division protein interacts with FtsZ, the bacterial homolog of tubulin. It is an ATP-binding protein and shows structural similarities to actin and heat shock cognate protein 70. [Cellular processes, Cell division].	3.32965e-119
NZ_CP054139.1\|WP_173413469.1\|673652_675302_+\|cell-division-protein-FtsZ	gnl\|CDD\|236468	PRK09330, PRK09330, cell division protein FtsZ; Validated.	2.43738e-165
NZ_CP054139.1\|WP_173413460.1\|660071_662204_+\|PASTA-domain-containing-protein	gnl\|CDD\|223839	COG0768, FtsI, Cell division protein FtsI/penicillin-binding protein 2 [Cell envelope biogenesis, outer membrane].	1.31583e-88
NZ_CP054139.1\|WP_173413458.1\|658771_659674_+\|16S-rRNA-(cytosine(1402)-N(4))-methyltransferase-RsmH	gnl\|CDD\|234597	PRK00050, PRK00050, 16S rRNA (cytosine(1402)-N(4))-methyltransferase RsmH.	1.04436e-149
NZ_CP054139.1\|WP_173413466.1\|669824_671183_+\|UDP-N-acetylmuramate--L-alanine-ligase	gnl\|CDD\|234757	PRK00421, murC, UDP-N-acetylmuramate--L-alanine ligase; Provisional.	0
NZ_CP054139.1\|WP_173413453.1\|652382_654275_+\|RecQ-family-ATP-dependent-DNA-helicase	gnl\|CDD\|223588	COG0514, RecQ, Superfamily II DNA helicase [DNA replication, recombination, and repair].	3.6772e-148
NZ_CP054139.1\|WP_173413457.1\|658302_658779_+\|division/cell-wall-cluster-transcriptional-repressor-MraZ	gnl\|CDD\|224912	COG2001, COG2001, Uncharacterized protein conserved in bacteria [Function unknown].	3.95914e-32
NZ_CP054139.1\|WP_173413454.1\|654381_654894_+\|fasciclin-domain-containing-protein	gnl\|CDD\|367095	pfam02469, Fasciclin, Fasciclin domain. This extracellular domain is found repeated four times in grasshopper fasciclin I as well as in proteins from mammals, sea urchins, plants, yeast and bacteria.	1.95701e-22
NZ_CP054139.1\|WP_173413461.1\|662200_663664_+\|UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,-6-diaminopimelate-ligase	gnl\|CDD\|234660	PRK00139, murE, UDP-N-acetylmuramoylalanyl-D-glutamate--2,6-diaminopimelate ligase; Provisional.	0
NZ_CP054139.1\|WP_173413456.1\|657236_657839_+\|DUF2807-domain-containing-protein	gnl\|CDD\|371327	pfam10988, DUF2807, Putative auto-transporter adhesin, head GIN domain. This bacterial family of proteins shows structural similarity to other pectin lyase families. Although structures from this family align with acetyl-transferases, there is no conservation of catalytic residues found. It is likely that the function is one of cell-adhesion. In Structure 3jx8, it is interesting to note that the sequence of contains several well defined sequence repeats, centred around GSG motifs defining the tight beta turn between the two sheets of the super-helix; there are 8 such repeats in the C-terminal half of the protein, which could be grouped into 4 repeats of two. It seems likely that this family belongs to the superfamily of trimeric auto-transporter adhesins (TAAs), which are important virulence factors in Gram-negative pathogens. In the case of Parabacteroides distasonis, which is a component of the normal distal human gut microbiota, TAA-like complexes probably modulate adherence to the host (information derived from TOPSAN).	1.50941e-10
NZ_CP054139.1\|WP_173413465.1\|668548_669643_+\|undecaprenyldiphospho-muramoylpentapeptide-beta-N-acetylglucosaminyltransferase	gnl\|CDD\|234825	PRK00726, murG, undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional.	4.18524e-140
NZ_CP054139.1\|WP_173413463.1\|665723_667067_+\|UDP-N-acetylmuramoyl-L-alanine--D-glutamate-ligase	gnl\|CDD\|223842	COG0771, MurD, UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell envelope biogenesis, outer membrane].	2.44199e-143
NZ_CP054139.1\|WP_173413455.1\|654972_656694_-\|M28-family-peptidase	gnl\|CDD\|349895	cd05643, M28_like, M28 Zn-peptidase-like. Peptidase family M28 (also called aminopeptidase Y family), uncharacterized subfamily. The M28 family contains aminopeptidases as well as carboxypeptidases. They typically 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 protein subfamily conserves some of the metal-coordinating residues of the typically co-catalytic M28 family which might suggest binding of a single metal ion.	2.08666e-59
NZ_CP054139.1\|WP_173413462.1\|664358_665600_+\|phospho-N-acetylmuramoyl-pentapeptide--transferase	gnl\|CDD\|234638	PRK00108, mraY, phospho-N-acetylmuramoyl-pentapeptide-transferase; Provisional.	3.36535e-166
NZ_CP054139.1\|WP_173413464.1\|667221_668415_+\|FtsW/RodA/SpoVE-family-cell-cycle-protein	gnl\|CDD\|274232	TIGR02614, Putative_lipid_II_flippase_FtsW, cell division protein FtsW. This family consists of FtsW, an integral membrane protein with ten transmembrane segments. In general, it is one of two paralogs involved in peptidoglycan biosynthesis, the other being RodA, and is essential for cell division. All members of the seed alignment for this model are encoded in operons for the biosynthesis of UDP-N-acetylmuramoyl-pentapeptide, a precursor of murein (peptidoglycan). The FtsW designation is not used in endospore-forming bacterial (e.g. Bacillus subtilis), where the member of this family is designated SpoVE and three or more RodA/FtsW/SpoVE family paralogs are present. SpoVE acts in spore cortex formation and is dispensible for growth. Biological rolls for FtsW in cell division include recruitment of penicillin-binding protein 3 to the division site. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Cellular processes, Cell division].	8.35769e-91

>NZ_CP054139.1|WP_173413461.1|662200_663664_+|UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,-6-diaminopimelate-ligase
MKYLSDLLEGLPFTELQGSADVEITAIVFDSRKVVPGCLFVAVKGTAVDGHDYIEQAVKDGAVAVICEELPGHTADGADFLMVANSAVALGIVAANFYGNPSDQLKLVGVTGTNGKTTIATLLYKLFRDLGYKCGLLSTVENQVNGKVVPATHTTPDPVALNALLADMVAQGCDYCFMEVSSHAVAQHRIEGLAFSGGIFSNLTHDHLDYHKTFDAYLKAKKTFFDTLPKTAFALTNVDDKNGNVMLQNTKAHKKTYGLKNMADFKVKILENGFNGLLLNIDGEEVWFKLVGNFNAYNLLAVYGAAMLLDQDKAAVLVSLSRLSGAEGRFDALVSPNKVIGIVDYAHTPDAVQNVLTTIHDLRKGTEQVITIIGCGGDRDRAKRPVMAAMACEWSDKVILTSDNPRSEDPAEIIKEMEAGVTGANKKKTISIVDRREAIKTACHLAKLGDIILVAGKGHEKYQEIKGVRNHFDDREELEEQFKLMNE
>NZ_CP054139.1|WP_173413460.1|660071_662204_+|PASTA-domain-containing-protein
MNIRANILLRVYIAFGLIVLFAGAVVVQLCRVQFIQGKKWQSMADSLSTKYVNVEASRGNILALDGSLLATSVPEYELHMDMLAAGIETEALFNKRIDSLAEKMASYFGDHTAQEYSRIFRSARKDSLRYQLVRRKVSYQQLKDIRKFPVFNLGKYKGGLIVVQKNKRIFPFKTLALRTIGYNNENVKNVVGLEGAYKDYINGENGKRLMQRMAGGVWAPVNDEDEVTAKDGADIMSTIDVNFQDVAQKVLKHQLDSVQADFGTVVLMEVATGEVRAIANYTRTKEGDYQERLNYAINYEAEPGSTFKLASYMAMIDDNKLDTGKMVDIMHGGPYQIINPRNGKVALTVRDAEDEGGLVSARRAFEKSSNIGAVKLVTAAYGSNPSAFTDKLYAWHLNERNGLQIPGEGRPIIKNPKSKLWNNLQSLAQIAYGYESTLSPLQMLTFYNSVANNGKMISPIFVKEIRRMGNTVERFQARVINPQVCSPEALAKVKGLLEGVVEEGTGKLVIKNKLYTVAGKTGTAQIANGKLGYGEKNSHQTSFCGYFPADKPKYSMIVVISNPHYNGSHLAAWVSGPVFRRIADRVYAHDIAMNRPPEQHLVGNTQPPKFKDGDYKALKQVYNKLGVKPLYASNNPGSSADTSAGIVFEEAKYKKGTVPNVTGMGLSDAMYALGNAGYKVNARGSGVVQNQSAAVGSVMPKGSTISIVLQ
>NZ_CP054139.1|WP_173413459.1|659670_660075_+|hypothetical-protein
MSNRFRTEIEEEQAEQEAIAEEAPKTGIPENWFTTFLSKGVISTETATGALPFILFLAALGMIYIGNMHMAENNIREIDKLSKEVKELSWDYKTTKADLAFKSTLNEVTKLADTLGLKEPVSPPQKIVVKEDAQ
>NZ_CP054139.1|WP_173413458.1|658771_659674_+|16S-rRNA-(cytosine(1402)-N(4))-methyltransferase-RsmH
MSNYHVPVMLQECIEALNIKSNGTYVDVTFGGGGHSREIMKHLGADGRLLAFDQDADAQRNKIADDRFTFIDQNFRYLKNFCRLHNAVPVDGILADLGVSSFQFDQAERGFSIRFDAELDMRMNQSAELSAKDIVNTYAEADLHRIFGMYGEIQNSKTLAKTIVTARLNAPINTVADLKSAIQNLIPRGKENKYLAQVFQALRIEVNQELEALKDFLTQSAEVLVPGGRLVVMSYHSLEDRLVKNFIAKGKFSGEVEKDFYGNDQKPFDAVSRGAIVANDEEIQLNNRARSAKLRIAVKK
>NZ_CP054139.1|WP_173413457.1|658302_658779_+|division/cell-wall-cluster-transcriptional-repressor-MraZ
MSYFFGDYSCKLDVKSRLTLPSALKQQLPGEGKEPLMIARGFDKNLLIYTKIEWDGVIAELLKLNQYERENQQFIRHFTRGATMIEPDGAGRVLLPKILCDHAGIDPQSANEIILSCQINKIEVWEKSAHEAMLANEPADFAALAERVMGNKARRGDE
>NZ_CP054139.1|WP_173413456.1|657236_657839_+|DUF2807-domain-containing-protein
MKTSIITLATLLAIATISNTAFAADKKDKTVTVINEAKNFNKIEVRGNVEVYLTNGPANSVKAYNNYYGESALVQNQNGTLRISSFSKEALVVYVTADDLSAITLYDNAYIKTGKNFSSLDLTVNLFDTATAQLDIQTVNASININNRAKADLVGKVENCDMQVNQASTVNSTNFVAGSLTKKVNGFVTEVKSNQELAIL
>NZ_CP054139.1|WP_173413455.1|654972_656694_-|M28-family-peptidase
MKKTLLITALALSACSTLAQKNNAIDAYYPLLRGTFIEANAYKTTSFVESRWRVPGNSGFTQSIYEVEKTLQKAGFKKEVKGEADGPLTYRIESRDMRGPTWEPVNAVVSIVGESQPLLSFATNRNMIAMYSGSTPAGGITAEVVMMDRVKLNAATPESLKDKIVFSESSVGSVYQGAVTKGALGAMGYSMPAYTQPDKNVNSIQFTRISNQDSTSQKFGIVMSYAAKERLKAALHKGPVKLHVEVTCKIYKAKELTIVANARGTAKPDERFVFSAHVQEPGANDNATGVGTLAEMARVTAQLINAKKFEPKRTITFLWGDEINSTARYIREDSVRAKGIKWGLSLDMVGEDVSKTGGTFLIEKMPDPSAIWTRGEEKHTEWGGRPLKESDMFPHYFNDVLLNRCKQQAANNGWVVKTNPFEGGSDHTPFLQAKIPGLLMWHFTDVYYHTDADRLNMVSAQEMKNVGVSALATAYTLASANEATTSTLIAELQKNATDRLQVEYQLSAAAVKNGTPAADEKHKLDVWTKWYTDAIGKMTDINVGGATASVNDKIASAQKAVNDLNAKLDADLK
>NZ_CP054139.1|WP_173413454.1|654381_654894_+|fasciclin-domain-containing-protein
MKKVFFLLVLATVAVGLSKTYAQSTALKGIKDDSDFYKFATLVRQANMDATLNALGSFTMFAPDNTTFREMPGDKLDSIAADPAKLTALLKAHIVKGKFTTNEIIKKLTLGKGKTTLTNLLGQTLKLSRTPDNKLLITDANGDQVHFLAFDMPDAHGVIHGIDHLLVAGK
>NZ_CP054139.1|WP_173413453.1|652382_654275_+|RecQ-family-ATP-dependent-DNA-helicase
MTIQEILKQYWNHDSFRPLQEEIIQSVLLGYDTLALLPTGGGKSVCFQVPALAKDGICIVVSPLIALMKDQVENLRAKGINAIAIVSGMSRREVDILLDNCIYGPVKFLYLSPERLLSDLVRERIKYMNVNLFAIDEAHCISQWGYDFRPPYLHIADLRKLHPKVPVLALTATATAEVKIDIQEKLQFAKPNVFQKSFERKNLAYVVQAHEDKLRKMMDVIRGVKGSGIVYVRNRKETFEIAKYLTQHGFRADYYHAGLPSDQRSVKQAAWKTGKVPIIVATNAFGMGIDKPDVRFVIHLEIPESLEAYYQEAGRAGRDEQKAYAVLLYGPADRAKQERKFISAFPSADEIKVTYHYLANYYQIAYGAGEGLSLELDLGEFCSRFKLEPIKTLNALKFLEKDEYLAFNESVFLPSRFRFEVRNEELYNFQIQNPGWDAFIKTLLRSYAGAFDNYVRIREFDIAKRTHMNVQQVIDGLNQLQQFGILNYLPQTDRPQVTWIRARQIPDNVTINTQYIEERKAVARRKLEAVFAYAEHKRCRSQMLLAYFDESDSDKCGICDVCLAERRQNNAATITDDIITEMLQLLSNAPQKLDDLVSSIHTGTDKEKIDTLRQLLDAGKIKTDGSRYYV
>NZ_CP054139.1|WP_173413452.1|651651_652293_+|hypothetical-protein
MADGRKIRKTIFIIIGSLLLLYILTVVYNVVMLGYDFGFFDKEYSTYDLAYQYDSKHGEINSAKRYFNSIVPANKIVEVEFKGDNKITILEIHPGKGDSVQTDKFSAHNLDIDSKRVDEALQILGWTRDKLGTLKQKLDAANCIGIKNGEPAQVRFQRHGSDTYIFNVFNTPIPDSLKKHYNDSCTYVYVNSHLVLENGGEGMGSHCFPNGGR
>NZ_CP054139.1|WP_173413462.1|664358_665600_+|phospho-N-acetylmuramoyl-pentapeptide--transferase
MLYYLFTYLNKNYSIPGLGVFQYITFRTAMAVIVSLLITTVYGRRLIDYLRFKQVGETVRNLGLEGQMQKAGTPTMGGLIILSGILVPTLLFAKLENVYIILMIVTTVWLGAIGFLDDYIKVFKKNKEGLAGKFKIVGQVGLALIVGYTMYFHTDIKIRQEVKLPVKYDAPVDFHMKNDKPIYTQDIKSTKTTMPFYKNNEFDYGKVLKFLGHGYEKYTLIVFLFFVIVIITFISNGANITDGIDGLATGTSAIIGITLAILAYVSGNIVISDYLNIMYIPNSGELVIFAGAFVGACVGFLWYNSYPAQVFMGDTGSLAIGGIIAVFAVVIRKELLLPVLCGVFVVENVSVMMQVGWFKYTKKKFGEGRRIFLMAPLHHHYQKKGFHEAKIVTRFWILCIMLAIITVITLKLR
>NZ_CP054139.1|WP_173413463.1|665723_667067_+|UDP-N-acetylmuramoyl-L-alanine--D-glutamate-ligase
MNDNKNIAILGAGESGVGAAYLAQQQGYDVFVSDMGAIAPKYKQQLQQWGIRFEEGQHTEADILNAVEVIKSPGIPERAPLIKKLREKGVPVISEIEFAGRYTNAKMVCITGSNGKTTTTTLTYHILKKAGLNVGLAGNIGKSFAYQVATEKFDIYVLEISSFMLDDMYKFKADIAILLNITPDHLDRYEYKMENYVASKFRIAQNQTAGDHFIYCADDAETIKGMQSRHFEAKLLPFSIEQIIEPGAYLENDNIVININQEHFTMSITDLALQGKHNVYNSLASGLAAKVLEIRNVTVRESMMDIQPIEHRMEFVAKISGIRFINDSKATNVNSTWFALESMSTDVVLILGGVDKGNDYSMLTELVKQKVRGIVCLGVDNSRIHDAFESVVDVIANTSSAEEAAQVAFHMAKKGDTVLLSPACASFDLFKNYEDRGTQFKNAVMQL
>NZ_CP054139.1|WP_173413464.1|667221_668415_+|FtsW/RodA/SpoVE-family-cell-cycle-protein
MNKILNNTKGDRWIWLIVILLSIISMLAVYSSTGTLAYKQGKSTETILFKHMLMIFAGIALMYISHKIDYRYYAGISKVFMIITIPLLLITLVFGNNVNGASRWLAIPGTGFTFQTSDFAKLALITYLARMLSRKQENIRDVKESFAPIMGAVCLVFVLIMWANMSTALMLFGVSILLLIMGRVSIKQIMITCAVGGCLVVMVALLGPRRHLYMTRIETWRHPEKASVEKKFQGDHAKIAIATGGIFGKGPGNSTERNYLPESYSDEIYAIIVEEYGLIGGVTILGLYLFLLYRCVKIVTKAPKAFGALLAAGLSFSLCIQAFANMAIAVGLGPVTGVPLPLVSMGGTSILFTSVAFGIILSVSRHIDENEELKSAEKTEAAPKIKNKVIVGEIGLA
>NZ_CP054139.1|WP_173413465.1|668548_669643_+|undecaprenyldiphospho-muramoylpentapeptide-beta-N-acetylglucosaminyltransferase
MKAKRIIISGGGTGGHIFPAIAIANALKRLDPSTEILFVGANGRMEMEKVPAAGYKIIGLDIQGIQRKSLWKNVMFPVKLIGSVRKALQIIKEFKPDAAVGVGGYASGPLLYAAGLKGIPYLIQEQNSYAGITNKMLGKKAKKICVAFDGMDKFFPADRIIKTGNPIRKESVDIANKRLQAIELMKLSAEKKTILVTGGSLGARTLNNSIMAHLDEIIKADVQLIWQTGKFYYKGIIEKLGEDYHPNIRVMNFLNRMDLAYAAADVIISRAGAGTIAELCEVKKPVILVPSPNVAEDHQTKNALALVQENACVFVADRDAEVKLVDTALELLKDKDKQKKLSQNIAKLAMPNADDVIAKEVTQI
>NZ_CP054139.1|WP_173413466.1|669824_671183_+|UDP-N-acetylmuramate--L-alanine-ligase
MELHNIQRVYLAGIGGIGMSGLARYFARKGCIVCGYDKTATDLTMALQNEGMQIIYEDRAEFIPMSFHKPCDGTLIIYTPAMPKDSAILHFFKQQGFELFKRSQVLGLISKGMYTIAVAGTHGKTTTSCMIAHILKYSGTDCSAFLGGIAANYQSNVLYGDNNVMVVEADEYDRSFLTLHPDVAIITSMDADHLDIYGDHSHLTESFRLFASQIKDGGTLIYHKGLPVGHDGITYARDEEAGAMAENVRIESGDFYFDFDNGGTQIEDIRMGIAGMHNIDNATAAIQAALLLNVAPDAIKSALGSFKGVKRRFEYIVKNEAHIYIDDYAHHPEELRAAISSVKKLYPNKKLTVVFQPHLYTRTRDFVDGFAEVLDMSDELLLLDIYPARELPIEGVNSELILDRMKMWNKRKCGKQECLDIVRVEKPELLLTVGAGDIDQLVHSLKNILEHV
>NZ_CP054139.1|WP_173413467.1|671175_672078_+|cell-division-protein-FtsQ
MFKNKRLWRNILFGFIWLVSLSGLVVLMSFIEVKKSATVCKDVQIIIPGNQFFIDKQEVDNILGLNGTSLKGLRISNINIQALENKLRKNPFVESATVYVDMDGVLMVEISQRQPMLRIVNRYDRDFYVDQHGLKIPLSDNFTAKVLVANGYIDEGFANRVDTLMTPMARNLFKTADFIRRDSLWSAQIAQLYVNEKQEIELIPRVGNQRILLGNADSLEVKFRNLLAFYKQAIPQVGWVAYKAINIKYTNQVIGIKNDNLKHDTAAVNNAVKPDSLLKAAVDTTKKATTTTTSTNKVKN
>NZ_CP054139.1|WP_173413468.1|672084_673434_+|cell-division-protein-FtsA
MDKSSTHEKSAPIAVGLDIGTTKICAIVGRRSKNGKIEVLGIGKAESAGVTRGMVSNIDKTVQGIIQAVDIAGTQSNVEIKVVNVGIAGQHIKSLQHRGLITRRALDTEISRKDIEKLVEDMYNLVMSPGEEIIHVLPQEFTVDNEPGIKDPVGMAGVRLEANFHIISGQVTAIKNIVKCVNKASLDSQELILEPLASSESVLSEEEKEAGVVLVDIGGGTTDVAIFHEGIIRHTAVIPFGGNSVTEDIREGCSVMRNIAEQLKLRFGSALADENKENEIVCVPGLRGREPKEISVKNLAYVIQARMEEIVEHIYYEIKSSGYEKKLIAGIVITGGGAQLKHLSQLVEFVTGLDCRIGYPNEHLAKNEVLPKPTYEELQSPMFATGIGLLIKGIQKMEYEMEGQTPTAASMKPEKPKYADERRLGLFGKLLETGKKFIKDDIKDEDFLK
>NZ_CP054139.1|WP_173413469.1|673652_675302_+|cell-division-protein-FtsZ
MQFEMLKEKSSIIKVIGVGGGGGNAVNHMYKQGITGVDFIICNTDAQALELSPIPNKVQLGASLTEGMGAGSIPEVGKNSAIENIDDIKQMLGSNTRMLFITAGMGGGTGTGASPIIAKAARELDILTVGIITTPFSFEGKRRKMQADEGLEELKKYVDSFLVISNDRLRQIFGNLTLGSAFAQADNILTTAAKGIAEIITLPGYINVDFKDVRTVMKDSGVSIMGSCSAEGENRALKAVEGALASPLLKDNEIEGARYILLNISSGINEVTMDEVSIITDYIQEEAGLAADLIWGNCQDDTLGEKLSVTIIATGFQTKDEREKEQSTKRVVSMLVPEEKGAPLVRPVNEFITPVAPPPTAESYSTEPYMKGSEPAKPQTGLFDLFAPSAAVTETPQADNSDVVKHSLVEEEPASAPEPDFGEFTFKVSDSMMEFESFKEEAVAEPEPEPELPPAPVAGADDHKTAESVEEQMRKARERIMRLKDLTMKNRNGNIQELENIPAYKRKEIALQQTPASSESEISRFTLLTDDEGNTEIRRNNSFLHDNVD
>NZ_CP054139.1|WP_173413470.1|675448_676705_+|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme
MDLFDKIEKNMGGPIGQHQKWSHGYFSFPKLEGEIAPHMMFNGVEHLVWSLNNYLGLANHPEVRKADAEAAADFGMAYPMGARMMSGNSRHHEELEAGLAEFVGKEDAFLLNYGYQGMVSIIDTLVDRNDVIVYDAESHACIIDGVRLHMGKRFVYQHNDMESCAKQLERATRLTEQTGGGILLITEGVFGMSGAQGKLKEIVALKEKFKFRILIDDAHGFGTLGATGAGAHEEQGCVDGVDVYFGTFAKSMAGIGAFVAADKMIVDFLRYNMRSQTFAKALPMPMVLGLKKRFELLKSQPELREKLWTIARALQNGLVEHGFDIGITNSVVTPVFLKGDLHEATSLTMDLRKRYHIFCSIVVYPVIPKGLIELRLIPTAVHTLEDVQRTLDAFSDVAEKLKAGDYKQKEEKLAEVEA
>NZ_CP054139.1|WP_173413471.1|677036_678320_+|hypothetical-protein
MISSLPVVKMPLAVKIMLALVAILLLANILSPLRLNTDAIRYFNIMLYLKGMLPPTDYAGSDFLPHGYPLLLKYLDKAGLLNSKAMIAINILAGVTVGYLICRLLPAKNRLIVTALLLLSYINIKHLILPIPDELFAGSLLLATWCWAKALKDKWIYCLPAFLITAAAIYLRTAGIVIPCGIVLFLIYTNWPAIKKNKYLLTALIGVVLTAIALFLYRLKGLEQRNDYFRYLNLEGIVHGPNNLSARVLLHLQEMGELLLNIPCSKLNTFVPHPLAFLIMPLIIATGLFMFALTVYIIIRTELYRHLILWVYLCYMTIIIIWPFYDTRFLIPIIPLFIYCLYTAFERCRPLWALKLLATVYVLMGLFALSYSTAISINQSVFLKLYGFDKEMTASYRQHFEDKRSGTVVVYDINKQRVLYILNAYDK

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Crispr_ID: NZ_CP054139_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP054139_3

901255-901413

Orphan

Consensus_repeat	Method
AAAAAGTAAAACTGTGCAAGGTTTTAT	PILER-CR

2 spacers

The CRISPR arrays of NZ_CP054139_3

>merge|NZ_CP054139|3|901255-901413|PILER-CR
AAAAGTAAAACTGTGCAAGGTTTTAAAGTCTCCCCCCTCGGGGGAGATTTAGAGGGGGAGATTTCCTCAAAAAGTAAAACTGTGCAAGGTTTTATTAATGAGGGAGATAAACGATACCCGGCCCCGAGCGATAAAAGGTAAAACTGTGCAAGGTTTTAT

>NZ_CP054139|3|1|901255-901413|PILER-CR
AAAAGTAAAACTGTGCAAGGTTTTAAA	GTCTCCCCCCTCGGGGGAGATTTAGAGGGGGAGATTTCCTCA
AAAAGTAAAACTGTGCAAGGTTTTATT	AATGAGGGAGATAAACGATACCCGGCCCCGAGCGATA
AAAGGTAAAACTGTGCAAGGTTTTAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP054139.1\|WP_173417710.1\|897452_898268_-\|HEAT-repeat-domain-containing-protein	unknown	unknown	gnl\|CDD\|379219
NZ_CP054139.1\|WP_173413635.1\|904244_905060_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|236216
NZ_CP054139.1\|WP_173413630.1\|899645_900059_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173413640.1\|911261_911783_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173413628.1\|896583_897438_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173413636.1\|906242_906833_-\|NTP-transferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|133025
NZ_CP054139.1\|WP_173413625.1\|890586_892926_-\|DPP-IV-N-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|366374
NZ_CP054139.1\|WP_173417711.1\|898283_898808_-\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|224511
NZ_CP054139.1\|WP_173413629.1\|899307_899544_+\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|238045
NZ_CP054139.1\|WP_173413637.1\|906825_907980_-\|XdhC-family-protein	unknown	unknown	gnl\|CDD\|379212
NZ_CP054139.1\|WP_173413624.1\|889483_890389_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|197666
NZ_CP054139.1\|WP_173413633.1\|902985_903183_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173413631.1\|900558_901194_+\|peroxiredoxin	unknown	unknown	gnl\|CDD\|239314
NZ_CP054139.1\|WP_173417712.1\|905263_906004_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173413627.1\|895748_896561_-\|DUF4097-family-beta-strand-repeat-protein	unknown	unknown	gnl\|CDD\|372574
NZ_CP054139.1\|WP_173413632.1\|901740_902391_+\|redoxin-domain-containing-protein	unknown	unknown	gnl\|CDD\|239268
NZ_CP054139.1\|WP_173413626.1\|893162_895619_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|379720
NZ_CP054139.1\|WP_173413639.1\|909750_911082_-\|amino-acid-permease	unknown	unknown	gnl\|CDD\|273332
NZ_CP054139.1\|WP_173413634.1\|903383_904214_+\|5-dehydro-4-deoxy-D-glucuronate-isomerase	unknown	unknown	gnl\|CDD\|179169
NZ_CP054139.1\|WP_173413638.1\|908243_909404_-\|aminotransferase-class-V-fold-PLP-dependent-enzyme	unknown	unknown	gnl\|CDD\|99738

Protein	Function_ID	Function_description	E-value
NZ_CP054139.1\|WP_173417710.1\|897452_898268_-\|HEAT-repeat-domain-containing-protein	gnl\|CDD\|379219	pfam13490, zf-HC2, Putative zinc-finger. This is a putative zinc-finger found in some anti-sigma factor proteins.	8.99455e-08
NZ_CP054139.1\|WP_173413635.1\|904244_905060_+\|SDR-family-oxidoreductase	gnl\|CDD\|236216	PRK08277, PRK08277, D-mannonate oxidoreductase; Provisional.	1.29897e-118
NZ_CP054139.1\|WP_173413636.1\|906242_906833_-\|NTP-transferase-domain-containing-protein	gnl\|CDD\|133025	cd04182, GT_2_like_f, GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function. GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.	1.97045e-65
NZ_CP054139.1\|WP_173413629.1\|899307_899544_+\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|238045	cd00093, HTH_XRE, Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.	2.39929e-08
NZ_CP054139.1\|WP_173417711.1\|898283_898808_-\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|224511	COG1595, RpoE, DNA-directed RNA polymerase specialized sigma subunit, sigma24 homolog [Transcription].	1.22446e-32
NZ_CP054139.1\|WP_173413625.1\|890586_892926_-\|DPP-IV-N-terminal-domain-containing-protein	gnl\|CDD\|366374	pfam00930, DPPIV_N, Dipeptidyl peptidase IV (DPP IV) N-terminal region. This family is an alignment of the region to the N-terminal side of the active site. The Prosite motif does not correspond to this Pfam entry.	1.05635e-60
NZ_CP054139.1\|WP_173413637.1\|906825_907980_-\|XdhC-family-protein	gnl\|CDD\|379212	pfam13478, XdhC_C, XdhC Rossmann domain. This entry is the rossmann domain found in the Xanthine dehydrogenase accessory protein.	6.69564e-45
NZ_CP054139.1\|WP_173413624.1\|889483_890389_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|197666	smart00342, HTH_ARAC, helix_turn_helix, arabinose operon control protein.	2.78762e-17
NZ_CP054139.1\|WP_173413631.1\|900558_901194_+\|peroxiredoxin	gnl\|CDD\|239314	cd03016, PRX_1cys, Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one conserved cysteine, which serves as the peroxidatic cysteine. They are homodimeric thiol-specific antioxidant (TSA) proteins that confer a protective role in cells by reducing and detoxifying hydrogen peroxide, peroxynitrite, and organic hydroperoxides. As with all other PRXs, a cysteine sulfenic acid intermediate is formed upon reaction of 1-cys PRX with its substrates. Having no resolving cysteine, the oxidized enzyme is resolved by an external small-molecule or protein reductant such as thioredoxin or glutaredoxin. Similar to typical 2-cys PRX, 1-cys PRX forms a functional dimeric unit with a B-type interface, as well as a decameric structure which is stabilized in the reduced form of the enzyme. Other oligomeric forms, tetramers and hexamers, have also been reported. Mammalian 1-cys PRX is localized cellularly in the cytosol and is expressed at high levels in brain, eye, testes and lung. The seed-specific plant 1-cys PRXs protect tissues from reactive oxygen species during desiccation and are also called rehydrins.	2.62308e-133
NZ_CP054139.1\|WP_173413627.1\|895748_896561_-\|DUF4097-family-beta-strand-repeat-protein	gnl\|CDD\|372574	pfam13349, DUF4097, Putative adhesin. This has a putative all-beta structure with a twenty-residue repeat with a highly conserved repeating GD, gly-asp, motif. It may form part of a bacterial adhesin.	5.40184e-08
NZ_CP054139.1\|WP_173413632.1\|901740_902391_+\|redoxin-domain-containing-protein	gnl\|CDD\|239268	cd02970, PRX_like2, Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.	9.61157e-05
NZ_CP054139.1\|WP_173413626.1\|893162_895619_-\|TonB-dependent-receptor	gnl\|CDD\|379720	pfam14905, OMP_b-brl_3, Outer membrane protein beta-barrel family. This family includes proteins annotated as TonB dependent receptors. But it is also likely to contain other membrane beta barrel proteins of other functions.	3.52821e-101
NZ_CP054139.1\|WP_173413639.1\|909750_911082_-\|amino-acid-permease	gnl\|CDD\|273332	TIGR00911, High-affinity_methionine_permease, L-type amino acid transporter. [Transport and binding proteins, Amino acids, peptides and amines].	1.06665e-38
NZ_CP054139.1\|WP_173413634.1\|903383_904214_+\|5-dehydro-4-deoxy-D-glucuronate-isomerase	gnl\|CDD\|179169	PRK00924, PRK00924, 5-keto-4-deoxyuronate isomerase; Provisional.	2.12404e-180
NZ_CP054139.1\|WP_173413638.1\|908243_909404_-\|aminotransferase-class-V-fold-PLP-dependent-enzyme	gnl\|CDD\|99738	cd00614, CGS_like, CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.	1.13006e-144

>NZ_CP054139.1|WP_173413631.1|900558_901194_+|peroxiredoxin
MSLRLGDDAPNFKAQTSQGEIDFYEFLGDGWGVLFSHPADYTPVCTTELGRTAALKEEFAKRNVKVAALSVDSVESHHGWISDINETQGVEVTFPIIADEDRKIAEAYDMIHPNASLNATVRSLFIIGPDKKIKLIITYPASTGRNFNEILRVIDSLQLTAYHSVATPADWKDGEDVVVLPSIKTEDIPDKFPKGHKVVKPYLRTTPQPNK
>NZ_CP054139.1|WP_173413630.1|899645_900059_+|hypothetical-protein
MKAICTLILAAAALSITACRNPQTEASNKKITAYPDNSTKYKQALIAELKAHPEGFTYTFRGYTKKANAEYMSVRIKRGSFDNVEEVLVNKWNKLDGIRRTKGLGYRAAELKGLKLDLVSTGNEQCFVYEDLDRIVD
>NZ_CP054139.1|WP_173413629.1|899307_899544_+|helix-turn-helix-domain-containing-protein
MKQQEEHDHDKTVRRLLDKVRHYRKLNKLTQGHLARHLRISQNAYSKLERGISELTIYKLLVIMQILGISIFELLEKH
>NZ_CP054139.1|WP_173417711.1|898283_898808_-|sigma-70-family-RNA-polymerase-sigma-factor
MLKVKAGDLDRMGLLFQRYHRQLYGFLFHMTYQREAAEDMVQQVFYKMLKYRQNFTGSGEFIHWMYAIARNVLKDQGKRKKLVMAKDGVEDMADYLPGGTDVAEQLDKKQAAQGLHRAMAKLNDDEREILSLSRFQELKHQEIAQILNISEGAVKVRVHRAMCQLKEIYTKIER
>NZ_CP054139.1|WP_173417710.1|897452_898268_-|HEAT-repeat-domain-containing-protein
MDCEKYSELFTSWIDKALPPAERLKLEQHLSGCPGCRAELEAMKELWIEMGEMETPAPSEHMQVKFEAMLNTFKEEAADKTNAWANFKNALAQLWQWQPRLPLAYSLVIIMMSFACGYWVFSMGKGGQQDKQLATLSSQVHELKQTMMLAMLENPSASERIKGVSYTSEIKHVDQQVIDALFATLNNDPNVNVRLSTLDALSQLSNHPEVRTGLIKSITQQDSPLMQSAIADVMLKLQEKRSVNSFKELLKQKDLDKGVRNKIKETINNLI
>NZ_CP054139.1|WP_173413628.1|896583_897438_-|hypothetical-protein
MKRLIWIALLAGWGHCFAQKQEFKTHVSKQFTLQKPASGTVFALYNVFGDVKIEGYSGNEVVIEIEETITAKDAAELETAKKEFKLGFDQKADSIIAYTAEPYDTRPHRNWNKDDDRKERHYNVKLDYTVKVPNNINLNAGTVNNGEAYVKDVYGTLKVNNVNGPLTIVNAKSTTMARTVNGPVTVNYLSIPQEESSYYTVNGKMEITYPANFEANLQFKSMNGQFFTDFPDTEVLPTEITKTQNKGNNGTIYRLNKNTAIRVGKGGKVFKFETLNGNIYIKKA
>NZ_CP054139.1|WP_173413627.1|895748_896561_-|DUF4097-family-beta-strand-repeat-protein
MKALKFTGLVALALALSTRLMAQESQQLTVPLSDPGKPYKLNVDLVTGSIKVSVHDGKDIIIDASAPHGRKEAKESGGMRRLSSGENLDVEAREKNNQVRISNNMPNKNVALDIKIPRGATNIKLMAVNGGDISVNDVSSDIEASNTNGAIKLTNISGSAVANTTNGRVLVTFKTLDNKAALAFTTLNGDVDVTFPATFKANLKARSDNGNVFSDFDMVTEKSPSKSTKTAKDGMYRITIEDWVYGKINGGGPELLMKNMNGNIYIRKAK
>NZ_CP054139.1|WP_173413626.1|893162_895619_-|TonB-dependent-receptor
MKTIITAIIAAWLSFALNLASAQTPQGKISGQVFDAAKQPAIAATIVLVRFKDSSTVKTTLADAQGRFVFDKIAAGDYRVNITAVGFQKYRSAKVALGETVPAIELPSINLKPGTSTLKEVAITAQKPFIELKADRTVVNVGASITNAGANALEALEKAPGIIVNDDGTISYKGKTGLQIMIDNKPSYLSGEALANYLRSLPASVLDQIELMPNPPAQYDASGTAGIINIKTKRFKIKGFNGSAAASVGRAKYMRTSESFNMNYRENKVNFFALAGYSAQNNYRRLDVGRTYFDALNSIKSSYTEVAFFNPSTQNTNVKTGMDYYVSPKTTLGVVLTGVMTTGDNYNPVNSFLRNKTGGLDSSIVANNNTNYNFKNGGINLNYSHQYDSLGRNITVDVDYIRYNNYRDQSFMSASYNTAGALGSKQDIIDNLPNIINIWSAKSDYTLPIDKKSKLAFGVKTSYVNTDNGANYFNIINNIQTIDYTRTNRFLYKENINAAYINYNKDFKRFSLQLGLRAENTRVNAHQLGNALGQDSSFVKNYTNLFPTGFVLYKLDSAGNNSLNLSYGRRIERPSYQDLNPFVIILDKYSAFSGNPFLRPQFVNVYQFSYSFKSKLILQASYNYVSDYQVEYDYQQGDIFFANRINLGSREETAFGAILNLEPVKWWKFYMDLEYNFARFKGQLGSVPINTPSNYAFMNTTSQFNLSHGWSSELNVFYVAPNHDSQFTHIARKQVNIGLAKKVLNNNGTIRLSARDLFKGNYSAGTINNIPGAAITYHNDNGNRSVNLAFSYNFGKSANIPKKRQTGSAEAEQNRAGN
>NZ_CP054139.1|WP_173413625.1|890586_892926_-|DPP-IV-N-terminal-domain-containing-protein
MNKFLLTALPFALALGANAQAPKAYTAQDYQRAESQMAASLSPLVTRSGIRPNWMPDDRFWYKEDSKFIVFNPAKGSKSAAFDHDKLAAALSTASGKSYTAANLPFDAIVYASDNKSVIFMADGKQWKFDGSKVEADSSPVQFPSAGGAFGGGRGGRGGRGGFGRGGNPNENVSPDGKTAVFIKDFNLWSRDIASNKLTQLTTDGVKDNGYATDNAGWAQGIRPILVWSPDSKKIATFQQDEREVNNMYMVNTKVGAPNLTQWKYPFPGDKVIPMLRRVIVNVDQPKVISIKCAPDPHRSTLSDDIKGGEGWADVYWSDDATKLVFASTNRDHKEEKVRMADAATGDVKELFTETVKTQFESGWAGVNWRYLSKSNEILWFSERDNWGHLYLYDANTGALKNQVDKGDWVQANLIKVDEKARVIYFMADGLQAENPYFSQLCKVGFDGKGFTVLTPGAGTHSVTFSPSGNYIVDTYSKPDVPPVTVLRDMKGKQLLELEKTDISKLTATGWKPCIPFSTKAHDGKTDVYGLMWVPRNVDPNKKYPVIDYIYPGPQGGSVGSWAFSVTRGDNGALAELGFVVVEIEGTSNPYRSKSFHDMSYGNMADNTLGDQVAGIKELATKYPYMDLTRVGIWGHSGGGFATAGAMFRYPDFFKVGIAESGNHENLNYEDNWGERYNGLTSNSDYAAQANESLAKNLKGKLMLAHGLMDNNVPPQNTLLVVEALERANKSFDLVIFPNSAHGYGQHSQYMMRRRWDYFVKNLLGVEPPLDYQMKGGGF
>NZ_CP054139.1|WP_173413624.1|889483_890389_-|helix-turn-helix-domain-containing-protein
METTTIEDFYRETSGLIPEGINKEIGHFNVFPIADMVARHHKKMPMPYNRRAYYKISFIVGHNRAEYADKVVEIERSALLFATPKIPYNYIPQDDKQGGYFCIFTHDFLLPAKSGIVIDDLPLFRPGTVPIFQINDEHAAELQHIFGKIRRELESDYAYKYDLLRNYVIELLHFGQKLQPATALYPSHTASARVSSLFIELLERQFPIESPNQRLNLRTAKDYADRLAVHVNHLNKVLKENTGKTTTDIISSRIVQEAKILLKQTDWNISEIAWSLGFEELAHFSNFFRKQTALAPVAFRG
>NZ_CP054139.1|WP_173413632.1|901740_902391_+|redoxin-domain-containing-protein
MLATTINNTKYPFFDLSEIIPERDLGFRAYKPLKPVRNGNYLPGFTLQAAYTRWQHFFNGAETHGALLLRQLLSKPLVISFYSPQWRQHGLEQLKQLNAIQSEIKASGGNLIIITAEKEKALEKLVWENNLSLNFYFDAKYEIAQSLRIYSDADPVWNRFSGIDTNVPLLATYVLDANRQVIFDQVSYDLSEAIAAKSIISAVYGASLAENLKRSA
>NZ_CP054139.1|WP_173413633.1|902985_903183_+|hypothetical-protein
MITVLTSIVMLALIALPFFKRGSKPADKTVVYKNDTDTTHAHYAINDRGYLEEISGNKVHGNFID
>NZ_CP054139.1|WP_173413634.1|903383_904214_+|5-dehydro-4-deoxy-D-glucuronate-isomerase
MKVIQAVHPEDFKAYQTAQIRERFLLDGIVEPGKINLVYTHYDRMIVGGASPLGTELDLGNYPNLRAEYFLERREIGIINVGGDGTVTADGTAYNVNKLDCLYIGKGTKEVKFASKSADAPAVFFILSAPAHMTYPTALMTNEEAVKVHAGATETANKRTINKYIFLEGIRSCQLVMGLTILEPGSVWNTMPAHVHDRRMEAYFYFDLDKSQKLVHYMGEGNETRHIMMNNHEAVVSPPWSIHSGSATANYKFIWGMAGENQDYTDMDPIAIPDLR
>NZ_CP054139.1|WP_173413635.1|904244_905060_+|SDR-family-oxidoreductase
MENNFSLAGKVIVVTGGTGILGKSFIDGIVAAGGAVGILGRNAEIAEQRAAEINANGGRAVALVADVLDKDQLIAAKEKLWAEFGRLDGLVNGAGGNMPEGAIQPDEDIFNMNLDGMKRVAEVNLWGTIIPTQIFGELIAKTGGGSIVNISSMNSKRAITKVLGYNMGKAGVDCYNQWFAVELANRYGDAIRMNALAPGFFLTEQNRNMHLKPDGSYSPRAESVIRQTPFKRFGKPEELIGALVWLLSDASAFVTGSMVCVDGGFSIFGGV
>NZ_CP054139.1|WP_173417712.1|905263_906004_+|hypothetical-protein
MPFMGKAQTVTLDYYFNHEVHKNAAGQEERFHYIWEEKDLNGYSNWGDAFVKEGAKLKSLDAAPTTANLKGTDIYIIVDPDTKKESPNPNYIMPKDVEQIEQYVKAGGVLVMMANDSANVELPHFNTLAAKFGMHFSDELHNHVLGNKIESGTMMVEGNPFFKTAKKIYMKDVCSIDLSGPATAILKNEGVAIIATAKYGKGTVLAIADPWLYNEYTNGHLPADGHYDNDKAINDVTQWLLKQVKK
>NZ_CP054139.1|WP_173413636.1|906242_906833_-|NTP-transferase-domain-containing-protein
MDNIGIVILAAGGSSRMGQPKQLLKYKDTTLLRHAVETAKASRTKGPLLVVTGALHDELFKECADLNISVAHNTNWQQGMSTSIHTGLRALTRANPATTGALIMLCDQPLITTEHINNLLDMFAHHRSQVIVATAFANVVGAPCIFSREVFDALYQLKGDKGARQIFDDPPQRLTTVPFKPAAVDVDTIEDYEGLL
>NZ_CP054139.1|WP_173413637.1|906825_907980_-|XdhC-family-protein
MSELQRLLAAYDAERKLGNACALATVVEVKGSAYRRPGARMLVTGEGQLTGTISGGCLEGDARRRAQQVMHRGKPEIIVYDSTDIDDDLENGAQLGCQGQIFILLEPIDFTDVYNPLELLRDTFRLQQPSVLATVLKSSDAAIAPIAERVLLLNNGNTKAGAINPNFIQQQLLPEMQDVLVNGTSACLDMEYAGVNIRVFLELIKPAPLLTIYGAGNDAQPLAKQAKNLGWRVMVIDGRPLQASAARFPEAELVQVARTGELQQYVNPTGFTVLMSHNYYYDLAVLEQLEQFPTLDYIGILGPRKKTDRMLADLAQKGIDTEALDKRLHSPIGLDIGSENADEIALAIMAELLAVRNGLNGGFLRNLDAPIHNRNQIIKALSNG
>NZ_CP054139.1|WP_173413638.1|908243_909404_-|aminotransferase-class-V-fold-PLP-dependent-enzyme
MNISYILNELGEERDNYFNAIAPPIVQTSNFAFNSVADFRAALGDEYDKNIYSRANNPTINILRKKLAALDGAEDAMVFGSGVAAIAVPVIALLQSGDHVVCVENPYSWTIKLFTKLLPRFGVTCTFINGTDTANFENALQANTKLIYLESPNTFSYELQDIAAVAQLAKSKGIITMMDNSYCSPLYQQPIKLGIDLVAQSATKYLGGHSDVVAGVLTGSRTLLKKVFELEHMNIGAGMAPQTAWLLIRGLRTLPLRLQRSFETCQKVTAWLQQHPAVDKVVWPFMPGFKQAELACRQMQGCGGLFSFTLKEPSIKKIEVFCDALQHILMAVSWGGHESLVIPAIATIPVADYSLDNPRHQLIRMYVGLEDAEYLIGDLEQALGEL
>NZ_CP054139.1|WP_173413639.1|909750_911082_-|amino-acid-permease
MSIIPRLNRFDLTMIVISLVIGMGIFANPSEVAVRAGSTWVFFGAWIFGGLVTLCGALTFAEIGARYPTTGGFYKVFSYCYHPAFAFMINWVLVISNAASVAVVAIIGANYINPVLLPADWQGPVGVKIMAISSVLILYALAFMGIKVSARTQNFLTMFKVLAIVVLCCAVFMHDDSHVVTTAAPHSGNLVTAFGLSLVAIFFTYGGYQQTINFGGDIIEPKHNIPRAIAIGIGVVILLYLSINFAYFKILGLGGLQQTTTLAAVMAGVIFGSIGSKIASVLMFVSVLAYINVNVMANPRVYYAMSEDGILPYIFRKVNPKTQVQEFGVTFFVLCILVVLFFADSFRNMLNYVMFFDTIGLSLAALSIFILRKRTKELDGTGIYTIKWFPLVPVVFILSYWFVTINIFYANPQAAFVCLCVFAAGLAIYYASVYLNKGKLPKE
>NZ_CP054139.1|WP_173413640.1|911261_911783_+|hypothetical-protein
MAFAQTKPARESREFRNFNKVATRANVAVVIPDGFKEIDVKSDNPAFDYGITIPDQGFEIWLKVMPQTESTPDSVYLEIGRAQARQLAGDNEYLVRGMPERVLNDYNADAGKTYFFNLPDAAATKRYKFALLITLQKSHKGTIMAVCLTNDKGPDFFRNINRARNCIKFKPAS

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Crispr_ID: NZ_CP054139_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP054139_4

942967-943055

Orphan

Consensus_repeat	Method
AGCAAACTACTTAACTGATCTATAAACC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP054139_4

>merge|NZ_CP054139|4|942967-943055|CRISPRCasFinder
AGCAAACTACTTAACTGATCTATAAACCCGAAGCCGGATATTTATTATCCGGCTTTACTTGAGCAAACTATTTAACTGATCTATAAACC

>NZ_CP054139|4|3|942967-943055|CRISPRCasFinder
AGCAAACTACTTAACTGATCTATAAACC	CGAAGCCGGATATTTATTATCCGGCTTTACTTG
AGCAAACTATTTAACTGATCTATAAACC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP054139.1\|WP_173413667.1\|945519_946278_-\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|369777
NZ_CP054139.1\|WP_173413669.1\|947525_949973_-\|beta-propeller-fold-lactonase-family-protein	unknown	unknown	gnl\|CDD\|225926
NZ_CP054139.1\|WP_173413664.1\|943127_943781_+\|DNA-alkylation-repair-protein	unknown	unknown	gnl\|CDD\|132880
NZ_CP054139.1\|WP_173413661.1\|939092_940088_-\|fumarylacetoacetate-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|376566
NZ_CP054139.1\|WP_173413660.1\|938630_938834_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173413657.1\|932581_934081_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|185760
NZ_CP054139.1\|WP_173413659.1\|937256_938150_+\|3-hydroxybutyryl-CoA-dehydrogenase	unknown	unknown	gnl\|CDD\|180269
NZ_CP054139.1\|WP_173413655.1\|931292_931919_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173413671.1\|951088_951286_-\|UPF0175-family-protein	unknown	unknown	gnl\|CDD\|377095
NZ_CP054139.1\|WP_173413668.1\|946302_947169_-\|aldose-1-epimerase-family-protein	unknown	unknown	gnl\|CDD\|185701
NZ_CP054139.1\|WP_173413673.1\|951948_954408_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173413665.1\|943885_944359_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|183103
NZ_CP054139.1\|WP_173413662.1\|940493_941651_+\|homogentisate-1,2-dioxygenase	unknown	unknown	gnl\|CDD\|226039
NZ_CP054139.1\|WP_173413670.1\|950266_951061_-\|5'-nucleotidase,-lipoprotein-e(P4)-family	unknown	unknown	gnl\|CDD\|273674
NZ_CP054139.1\|WP_173413663.1\|941749_942874_+\|4-hydroxyphenylpyruvate-dioxygenase	unknown	unknown	gnl\|CDD\|273528
NZ_CP054139.1\|WP_173413656.1\|932008_932569_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173413666.1\|944367_944979_+\|YdeI/OmpD-associated-family-protein	unknown	unknown	gnl\|CDD\|378058
NZ_CP054139.1\|WP_173413672.1\|951320_951866_-\|peptide-methionine-(S)-S-oxide-reductase-MsrA	unknown	unknown	gnl\|CDD\|376578
NZ_CP054139.1\|WP_173413658.1\|934094_937103_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	unknown	unknown	gnl\|CDD\|274948
NZ_CP054139.1\|WP_173417715.1\|938210_938501_+\|YXWGXW-repeat-containing-protein	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP054139.1\|WP_173413667.1\|945519_946278_-\|methyltransferase-domain-containing-protein	gnl\|CDD\|369777	pfam08241, Methyltransf_11, Methyltransferase domain. Members of this family are SAM dependent methyltransferases.	5.48354e-20
NZ_CP054139.1\|WP_173413669.1\|947525_949973_-\|beta-propeller-fold-lactonase-family-protein	gnl\|CDD\|225926	COG3391, COG3391, Uncharacterized conserved protein [Function unknown].	5.62391e-17
NZ_CP054139.1\|WP_173413665.1\|943885_944359_+\|hypothetical-protein	gnl\|CDD\|183103	PRK11370, PRK11370, YciI family protein.	1.86062e-07
NZ_CP054139.1\|WP_173413661.1\|939092_940088_-\|fumarylacetoacetate-hydrolase-family-protein	gnl\|CDD\|376566	pfam01557, FAA_hydrolase, Fumarylacetoacetate (FAA) hydrolase family. This family consists of fumarylacetoacetate (FAA) hydrolase, or fumarylacetoacetate hydrolase (FAH) and it also includes HHDD isomerase/OPET decarboxylase from E. coli strain W. FAA is the last enzyme in the tyrosine catabolic pathway, it hydrolyzes fumarylacetoacetate into fumarate and acetoacetate which then join the citric acid cycle. Mutations in FAA cause type I tyrosinemia in humans this is an inherited disorder mainly affecting the liver leading to liver cirrhosis, hepatocellular carcinoma, renal tubular damages and neurologic crises amongst other symptoms. The enzymatic defect causes the toxic accumulation of phenylalanine/tyrosine catabolites. The E. coli W enzyme HHDD isomerase/OPET decarboxylase contains two copies of this domain and functions in fourth and fifth steps of the homoprotocatechuate pathway; here it decarboxylates OPET to HHDD and isomerises this to OHED. The final products of this pathway are pyruvic acid and succinic semialdehyde. This family also includes various hydratases and 4-oxalocrotonate decarboxylases which are involved in the bacterial meta-cleavage pathways for degradation of aromatic compounds. 2-hydroxypentadienoic acid hydratase encoded by mhpD in E. coli is involved in the phenylpropionic acid pathway of E. coli and catalyzes the conversion of 2-hydroxy pentadienoate to 4-hydroxy-2-keto-pentanoate and uses a Mn2+ co-factor. OHED hydratase encoded by hpcG in E. coli is involved in the homoprotocatechuic acid (HPC) catabolism. XylI in P. putida is a 4-Oxalocrotonate decarboxylase.	8.55079e-68
NZ_CP054139.1\|WP_173413657.1\|932581_934081_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|185760	cd08977, SusD, starch binding outer membrane protein SusD. SusD-like proteins from Bacteroidetes, members of the human distal gut microbiota, are part of the starch utilization system (Sus). Sus is one of the large clusters of glycosyl hydrolases, called polysaccharide utilization loci (PULs), which play an important role in polysaccharide recognition and uptake, and it is needed for growth on amylose, amylopectin, pullulan, and maltooligosaccharides. SusD, together with SusC, a predicted beta-barrel porin, forms the minimum outer-membrane starch-binding complex. The adult human distal gut microbiota is essential for digestion of a large variety of dietary polysaccharides, for which humans lack the necessary glycosyl hydrolases.	2.76872e-35
NZ_CP054139.1\|WP_173413658.1\|934094_937103_-\|SusC/RagA-family-TonB-linked-outer-membrane-protein	gnl\|CDD\|274948	TIGR04056, OMP_RagA_SusC, TonB-linked outer membrane protein, SusC/RagA family. This model describes a distinctive clade among the TonB-linked outer membrane proteins (OMP). Members of this family are restricted to the Bacteriodetes lineage (except for Gemmatimonas aurantiaca T-27 from the novel phylum Gemmatimonadetes) and occur in high copy numbers, with over 100 members from Bacteroides thetaiotaomicron VPI-5482 alone. Published descriptions of members of this family are available for RagA from Porphyromonas gingivalis, SusC from Bacteroides thetaiotaomicron, and OmpW from Bacteroides caccae. Members form pairs with members of the SusD/RagB family (pfam07980). Transporter complexes including these outer membrane proteins are likely to import large degradation products of proteins (e.g. RagA) or carbohydrates (e.g. SusC) as nutrients, rather than siderophores. [Transport and binding proteins, Unknown substrate].	0
NZ_CP054139.1\|WP_173413671.1\|951088_951286_-\|UPF0175-family-protein	gnl\|CDD\|377095	pfam03683, UPF0175, Uncharacterized protein family (UPF0175). This family contains small proteins of unknown function.	4.22987e-06
NZ_CP054139.1\|WP_173413668.1\|946302_947169_-\|aldose-1-epimerase-family-protein	gnl\|CDD\|185701	cd09024, Aldose_epim_lacX, Aldose 1-epimerase, similar to Lactococcus lactis lacX. Proteins similar to Lactococcus lactis lacX are uncharacterized members of aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism, catalyzing the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen.	2.9965e-130
NZ_CP054139.1\|WP_173413662.1\|940493_941651_+\|homogentisate-1,2-dioxygenase	gnl\|CDD\|226039	COG3508, HmgA, Homogentisate 1,2-dioxygenase [Secondary metabolites biosynthesis, transport, and catabolism].	1.03509e-69
NZ_CP054139.1\|WP_173413670.1\|950266_951061_-\|5'-nucleotidase,-lipoprotein-e(P4)-family	gnl\|CDD\|273674	TIGR01533, Lipoprotein_E, 5'-nucleotidase, lipoprotein e(P4) family. This model represents a set of bacterial lipoproteins belonging to a larger acid phosphatase family (pfam03767), which in turn belongs to the haloacid dehalogenase (HAD) superfamily of aspartate-dependent hydrolases. Members are found on the outer membrane of Gram-negative bacteria and the cytoplasmic membrane of Gram-positive bacteria. Most members have classic lipoprotein signal sequences. A critical role of this 5'-nucleotidase in Haemophilus influenzae is the degradation of external riboside in order to allow transport into the cell. An earlier suggested role in hemin transport is no longer current. This enzyme may also have other physiologically significant roles. [Transport and binding proteins, Other, Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides].	4.92948e-85
NZ_CP054139.1\|WP_173413663.1\|941749_942874_+\|4-hydroxyphenylpyruvate-dioxygenase	gnl\|CDD\|273528	TIGR01263, 4-hydroxyphenylpyruvate_dioxygenase, 4-hydroxyphenylpyruvate dioxygenase. This protein oxidizes 4-hydroxyphenylpyruvate, a tyrosine and phenylalanine catabolite, to homogentisate. Homogentisate can undergo a further non-enzymatic oxidation and polymerization into brown pigments that protect some bacterial species from light. A similar process occurs spontaneously in blood and is hemolytic (see . In some bacterial species, this enzyme has been studied as a hemolysin. [Energy metabolism, Amino acids and amines].	3.22808e-169
NZ_CP054139.1\|WP_173413659.1\|937256_938150_+\|3-hydroxybutyryl-CoA-dehydrogenase	gnl\|CDD\|180269	PRK05808, PRK05808, 3-hydroxybutyryl-CoA dehydrogenase; Validated.	5.5597e-150
NZ_CP054139.1\|WP_173413666.1\|944367_944979_+\|YdeI/OmpD-associated-family-protein	gnl\|CDD\|378058	pfam08818, DUF1801, Domain of unknown function (DU1801). This large family of bacterial proteins is uncharacterized. They contain a presumed domain about 110 amino acids in length.	1.09898e-20
NZ_CP054139.1\|WP_173413672.1\|951320_951866_-\|peptide-methionine-(S)-S-oxide-reductase-MsrA	gnl\|CDD\|376578	pfam01625, PMSR, Peptide methionine sulfoxide reductase. This enzyme repairs damaged proteins. Methionine sulfoxide in proteins is reduced to methionine.	1.45257e-94
NZ_CP054139.1\|WP_173413664.1\|943127_943781_+\|DNA-alkylation-repair-protein	gnl\|CDD\|132880	cd06561, AlkD_like, A new structural DNA glycosylase. This domain represents a new and uncharacterized structural superfamily of DNA glycosylases that form an alpha-alpha superhelix fold that are not belong to the identified five structural DNA glycosylase superfamilies (UDG, AAG/MNPG, MutM/Fpg and helix-hairpin-helix). DNA glycosylases removing alkylated base residues have been identified in all organisms investigated and may be universally present in nature. DNA glycosylases catalyze the first step in Base Excision Repair (BER) pathway by cleaving damaged DNA bases within double strand DNA to produce an abasic site. The resulting abasic site is further processed by AP endonuclease, phosphodiesterase, DNA polymerases, and DNA ligase functions to restore the DNA to an undamaged state. All glycosylase examined to date utilize a similar strategy for binding DNA and base flipping despite their structural diversity.	1.97433e-38

>NZ_CP054139.1|WP_173413663.1|941749_942874_+|4-hydroxyphenylpyruvate-dioxygenase
MDTLIADKKLQTTDFLPLNGTDYVEFYVGNAKQAAHFYKTAFGFQNLAYAGPETGVRDRASYVLQQGKIRLMLTTPLHSDHPIAEHIKKHGDGVKVLAIWVDDAYDAFEQTTSRGAEPYQQPQTLTDEFGEVRTSGIKLYGETVHLFIERKNYNGVFLPGYEKLENNYNPTDTGLLYVDHCVGNVGWHKMNHWVNFYEEVMGFKNILTFDDKMISTEYSALMSKVMSNGNGYVKFPINEPAEGKKKSQIEEYLEFYEDEGVQHLALATHDIVKTVTELQSRGVEFLTVPTTYYDELEARVGKIDEDIEPLAKLGILVDRDDEGYLLQIFTKPVEDRPTVFFEIIQRKGARSFGAGNFKALFEAIEREQELRGNL
>NZ_CP054139.1|WP_173413662.1|940493_941651_+|homogentisate-1,2-dioxygenase
MPIYHTLGQIPHKRHTVFRKPDGGLYAEELVSTEGFSSLYSLVYHCYPPTIVKTLGEPYSVEPKIARAKYLKHTSLIGFNIKPADDYLESRKAVLVNNDLHISLAAPRKSMTDYFFKNAQADEVIFVHIGSGTLKTGFGDIKFEYGDYLVIPRGTIYQMEFNTEDNRLCIVESFGPIRTPKRYRNQFGQLMEHSPYCERDIKRPQNLQTHDEKGDFKILIKKQGLIYPYIYGTHPFDFIGWDGFHYPWGFSIHDFEPITGRLHQPPPVHQTFDGHNFVLCSFVPRKFDYHPDSIPAPYNHSNVDSDEVLYYVDGDFMSRKNVVKGQITLHPAGIPHGPHPGSVEKSIGKEATEELAVMIDPFHPLQLTEDAVNIEDEGYYHSWAE
>NZ_CP054139.1|WP_173413661.1|939092_940088_-|fumarylacetoacetate-hydrolase-family-protein
MKLVSYKTEDREHLGIFANNHIYNLNSCDKLIPDNMNAFLQGGDELMDRAKKINADIISGKLEAKEELFFELLAPVPHPASCRDGYAFRQHVAAARRNRKVDMIAEFDQYPIFYFTNHNAVQGVGEIECMPDHFQKLDFELEVAIVIGKKGRNVTAAEADNYIAGYMIMNDMSARTLQMEEMLLNLGPAKGKDFSTVIGPWLVTPDELEQYKVPAKAGHTGNNYNLAMNCSVNGIQVSAGNMADMDWTFAEIIERCAYGCDILPGDVIGSGTVGTGCFLELNGTGLLNDPNYQTQWLQAGDLVEMDITGLGVLSNVIVASKSDFSILGLKK
>NZ_CP054139.1|WP_173413660.1|938630_938834_-|hypothetical-protein
MTEPANNPNKPSPADTPTDRPNDEGHKNVVKNRDKQYHADEPEQENIAKRHENEEQPVHPVKKAPKD
>NZ_CP054139.1|WP_173417715.1|938210_938501_+|YXWGXW-repeat-containing-protein
MKTTSKLILGLALAGSMLAGCAGSYYVAEQPVEPVYTRPVAPYEGAVWVSGEWSWRGGRYVYTNGYWTRPRNNRVWVSGSWERGGNGYYWRRGHWR
>NZ_CP054139.1|WP_173413659.1|937256_938150_+|3-hydroxybutyryl-CoA-dehydrogenase
MKNITVIGSGTMGNGIAHVFAQHGFKVQLVDMKPEALDKAMNTILTNLDRQVKKGVITEDIKTDTLSNINPGTDLAAAVSNADLVVEAATENPEIKLGIFKQISDLCGPDTILATNTSSISITRIAAVTKAPGNVIGMHFMNPVPVMQLVEVIRGYATTNEVTQKVMDLSRQLNKVPVEVNDYPGFVANRILMPMINEAIYTLFEGVAGVYEIDTVMKLGMAHPMGPLQLADFIGLDVCLAILNVLYDGLGNTKYAPCPLLVNMVTAGHLGAKSGSGFYKYTPGSKELVVADKFSKG
>NZ_CP054139.1|WP_173413658.1|934094_937103_-|SusC/RagA-family-TonB-linked-outer-membrane-protein
MKKNLLNLLLLSFFAISSAFAQSRKITGSVTSADEGQPLPGVSIKIVGTNQGTQSNADGNFSLNVAAGAKSLQFSYLGYSTLTVPITSANTYTVKLQTDNKALSEIVVTGYGVQQKREVTGSIVSLKAVDIEDKPIQTMDRALQGRAAGVQVTSSSGQPGGGLSVVIRGTATINGTTQPLYIVDGVQLSTGGLSGQTSVNSLSSINPDDIESIEVLKDAASASIYGSLAGNGVVIITTKRGKAGKTTVNASAQFGEARNYNPYKTVSGADYFLLQKEAYENYNQRIGNAPGVGTAAAITASFPSGVLPANIPTYDYVKGITQTGKVGQYDLSFSGGDAKTKFFVAGSYNNTQGTIINSSFTRGTFRANVDHKVSDKFTMQAAINLTGSGEAGPSTNSGFFTNTPFTGAILTSPINPIYNADGSYNTATVGINAGNNIIQNVVQEVRTAGTFQTVSNLGLTYSILPELSFRAFGGLEFSDIRDVNYRPATIPIYAPLGSGVETYRRNINYNTSGTFNFTKKFGEHNFSAIAGFEYRSVTNRVESASSQGFPSPLLILVSSGSTPTAATSTFTGYRVAGFLGNAKYDYKGKYLFSANIRRDGSSRFGPNKKYGTFYGFSGGWNMMSESFMNNVKFISQLKPRVSYGVTGSQPTTDFTGLSLYGGGGQYGAPLAGGLRPAQLANPDFTWEKSTQIDLGLDYGFFNNRITGQFDIYRKKNTDLILGLTLPGDSGFTSYTVNAGAAQSEGIELQISSVNVDGPFKWTTNFNISWNRTKLLQLVNGLQQTGTFTYTVGSPLQNIYTQQWAGVNPADGRAMYYDINGNITYAPKTTDQRIIGNQLPRFYGGFGNTFTYAGFNLDVLLQYQYGNKSYLQTQQYLETSGDLANNQAASQLTRWTTPGQITSVPRPYVGSTGAEPGGVSVQTLSSRFVEDASYIRLKQVTLGYKLPKSVTDKVKVGSVSLFLQALNLATITHYRGDDPENTGNNLNFYPNARTLTAGINVKF
>NZ_CP054139.1|WP_173413657.1|932581_934081_-|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MNKKIFVVSLIIMLSSSFTACKKILDIQPQNQISTEAALKDVSGYYALLISVYDRMQSYTFWGRDMALEGDALADNIYTVTALAGGRYTTVNTNTRGAHYNIWTQAYAAINDLNNIIAGIDAAPAVGNTQLLQQAQVKAEAYALRGMIYFDIARVYGFEPNKVPTTGTDASFDKSAVIRLTPTTSFDQASSINRSTITQTYTQIESDLNKAIATFKASYSFTTVKKPTNPYHINESATHAFLGKLYLYWEKYPQAVTEFDNALDPTITPSTLAPITAGTYNAAFKKIPNPESLLELYYNQSVEVVGVTGSNDAPFTYTQPTGYNAANVATFAGQTASAELVALFEANDDRKGMFFNSRTTTNTNVYTWANKYSGAGGAFTDNILMMRYSDIILMKAEALANQTQYVAAAALVTTLRTARNATLAVPTDASLLTFIQTERRRELFFEGHRWFDLKRLGNGITKPALTAVGTIAATDYRLLAPLPTAEVTLNPALPQNPNY
>NZ_CP054139.1|WP_173413656.1|932008_932569_-|hypothetical-protein
MKMKKYIVYSILGVALCGLITGCLPEKAETGLTYKGPAVVEVKNQTLGQLTAQLTARGIYTTTAQTDSSRTVLINSRPTDSILVQLVGPQSSSPIDINYTVRGTVPASAPVGTTLAVEGTNYNFRTVGARKVTFAPNTSQAYILVDIIPNSITTVGQQRILTIDITGNAQIAPSANYSKFLLMLRR
>NZ_CP054139.1|WP_173413655.1|931292_931919_-|hypothetical-protein
MKNLLKATAMLLLFFAVDCKAQGNMVTDINGRPYRTKAYDDIEGSPYLYDAWMPGTVKMNYGSVYTNISLKLNEQEGKLYFKGKNDEVLEFVDPVTEFTLNGMHFIAEAGTFYQVLADGSTKLLKQPVKEIQETKTYGSAVASKTFIAADKYFVMSNGKLTAVKKDKKAILAALAGKQAEVEAYMKKESLNFKNDADLAKLFIYYNSL
>NZ_CP054139.1|WP_173413664.1|943127_943781_+|DNA-alkylation-repair-protein
MTLTAALEHLKEHASPQYLAGMSRFGIDNSKALGVKLPVIRKLAKVIKKDQQLSLELWATDIHEARLLATMIGDPAQVSPQQMDTWAGDFSTWDVCDQACGNLFIRTPFVLDKIREYCTSDQEFVKRCGFVLMAEYAVHLKKATDDVFLSFLPIIEREAWDNRNFVKKAINWALRQIGKRNTLLKHTAIDTADRILEQDIKAARWIAKDALRELHNR
>NZ_CP054139.1|WP_173413665.1|943885_944359_+|hypothetical-protein
MKKLLILAFAAFTYCGSFAQTTTAKPNPEYDAALAKKLGADEYGMRKYVMAFLKTGPTKIADKAKSAELQKAHLKNITKLADEGKLVVAGPFMDPGEVEGIFIFDVSTIAEAKALTETDPAIKAGVLVMELRPFYCSAALMEVAKTHKKLAKKNFAD
>NZ_CP054139.1|WP_173413666.1|944367_944979_+|YdeI/OmpD-associated-family-protein
MENTEPKVDAYIAKSPAYAQPIITHLRKLIHQVTPQVTEVMKWGHPHFDYKGPFMGLAAFKEHLGLNFWKSTLMDDPAGLFAAAEKGSAGSIGKIRSMADLPADDVLITYMLNAIDLNEKGIKLPPPKKTEEPKELEMPTDLIEAFKSNTGTLQHFEKFSPSAKKEYISWLDEAKSEATRQKRLDTMMEWVAEGKTRHWKYKK
>NZ_CP054139.1|WP_173413667.1|945519_946278_-|methyltransferase-domain-containing-protein
MTGSTQRFTNRVDNYTKYRPGYPNAVLQLLRTSGHLSANAVVADVGSGTGIFTKLLLDEGYTVYAVEPNGAMRQAADDSLGGDKKYHSINGTAEATTLKAHSADMVVCAQAFHWFDAHKTKAEFARVLKPGGNVALIWNNRQVEVDEFSINYELLLQQQASDYKRVNHQNLTEANFNAFFKDGKYQLTRFPNTQVFDMEGLAGRAFSSSYVPSEETPEGALFLKKLQELFDRHQNNGTVNMEYQTEVYLGEV
>NZ_CP054139.1|WP_173413668.1|946302_947169_-|aldose-1-epimerase-family-protein
MIIIENEFLKAAIDTKGAQLSSLINKETGVEHMWQAGEAWPWHSPNLFPVIGTLIDNQIIVDGKPYEITQRHGFARYSEFLLIESDSNHAKFSLPYSETTMAMYPYKFDLHIIYDLIDNSLRVTFKVLNRDDKTIYFSVGGHPAFNVPFHPGENYDDYYLEFETEEQLTEHLLSPEGVFSGETRPLKLDGKNLQLTHELFANDALVFKHMKSRQVTIKSHKHDESLTVQFPHFQYLGIWAKTNADFVCIEPWLGHADTAGQHVEFKNKEGVQKLVHGHVFDASYYISI
>NZ_CP054139.1|WP_173413669.1|947525_949973_-|beta-propeller-fold-lactonase-family-protein
MLRKLFTAALAIAGLVQITIAQTPGKVSGTDQVLLPNGWKLSPAGHNSLPLGDLPLNIQLSSSGKLMAVTNNGQSTQSVQLIDAKSQKVLDTKIINKSWYGLAISNDEKKIYASGGNNNCIVVYPIENNKLGKADTITLGKPWPANKICATGLALKKDNSVLYAVTKEDNTLYTIDPANKSITGRVKLAAEAYSCLLSPDEKKLYISLWGGEEVAIYNTVSGKIENSIKVGNHPNELLLNKKGTLLFAANANDNSVSVINTQSNKVLETVSTALYPTKLTGSTSNGLALSPNEKTLYIANADNNCLAVFDLSNPGHSQSMGFIPVGWYPTNVKTLGNQIIVSNGKGFTSMANPNGPQPVSKTDNSGHHIGSTNSREQYIGGLFKGTMSFINAPTADQLKAYTKQVYANTPFTNDKVNLADGLAGNPIPRKVGDKSPIKHVFYIIKENRTYDQVLGDMKQGNGDSALCIFPRKVTPNLHAIASNYVLADNFYVDAEVSCDGHNWSMAAYATDFIEKTWPTSYGGRGGNYDGEGTRKIGDPRDGYIWDYCKRAGVSYRTYGEFAENGKANIKSLQGHLCPQSPGFTLDIKDVLRESIWEHDFDSLLKINAVPQFNTVRLGNDHTSGQRKGKISPIAAVADNDLAVGQFIDHLSHSPIWKESVVFILEDDAQNGPDHVDAHRSPVYVVGPYVKRNAVVHGMYSTSGVLRTMELILGLPPMSQYDAAAMPLYECFTSKPDFTPYTAKSAEVDLEQRNVAVNESSRRSELWNLAKEDAAPDIELNEVVWKYVKGEASVMPAPKRSAFVILEKKKKKDDDD
>NZ_CP054139.1|WP_173413670.1|950266_951061_-|5'-nucleotidase,-lipoprotein-e(P4)-family
MKIKYPIAALLLCFAINSFAQAPNLSTANAGKLWASLYQQRAAEYKALCFQAYNIARLRIDEAVKHKGTKPLAVVTDIDETLLDNSPEDARAAINNQEFDAKAWKKWTAQGIADTVPGAPSFFKYAAAKGVKVFYITNRDEDERAGTLKNLQLYHLPFADDAHLILKTTTSSKETRRQEVLKKYNIVLLCGDNLADFDALYDNHPSEENREATTQKLRKQFGTKYIVLPNPGYGDFEGALFKFNYKLTPAQKDSVIRANIKLAQ
>NZ_CP054139.1|WP_173413671.1|951088_951286_-|UPF0175-family-protein
MNINLPDGVKISEKDVLTAVATRLYDTGKLSIEQAANMAGYNLSAFIEELTAQSLKENSAVMYHY
>NZ_CP054139.1|WP_173413672.1|951320_951866_-|peptide-methionine-(S)-S-oxide-reductase-MsrA
MNIQKATFGNGCFWCTEAIFQILKGVIKVRSGYTGGHTINPTYMEICNGDTGHAEVIDIEFDADAISYDELLLAFFKSHNPTTLNRQGNDVGTQYRSAIFYHSEEQKQQAEQMIKKLTDEKVFDRPIVTEVTPASEFYKAEDYHQNYYNDNTLKPYCMVVIQPKLNKFIKEFVEKIKPEVL
>NZ_CP054139.1|WP_173413673.1|951948_954408_+|hypothetical-protein
MMFKLAMRMAILILLTIGNMVVRAQGNNPMVDSILKHAAYYHVKNPVSLMFVHLDKTVYVNNDMMWFTAYLLGVKAHEAAGHQVLSAALVNNNDQKIAVQGRFVMSRGLAYGNMMIPDSVPPGHYSFVAYTNRMLNGKPQVCFVQAITLKTVTEPNFNVELALDTMYHDPANMRVLLKADSRSTPLDGASVSYFLGKNAKTRVAGKAKTNVIGSYTIMLPRDRINATQHNLEVQVKSGADVKTLHLDIPVKRPAVAIGFYPEGGHLIENIVSRVGWEVKTPGGTAIKTDAVLYINGNPADTIHTDSFGMGVFSINPQVNATYAVKLLDNDYDTELHPLPAALKAGVVVRVADAIINDSLRLQLRAQQVGRVTLLVHNYRQVYSATPLTVSQAARGVKVDMSAIPRGISCITVLDSLNRPCAERLFFAHYNQRPRLSINIDNTDPLLRQKVSVKLKLNENNGHPQQGIVSVACVQDSRFEVKNDNNIENYVYLQSEIDDLPVKERLMGSAELDLQYLNELLLIRGWSKYKWLDMMKTSEADTIIRNDSLFYAGTITHFGNKLKKPVEVLLMKDSSAMNMIASTATGGFTLANNQLYTPADKKVHLIVSGSSSDYLIDVADPYPDRNKQLAKDIEPVMFEPPIVQSTKELVLKGFEHTTHLKEVVIKSSNSRNFKHGFAVNANACGDYVCPYHILNCPNHTSDPGNHAPQQGEMVHMGGQGLTPYYGCSDEVPKGGMLIFQGIYAAREFYGADYAKINPTEPDYLSTICWKHGVGISSEKETEISFYTSDITGKFRIVVQGITNSDVVYGEDSFTVRKKSP

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Crispr_ID: NZ_CP054139_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP054139_5

2887151-2887266

Orphan

Consensus_repeat	Method
TTGGTGGTGTCTTTTTTCATTTTAGACAT	CRISPRCasFinder

1 spacers

csa3

The CRISPR arrays of NZ_CP054139_5

>merge|NZ_CP054139|5|2887151-2887266|CRISPRCasFinder
TTGGTGGTGTCTTTTTTCATTTTAGACATCTTCTTATCCATTTTCTTGTCCATTTTTTTGTGATCCATTTTAGACATTTTCGACATCTTGGTGGTGTCTTTTTTCATTTTAGACAT

>NZ_CP054139|5|4|2887151-2887266|CRISPRCasFinder
TTGGTGGTGTCTTTTTTCATTTTAGACAT	CTTCTTATCCATTTTCTTGTCCATTTTTTTGTGATCCATTTTAGACATTTTCGACATC
TTGGTGGTGTCTTTTTTCATTTTAGACAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP054139.1\|WP_173415165.1\|2885510_2886080_-\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|274359
NZ_CP054139.1\|WP_173415176.1\|2891799_2892360_+\|DUF4256-domain-containing-protein	unknown	unknown	gnl\|CDD\|339073
NZ_CP054139.1\|WP_173415174.1\|2890818_2891202_+\|DoxX-family-protein	unknown	unknown	gnl\|CDD\|379266
NZ_CP054139.1\|WP_173415172.1\|2890013_2890337_+\|metalloregulator-ArsR/SmtB-family-transcription-factor	csa3	COG0640_csa3_CAS-I-A	gnl\|CDD\|238042
NZ_CP054139.1\|WP_173415166.1\|2886104_2886488_-\|thioredoxin-fold-domain-containing-protein	unknown	unknown	gnl\|CDD\|234717
NZ_CP054139.1\|WP_173415167.1\|2886484_2887093_-\|redoxin-domain-containing-protein	unknown	unknown	gnl\|CDD\|239268
NZ_CP054139.1\|WP_173415169.1\|2887451_2887907_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_CP054139.1\|WP_173415170.1\|2888317_2888965_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|236766
NZ_CP054139.1\|WP_173415164.1\|2885217_2885514_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173415162.1\|2883775_2884552_-\|molybdopterin-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|239026
NZ_CP054139.1\|WP_173415160.1\|2881756_2882239_+\|RecX-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|376870
NZ_CP054139.1\|WP_173415171.1\|2888969_2889497_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|379112
NZ_CP054139.1\|WP_173415175.1\|2891207_2891786_+\|YdeI/OmpD-associated-family-protein	unknown	unknown	gnl\|CDD\|226851
NZ_CP054139.1\|WP_173415161.1\|2882840_2883779_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|182510
NZ_CP054139.1\|WP_173415163.1\|2884535_2885231_-\|cytochrome-b/b6-domain-containing-protein	unknown	unknown	gnl\|CDD\|226602
NZ_CP054139.1\|WP_173414268.1\|2893046_2894498_-\|IS1182-family-transposase	unknown	unknown	gnl\|CDD\|377531
NZ_CP054139.1\|WP_173415159.1\|2879237_2881697_-\|bifunctional-UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine-ligase/alanine-racemase	unknown	unknown	gnl\|CDD\|237026
NZ_CP054139.1\|WP_173415173.1\|2890344_2890812_+\|SRPBCC-domain-containing-protein	unknown	unknown	gnl\|CDD\|176868
NZ_CP054139.1\|WP_173415158.1\|2878626_2879226_-\|DUF502-domain-containing-protein	unknown	unknown	gnl\|CDD\|225480
NZ_CP054139.1\|WP_173415177.1\|2892482_2892824_+\|potassium-transporter-KefB	unknown	unknown	unknown

Protein	Function_ID	Function_description	E-value
NZ_CP054139.1\|WP_173415165.1\|2885510_2886080_-\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|274359	TIGR02943, RNA_polymerase_sigma-24_subunit_RpoE, RNA polymerase sigma-70 factor, TIGR02943 family. This group of sigma factors are members of the sigma-70 family (TIGR02937). They and appear by homology, tree building, bidirectional best hits and one-to-a-genome distribution, to represent a conserved family.	3.44712e-41
NZ_CP054139.1\|WP_173415176.1\|2891799_2892360_+\|DUF4256-domain-containing-protein	gnl\|CDD\|339073	pfam14066, DUF4256, Protein of unknown function (DUF4256). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are approximately 190 amino acids in length.	1.07999e-136
NZ_CP054139.1\|WP_173415174.1\|2890818_2891202_+\|DoxX-family-protein	gnl\|CDD\|379266	pfam13564, DoxX_2, DoxX-like family. This family of uncharacterized proteins are related to DoxX pfam07681.	1.2518e-18
NZ_CP054139.1\|WP_173415172.1\|2890013_2890337_+\|metalloregulator-ArsR/SmtB-family-transcription-factor	gnl\|CDD\|238042	cd00090, HTH_ARSR, Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions.	1.14523e-17
NZ_CP054139.1\|WP_173415166.1\|2886104_2886488_-\|thioredoxin-fold-domain-containing-protein	gnl\|CDD\|234717	PRK00293, dipZ, thiol:disulfide interchange protein precursor; Provisional.	1.56236e-20
NZ_CP054139.1\|WP_173415167.1\|2886484_2887093_-\|redoxin-domain-containing-protein	gnl\|CDD\|239268	cd02970, PRX_like2, Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.	5.99155e-34
NZ_CP054139.1\|WP_173415169.1\|2887451_2887907_+\|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.	1.58084e-12
NZ_CP054139.1\|WP_173415170.1\|2888317_2888965_+\|hypothetical-protein	gnl\|CDD\|236766	PRK10811, rne, ribonuclease E; Reviewed.	0.00714979
NZ_CP054139.1\|WP_173415162.1\|2883775_2884552_-\|molybdopterin-dependent-oxidoreductase	gnl\|CDD\|239026	cd02108, bact_SO_family_Moco, bacterial subgroup of the sulfite oxidase (SO) family of molybdopterin binding domains. This domain is found in a variety of oxidoreductases. Common features of all known members of this family, like sulfite oxidase and nitrite reductase, are that they contain one single pterin cofactor and part of the coordination of the metal (Mo) is a cysteine ligand of the protein and that they catalyze the transfer of an oxygen to or from a lone pair of electrons on the substrate. The specific function of this subgroup is unknown.	2.61508e-40
NZ_CP054139.1\|WP_173415160.1\|2881756_2882239_+\|RecX-family-transcriptional-regulator	gnl\|CDD\|376870	pfam02631, RecX, RecX family. RecX is a putative bacterial regulatory protein. The gene encoding RecX is found downstream of recA, and is thought to interact with the RecA protein.	3.36281e-21
NZ_CP054139.1\|WP_173415171.1\|2888969_2889497_+\|GNAT-family-N-acetyltransferase	gnl\|CDD\|379112	pfam13302, Acetyltransf_3, Acetyltransferase (GNAT) domain. This domain catalyzes N-acetyltransferase reactions.	1.61658e-21
NZ_CP054139.1\|WP_173415175.1\|2891207_2891786_+\|YdeI/OmpD-associated-family-protein	gnl\|CDD\|226851	COG4430, COG4430, Uncharacterized protein conserved in bacteria [Function unknown].	7.73711e-80
NZ_CP054139.1\|WP_173415161.1\|2882840_2883779_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|182510	PRK10514, PRK10514, putative acetyltransferase; Provisional.	1.47376e-29
NZ_CP054139.1\|WP_173415163.1\|2884535_2885231_-\|cytochrome-b/b6-domain-containing-protein	gnl\|CDD\|226602	COG4117, COG4117, Thiosulfate reductase cytochrome B subunit (membrane anchoring protein) [Energy production and conversion].	2.33491e-27
NZ_CP054139.1\|WP_173414268.1\|2893046_2894498_-\|IS1182-family-transposase	gnl\|CDD\|377531	pfam05598, DUF772, Transposase domain (DUF772). This presumed domain is found at the N-terminus of many proteins found in transposons.	1.53353e-15
NZ_CP054139.1\|WP_173415159.1\|2879237_2881697_-\|bifunctional-UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine-ligase/alanine-racemase	gnl\|CDD\|237026	PRK11930, PRK11930, putative bifunctional UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine ligase/alanine racemase; Provisional.	0
NZ_CP054139.1\|WP_173415173.1\|2890344_2890812_+\|SRPBCC-domain-containing-protein	gnl\|CDD\|176868	cd07826, SRPBCC_CalC_Aha1-like_9, 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.	4.51158e-21
NZ_CP054139.1\|WP_173415158.1\|2878626_2879226_-\|DUF502-domain-containing-protein	gnl\|CDD\|225480	COG2928, COG2928, Uncharacterized conserved protein [Function unknown].	4.68281e-29

>NZ_CP054139.1|WP_173415167.1|2886484_2887093_-|redoxin-domain-containing-protein
MKKIFTLILLFGIAFTTALAQAVSYPAKPTDISPLLIGEAIPAVKVPAANGQVFDLNARIAEKPTILIFYRGGWCPYCNKELAGLQKAQADLVKLGYQLIAISTDSPENLNKSITKHQLGYTLLSDADLAVSKQFGLAYQAPAAYAKTIAEGSAGKNTDKLLPVPSVFILDQKGKIQFEYINPDFTQRISPALLTAAATALK
>NZ_CP054139.1|WP_173415166.1|2886104_2886488_-|thioredoxin-fold-domain-containing-protein
MIRLATILLLLTAFAEARFTESDISTALAKAKKAHRPVFVDAYASWCAPCKELRKTTFKNKRVAAYLNNHYINAAIDVEKGNGMQFAEKYHIESYPTLLLIDENGKEVKRIEGFVDATELAQKLDMK
>NZ_CP054139.1|WP_173415165.1|2885510_2886080_-|sigma-70-family-RNA-polymerase-sigma-factor
MPETVTIQDKELLQPQLWVSRYADYLYSYALSRLNDEELAQDLVQETFLAALEKISNFRGESSERTWLTAILKFKVIDVYRKQSRTAGTVNEETEFFESGLHHWKKEHWPLPFGVEDQDPLHNKEFMGVLQKCMQRLPPLWLSVFRMKHLDEEGTEQICEALKLTSSNFWVIIHRAKVNLRSCLQKNWL
>NZ_CP054139.1|WP_173415164.1|2885217_2885514_-|hypothetical-protein
MKKGTNNPLKSIAYNCRRATLLIEKKQSVSLSLREKLELKIHLAGCSICRTYERQSILISQMMHRLFNNKPTGELRLDPDFKAAMQKKIEEKLSDESH
>NZ_CP054139.1|WP_173415163.1|2884535_2885231_-|cytochrome-b/b6-domain-containing-protein
MKAIKEKHPLVMRWTHWINFPLLGIMIWSGLLIYWANDVYTVTIFGHTFVRFFPQWFYDALHIPQRLSEGMAFHFLFMWFFTLNGIFYVLYTAISGEWRHLLPNKHSFKEAWLVLLHDLHIKKTAPPQGKYNAAQRIAYTAIILMGAGSVLTGLAIYKPVQFNWLTWLMGGYHLARIWHFVLTLGYVFFFLVHVIQVVLAGWNNFRSVISGFEVIRQHEPKINIETDEKES
>NZ_CP054139.1|WP_173415162.1|2883775_2884552_-|molybdopterin-dependent-oxidoreductase
MKKKAKVSLTIDQRIKRRNFISFGVFGAMGAAAYGGWKWLYNAPQEVPGVTAGTRAPLRRALNKTELFFRRLTFNENHLVKTYPVEMAVKTVRHNEDIGSDSTIDFDQWKLEVIKNNGQKLYVDLDQIKALPKTDLVFDFKCVEGWDQIQHWGGLLMRDFVRHFGLDEETSLDYMGLTTPDKQYYVGLDMPSAMHPQTLLAYEMNGKPLPPQHGKPLRLIIPVKYGIKNLKRIGSMTFSNQRPPDYWAEQGYDYYSGL
>NZ_CP054139.1|WP_173415161.1|2882840_2883779_-|GNAT-family-N-acetyltransferase
MMHHAISQLLPGEHQRLMEVWEASVRATHHFVKEEKIQLLKSLIEEHKYFEQPGIFCIRNNAGDITGFAGVSGNSLDMLFLHPSVIGIGVGGALMRHAIDHYKVTKVEVNEQNQQALGFYQHFGFSITGYSETDSNGEPFPLLYLERQPLEINRIGISGLDELISICQRSYYETFFEAFGDAEAYQNFTRELFNRARLLAELSNPAVIFYLASYNGQTAGYLKLCLDEMKTEIDSIYVLGTYQKLGIGKALIAHALGVAKNRASTELILRVWDQNQQAICFYERQGFVRSSEIRYQVMGDPQVDILMRLAIL
>NZ_CP054139.1|WP_173415160.1|2881756_2882239_+|RecX-family-transcriptional-regulator
MEPAKTRKITDETAALAKAEAFCAYQERAQQEVRDKLYEWGLWPDAVEHIIIKLIGSNFLNEERFAYAYTSGKFNQKGWGKNKIKQGLKFKKVSDVLIRKALSRIDADDYITSLEKLLQKKAAQLNEKDEYKRHYKLKQYAMSRGYENDLICDVLKDSVL
>NZ_CP054139.1|WP_173415159.1|2879237_2881697_-|bifunctional-UDP-N-acetylmuramoyl-tripeptide:D-alanyl-D-alanine-ligase/alanine-racemase
MANGIYTTSLIGQILNANEIIVNDGPVSTLLTDSRRIANAPEALFFALSNRRDGHEFIAEAYEGGVRNFVVRSAPAEPLINANYLIVPDVLAALQTIAAHHRAQFDLKVIGITGSNGKTMVKEWLYQLLSPEHNIVRSPKSYNSQIGVALSVWNITADNDMGIFEAGISTVNEMDKLQPMIMPEIGILTHMGSAHDEGFKDRREKVNEKLKLFKDCKLLIGEYELLLDHKKQNQEQHHFCWSRKFNSASLYVFSETSISGNYYMRAMYNKQEIECLVPFLDQASVENAITCWATLLALGYSPAVIDERMERLAPVSMRLELKNGINDCSVIDDSYNSDIQSLEIALNFLDQQNQHPKKTLVLSDIYQSGLSRDNLYRQVANMLNDKKIDRFIGVGEALQHYKDWFHVTEKHFYKDTYDMLVDIHRLNFKDETILLKGARNFEFERISRALVQKSHETVMEINLNALLNNLNYYKSQLQPGVKLMAMVKAFSYGSGTFEIANLLQYHKVDYLAVAYIDEGVALRQAGITLPIMVLNPEATAFDKLTEFKLQPEIYSFGLLAEFVNYLQVNDIINYPIHIKIDTGMHRLGFEGFEIEPLCDLLEDNPYIKVRSVFSHLAASDAEEHDTFTMKQIRRFEKAFKQIEQTLDYKVIKHIANTSAITRWKVAQFDMVRLGIGLYGIDSAVTDPNALESVATLKTSISQVKKIKAGETVGYNRNGSLKKDGRIATVRIGYADGYLRAFGNGVGKMLVKGMLVPTVGNIAMDMCMIDVSEVDVKEGDEVIIFNGDQRIEELAKQISTIPYEILTNISQRVKRVYFYE
>NZ_CP054139.1|WP_173415158.1|2878626_2879226_-|DUF502-domain-containing-protein
MLRRIARALLRYFIKGLLVVVPLGAACLLVYWAVASVDNALNLSDILWVNPKTGKPTYIPGTGILTVVIVILIAGILVTNVITDPIKRWWYRWLNRLPLFKFLYFSIKDLTEAFVGDEKKFNEPVLVDVNEFGLKKVGFLTQKDLKSINLPGMVAVYFPYSYSFAGQVVIIEAEKVKPLDMKAADAMKFVISGGVSGMH
>NZ_CP054139.1|WP_173415169.1|2887451_2887907_+|GNAT-family-N-acetyltransferase
MMYTRLLKKHEQLPYNLLLLADEEMQAIERYIHQSAVYVVEQDDLAIGVYALYPVDERVAEIKAIAVAEEFQNRGIGRFLLRDAEEKAREQGYTELIIGTPDIAVKQLAIYEKAGFERYEIKKNFFIDYYTAPIFEDGVQLSDMAMLRKLL
>NZ_CP054139.1|WP_173415170.1|2888317_2888965_+|hypothetical-protein
MMDKMKITEFEAGVLDAVLETCGDMEKLDRGQLLEIFDGDEELAASMVNLLIDAGLVEPDGLTTAELLPAWITREPEAEPFLAAGGFSTQFIKSVPHEKREIAFEIEVAEAPAEVIPIAEPLPTVPSPVATIAATEPVHTPVQSKDTTSDELTLLHREIEHLRKSEMFAEHKLREKEMQLQSLQSANKQLLNIRLFIWVLLGFIALLLILLFIRK
>NZ_CP054139.1|WP_173415171.1|2888969_2889497_+|GNAT-family-N-acetyltransferase
MNLQPILANDTVILQPLEAGDFDELYRVASDPAIWAQHPNKDRWQEPVFRNFFEGAIQSRGAFKIIEKATGQVIGSTRFYDHHEKDDEIFIGYTFYATAYWGTGINPMVKALMLDYAFGFVSKVLFHIGAENRRSQIAIGRLGAMKIAEEEVPYFGEAPKLNFVYKIDKAIWLQK
>NZ_CP054139.1|WP_173415172.1|2890013_2890337_+|metalloregulator-ArsR/SmtB-family-transcription-factor
MNLRRDVFQAIADPTRRAILLLLASQSLTAGAIAANFDTARPTVSKHLQILTECELLKQEQTGREIHYHINATNMKEIADFIEPFRQMWEERFNKLENIMKNYKPKK
>NZ_CP054139.1|WP_173415173.1|2890344_2890812_+|SRPBCC-domain-containing-protein
MELKTKIHAEEGRQDLTITREFDLPLELLFKAYEEAEIVEQWMDNKVLKLENKQHGGYRFEKRDANGNVVFSANGTIHDFVPNQKIIRTFEMENAPFGVQLEFLEFEKLTDSTSKLSIHTIYRSGVLRDQLLKLPFAQGINMAHNRLQDIVNKLK
>NZ_CP054139.1|WP_173415174.1|2890818_2891202_+|DoxX-family-protein
MEKKKLIVYWIATALLSVGMLGSGIGQLIRTKEMVDILSHLGYPVYLMTILGIWKILGVIVILMPGFKLVKEWAYAGFFFTMTGALISHLIMGDTGKAVAGPLMQTIFVILSWYFRPVNRKIDTPNK
>NZ_CP054139.1|WP_173415175.1|2891207_2891786_+|YdeI/OmpD-associated-family-protein
MNPKVNFYFDKEQKWQEEVNKLRMIALDCGLTEELKWGCPCYTHNGSNIVLIHDFKEYCAFLFFKGALLSDAHHILIQQTENVQAARQARFTSAEEIVKLAPTLKAYIHEAIEVEKAGLKVELKKTKEFPVADEFQYKLDHFPALKTAFEALTPGRQRGYLLYFSAPKQSKTREARIDKYIPHILEGKGLDD
>NZ_CP054139.1|WP_173415176.1|2891799_2892360_+|DUF4256-domain-containing-protein
MNDKQLSVQIQEELLSTLKARFEKNMNRHKGIDWNNIQEKLKANTEKLWSLNEMETSGGEPDVVGYNDKTGEYIFYDCSAESPKGRRSFCYDRAALDSRKEYKPENNAVGAAAAMGINLLTEGQYRGLQQLGNFDTKTSSWVLTPADIRDLGGALFCDRRYNNVFLYHNGAESYYAARGFRGCLSV
>NZ_CP054139.1|WP_173415177.1|2892482_2892824_+|potassium-transporter-KefB
MMTHANNLTIQPINRAALIKRMLIGGGIAFVLIALLVLPIRNPKPEWGELWMIRPFIITPLAGAAGGAFNYLMNNTFALTGWKKVLALVISILGFVIAIWLGIVLGLAGTLWN
>NZ_CP054139.1|WP_173414268.1|2893046_2894498_-|IS1182-family-transposase
MLIQQQQIQFSAYSGLYDLIVPKDNLLRKINDLIDFTFIYEELISKYCTTNGRTAESPVRMFKYLLLKTIYTVSDVDVVERSQYDMSFKYFLEMSPEEGVIDPSSLTKFRKLRLKDNDLLNLLINKTVTIAIEKGIIRSKSITVDATHSLSRSNPYSALEVLRERSKRLRKAVYAIDEDMKAGMPEKNTTDELEKELAYCSALEKYIEADPPLSQIPAVKEKLNLLKETVADTQEHYTLSKDKDAKTGHKSADSSFFGYKTHLAMTEERIITAAVVTSGEKGDGPELPKLLEISQQNGIDVKTIIGDSAYSGKENLEMTNEQDIKLVAKLNPSITQGFRKDENKFDYNKDADRFVCPAGHLAIRKARGGKKDIGENQVDTYYFDVEKCKVCPLRDGCYKPGAKTKTYSVSIKSGLHQQQMAFQETDEYKQSSKHRYKIEAKNSELKNAHGYDRAIAYGIENMQMQGALAIFTVNLKRIIKLMS

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Crispr_ID: NZ_CP054139_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP054139_6

3896367-3896493

Orphan

Consensus_repeat	Method
TGTAGAGACACGATACTTCGTGTCTC	CRISPRCasFinder

2 spacers

The CRISPR arrays of NZ_CP054139_6

>merge|NZ_CP054139|6|3896367-3896493|CRISPRCasFinder
TGTAGAGACACGATACTTCGTGTCTCCCCGTTGAAAATTATACGTTATGGCAATGTAGAGACACGATACTTCGTGTCTCTTTTTGTTTTTTGGATCTCCATAAGAGAGACACGAAGTATCGTGTCTC

>NZ_CP054139|6|5|3896367-3896493|CRISPRCasFinder
TGTAGAGACACGATACTTCGTGTCTC	CCCGTTGAAAATTATACGTTATGGCAA
TGTAGAGACACGATACTTCGTGTCTC	TTTTTGTTTTTTGGATCTCCAT
AAGAGAGACACGAAGTATCGTGTCTC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP054139.1\|WP_173415892.1\|3893724_3894327_-\|sigma-70-family-RNA-polymerase-sigma-factor	unknown	unknown	gnl\|CDD\|274357
NZ_CP054139.1\|WP_173415903.1\|3906967_3908869_-\|acetate--CoA-ligase	unknown	unknown	gnl\|CDD\|234677
NZ_CP054139.1\|WP_173415890.1\|3890296_3891337_-\|SUMF1/EgtB/PvdO-family-nonheme-iron-enzyme	unknown	unknown	gnl\|CDD\|335469
NZ_CP054139.1\|WP_173415898.1\|3901367_3902594_+\|imidazolonepropionase	unknown	unknown	gnl\|CDD\|236478
NZ_CP054139.1\|WP_173415899.1\|3902706_3904350_+\|glutamate-formimidoyltransferase	unknown	unknown	gnl\|CDD\|131079
NZ_CP054139.1\|WP_173415889.1\|3888853_3890287_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|226064
NZ_CP054139.1\|WP_173415891.1\|3893286_3893733_+\|MarR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197670
NZ_CP054139.1\|WP_173415895.1\|3897554_3898061_+\|MarR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197670
NZ_CP054139.1\|WP_173415896.1\|3898057_3899617_+\|histidine-ammonia-lyase	unknown	unknown	gnl\|CDD\|236484
NZ_CP054139.1\|WP_173415894.1\|3896502_3897348_-\|esterase-family-protein	unknown	unknown	gnl\|CDD\|223700
NZ_CP054139.1\|WP_173415902.1\|3906155_3906833_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173415885.1\|3885493_3885709_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173415886.1\|3885790_3886504_+\|2-C-methyl-D-erythritol-4-phosphate-cytidylyltransferase	unknown	unknown	gnl\|CDD\|234670
NZ_CP054139.1\|WP_173417830.1\|3891531_3893010_-\|sulfatase-like-hydrolase/transferase	unknown	unknown	gnl\|CDD\|293755
NZ_CP054139.1\|WP_173415893.1\|3894801_3896355_+\|carbohydrate-binding-domain-containing-protein	unknown	unknown	gnl\|CDD\|379528
NZ_CP054139.1\|WP_173415888.1\|3887925_3888840_-\|TIM-barrel-protein	unknown	unknown	gnl\|CDD\|224007
NZ_CP054139.1\|WP_173415887.1\|3886616_3887924_-\|Gfo/Idh/MocA-family-oxidoreductase	unknown	unknown	gnl\|CDD\|223745
NZ_CP054139.1\|WP_173415901.1\|3905771_3906134_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173415900.1\|3904891_3905641_+\|HAD-IIB-family-hydrolase	unknown	unknown	gnl\|CDD\|319784
NZ_CP054139.1\|WP_173415897.1\|3899594_3901268_+\|urocanate-hydratase	unknown	unknown	gnl\|CDD\|235448

Protein	Function_ID	Function_description	E-value
NZ_CP054139.1\|WP_173415892.1\|3893724_3894327_-\|sigma-70-family-RNA-polymerase-sigma-factor	gnl\|CDD\|274357	TIGR02937, RNA_polymerase_sigma_factor, RNA polymerase sigma factor, sigma-70 family. This model encompasses all varieties of the sigma-70 type sigma factors including the ECF subfamily. A number of sigma factors have names with a different number than 70 (i.e. sigma-38), but in fact, all except for the Sigma-54 family (TIGR02395) are included within this family. Several Pfam models hit segments of these sequences including Sigma-70 region 2 (pfam04542) and Sigma-70, region 4 (pfam04545), but not always above their respective trusted cutoffs.	5.3249e-28
NZ_CP054139.1\|WP_173415903.1\|3906967_3908869_-\|acetate--CoA-ligase	gnl\|CDD\|234677	PRK00174, PRK00174, acetyl-CoA synthetase; Provisional.	0
NZ_CP054139.1\|WP_173415890.1\|3890296_3891337_-\|SUMF1/EgtB/PvdO-family-nonheme-iron-enzyme	gnl\|CDD\|335469	pfam03781, FGE-sulfatase, Sulfatase-modifying factor enzyme 1. This domain is found in eukaryotic proteins required for post-translational sulfatase modification (SUMF1). These proteins are associated with the rare disorder multiple sulfatase deficiency (MSD). The protein product of the SUMF1 gene is FGE, formylglycine (FGly),-generating enzyme, which is a sulfatase. Sulfatases are enzymes essential for degradation and remodelling of sulfate esters, and formylglycine (FGly), the key catalytic in the active site, is unique to sulfatases. FGE is localized to the endoplasmic reticulum (ER) and interacts with and modifies the unfolded form of newly synthesized sulfatases. FGE is a single-domain monomer with a surprising paucity of secondary structure that adopts a unique fold which is stabilized by two Ca2+ ions. The effect of all mutations found in MSD patients is explained by the FGE structure, providing a molecular basis for MSD. A redox-active disulfide bond is present in the active site of FGE. An oxidized cysteine residue, possibly cysteine sulfenic acid, has been detected that may allow formulation of a structure-based mechanism for FGly formation from cysteine residues in all sulfatases. In Mycobacteria and Treponema denticola this enzyme functions as an iron(II)-dependent oxidoreductase.	5.60067e-82
NZ_CP054139.1\|WP_173415898.1\|3901367_3902594_+\|imidazolonepropionase	gnl\|CDD\|236478	PRK09356, PRK09356, imidazolonepropionase; Validated.	2.46468e-130
NZ_CP054139.1\|WP_173415899.1\|3902706_3904350_+\|glutamate-formimidoyltransferase	gnl\|CDD\|131079	TIGR02024, FtcD, glutamate formiminotransferase. This model represents the tetrahydrofolate (THF) dependent glutamate formiminotransferase involved in the histidine utilization pathway. This enzyme interconverts L-glutamate and N-formimino-L-glutamate. The enzyme is bifunctional as it also catalyzes the cyclodeaminase reaction on N-formimino-THF, converting it to 5,10-methenyl-THF and releasing ammonia - part of the process of regenerating THF. This model covers enzymes from metazoa as well as gram-positive bacteria and archaea. In humans, deficiency of this enzyme results in a disease phenotype. The crystal structure of the enzyme has been studied in the context of the catalytic mechanism. [Energy metabolism, Amino acids and amines].	8.20218e-131
NZ_CP054139.1\|WP_173415889.1\|3888853_3890287_-\|hypothetical-protein	gnl\|CDD\|226064	COG3534, AbfA, Alpha-L-arabinofuranosidase [Carbohydrate transport and metabolism].	8.0546e-15
NZ_CP054139.1\|WP_173415891.1\|3893286_3893733_+\|MarR-family-transcriptional-regulator	gnl\|CDD\|197670	smart00347, HTH_MARR, helix_turn_helix multiple antibiotic resistance protein.	1.83485e-18
NZ_CP054139.1\|WP_173415896.1\|3898057_3899617_+\|histidine-ammonia-lyase	gnl\|CDD\|236484	PRK09367, PRK09367, histidine ammonia-lyase; Provisional.	0
NZ_CP054139.1\|WP_173415894.1\|3896502_3897348_-\|esterase-family-protein	gnl\|CDD\|223700	COG0627, COG0627, Predicted esterase [General function prediction only].	6.05161e-32
NZ_CP054139.1\|WP_173415895.1\|3897554_3898061_+\|MarR-family-transcriptional-regulator	gnl\|CDD\|197670	smart00347, HTH_MARR, helix_turn_helix multiple antibiotic resistance protein.	1.87367e-10
NZ_CP054139.1\|WP_173415886.1\|3885790_3886504_+\|2-C-methyl-D-erythritol-4-phosphate-cytidylyltransferase	gnl\|CDD\|234670	PRK00155, ispD, D-ribitol-5-phosphate cytidylyltransferase.	2.06491e-90
NZ_CP054139.1\|WP_173417830.1\|3891531_3893010_-\|sulfatase-like-hydrolase/transferase	gnl\|CDD\|293755	cd16031, G6S_like, unchracterized sulfatase homologous to glucosamine (N-acetyl)-6-sulfatase(G6S, GNS). N-acetylglucosamine-6-sulfatase also known as glucosamine (N-acetyl)-6-sulfatase hydrolyzes of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate. Deficiency of N-acetylglucosamine-6-sulfatase results in the disease of Sanfilippo Syndrome type IIId or Mucopolysaccharidosis III (MPS-III), a rare autosomal recessive lysosomal storage disease.	0
NZ_CP054139.1\|WP_173415893.1\|3894801_3896355_+\|carbohydrate-binding-domain-containing-protein	gnl\|CDD\|379528	pfam14262, Cthe_2159, Carbohydrate-binding domain-containing protein Cthe_2159. Cthe_2159 from Clostridium thermocellum is the first representative of a novel family of cellulose and/or acid-sugar binding beta-helix proteins that share structural similarities with polysaccharide lyases.	2.04801e-52
NZ_CP054139.1\|WP_173415888.1\|3887925_3888840_-\|TIM-barrel-protein	gnl\|CDD\|224007	COG1082, IolE, Sugar phosphate isomerases/epimerases [Carbohydrate transport and metabolism].	7.88698e-20
NZ_CP054139.1\|WP_173415887.1\|3886616_3887924_-\|Gfo/Idh/MocA-family-oxidoreductase	gnl\|CDD\|223745	COG0673, MviM, Predicted dehydrogenases and related proteins [General function prediction only].	6.00368e-37
NZ_CP054139.1\|WP_173415900.1\|3904891_3905641_+\|HAD-IIB-family-hydrolase	gnl\|CDD\|319784	cd02585, HAD_PMM, phosphomannomutase, similar to human PMM1 and PMM2, Saccharomyces Sec53p, and Arabidopsis thaliana PMM. PMM catalyzes the interconversion of mannose-6-phosphate (M6P) to mannose-1-phosphate (M1P); the conversion of M6P to M1P is an essential step in mannose activation and the biosynthesis of glycoconjugates in all eukaryotes. M1P is the substrate for the synthesis of GDP-mannose, which is an intermediate for protein glycosylation, protein sorting and secretion, and maintaining a functional endomembrane system in eukaryotic cells. Proteins in this family contains a conserved phosphorylated motif DxDx(T/V) shared with some other phosphotransferases. This family contains two human homologs, PMM1 and PMM2; PMM2 deficiency causes congenital disorder of glycosylation type I-a, also known as Jaeken syndrome. PMM1 can also act as glucose-1,6-bisphosphatase in the brain after stimulation with inosine monophosphate; PMM2 on the other hand, is insensitive to IMP and demonstrates low glucose-1,6-bisphosphatase activity. Arabidopsis thaliana PMM converted M1P into M6P and glucose-1-phosphate into glucose-6-phosphate, with the latter reaction being less efficient. Arabidopsis thaliana and Nicotiana benthamian PPMs are involved in ascorbic acid biosynthesis. 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.	6.80622e-40
NZ_CP054139.1\|WP_173415897.1\|3899594_3901268_+\|urocanate-hydratase	gnl\|CDD\|235448	PRK05414, PRK05414, urocanate hydratase; Provisional.	0

>NZ_CP054139.1|WP_173415893.1|3894801_3896355_+|carbohydrate-binding-domain-containing-protein
MLRPKTNLRLINLILPVTFTLCVLLAPGCKKGTKTSGEDTGPTVTPSLKIDSTTITSGTAEGSKETGANTDDQVEGSTFGSVVTIAFGTTVNITNAVSGVTIVQSGANLVITSKVDGVEYKVSGTTTNGSVKIYSDKKFKLTLNGANITSTSGPAINIQSKKRCFVVLADGSTNTLTDSPTYPTSTEDMKGTFFSEAQLVFSGTGSLTVQGNYKHAICSDDYVHIRTGTITVTGAVKDGIHSNSGFIADGGTVKITANTGDAIECEEGSMIINDGKFTLASNEKGINASYEGTDATITPYININGGTLNINVGTGEGISTKLSAITINGGNIAITSSDDCLNAAKAININSGFLYLYSKLNDGMDSNGTITITGGKTVAIGTTATEAGLDCNTNVMKLTGGVVVGIGSETSGPSATASTINSLVMGSGTANQLVHIEAADGTDAMTFLAPLNYTTMLYACAKVKSATAYTVYTGGSVAAGTNFRGLYTSGNYTKGDKKSIFTTSGVVTQTGGTVSTK
>NZ_CP054139.1|WP_173415892.1|3893724_3894327_-|sigma-70-family-RNA-polymerase-sigma-factor
MFQQGCDLWKLFLAGDKVAFQQLIAQHFRHLVNYGTKFTDDKELVKDTIQELFIRFWEKRANLSDDVNPRAYLTASLRRALHRKIQSVSRFQSFDDVENSSDLFDMELSVESRIIEKEYGRNIARAIAQNMEELPKRQKEVVYLKFFQEMSRDEISEVMGISAQTVSNLLQMALKNLRTRISKDLLVYLLLIFGNKRNLA
>NZ_CP054139.1|WP_173415891.1|3893286_3893733_+|MarR-family-transcriptional-regulator
MQPSEKLNDILFYTLEKAIKTYRQFAQKNITKAGFDITIDQWLVLKTLQQQPGIAQQEIAAMVFKDFASVTRIIELLVTKGYLNRSAHATDKRRSNLTLTDKGNTIIKDIQPLIMSNRKRALEGISGEESDLLNGVLNKLTGNCQSSG
>NZ_CP054139.1|WP_173417830.1|3891531_3893010_-|sulfatase-like-hydrolase/transferase
MPPNNVKNFERIPGTRPRNIIYILSDDHRYDFMGFTGKVPGLQTPNLDRLANEGAHFQNAFVTTSLCSPSRASILTGQYAHTHTVVDNESPAPVSLIYFPQYLQKVGYQTSFFGKWHMGGGDGHPRPGFNKWVSFNGQGVYYNPVLNIDGKIVKYKDSAYITDILTDLSLDWLKKRDKSKPFFMYLSHKAVHADFMPSKEDKGKYKNIQVQYPVSMFMTETPTSKKFTRGVRADGSKYTFNNKDIPAWVRAQRYSWHGVDYMYHGATDFDQFYVDYLETLLGIDKSVGRVLQYLKDNGLDKETLVIYMGDNGFAFGEHGLIDKRQAYEESMRVPLLARCPALIKPGTKIKQMVLNVDIAPTILEMAGVKKPKQMQGMSFYPLMQGKDVPWRSEFFYEYYWESNFPQTPTQYAVRTDRYKFIRSWGVWDIDQLYDIQKDPYEVNNLIRDPQYQQTAKELNDKLFDWMAKTNGLQIPLKPILEKKKDHLYKGTW
>NZ_CP054139.1|WP_173415890.1|3890296_3891337_-|SUMF1/EgtB/PvdO-family-nonheme-iron-enzyme
MFIKKHHILLASALIAMASACNQPAKNGNAATATTTAATPAPADTVPLKMIHIPGGTFQMGSNDPAFPDAAPVHAVTVKSFWMDEHEVTNAEFARFVNATGYLTIAERPIDPKDFPGVPKENLVPGSGVFTPTPQPVSLDDPMQWWRYVNGANWKHPFGPQSNINGKQNEPVVHISYTDAAAYAKWAGKRLPTEAEWEYAAQGGKGSHKYYWGDELKPGGKWQANIFEGHFPDANTKEDGYEGVAPVKSFPANGYGLYDMDGNVWEWCHDFYRPDYYKHSPAVNPQGPTDSYDPEEPGAVKRVQRGGSFLCSDQYCIRYRAGSRAKGEVNSASNNLGFRCVKDDTK
>NZ_CP054139.1|WP_173415889.1|3888853_3890287_-|hypothetical-protein
MLKPILKPAACLVIALSLSFITNHADAPDCTININAAEEQGIVSPNIMGFNIVYCYEGDAAWQSGKGKVPEMLSAIGTRQLRYPGGTVVTKFHWEKPTGQGWSDSWSPDYNPAKNTDPSTFMDIDEYLGVVKTQHTEPLVGINMGSGMKYNRVQEGVDEAIRLMKHCIASGVKVKYYYLDNEPYQPDANFTFTAEQYAESVNTYANAMRKIDPAIKIIVNTHPNTAMYTKQLLAIAGKNIDLVDVHMYWKFKNATYENWQKEGAMKHRGIAPYSEQRGIFEKIFADAGYPNIKMVVLEWNIGPQGPDHTPPTEEQAALMASEQFTQYIQSGLFMACFWPLSWPQQADWSSRALMKQKDNYKPNKMYQMFTQYANVLGQQKVSSTGSVQNVINLAVKSTDGKTAWVYIINKEQSKEMMNVSVALDGFKAKTYTATGFNGDDNGGDSLALHDVKINSVNATHFNVQIPKNSFTKITFKI
>NZ_CP054139.1|WP_173415888.1|3887925_3888840_-|TIM-barrel-protein
MTDKYTRREWAGLALTGLGALMLPSFLSSCKSMAVAVPPVLKGTLAAKQAAEIGIVLGAQTYSFRDHTLDDAIKIMGQLGIRSCELWNGHIQPKTDLKGWRAKDHTDEMKAIRAKFDAAGITIMAYTDGFRDNFSEQEIEQVFRIARDLGTDTITTSATVSVMKRVDVYAKKYKIRVGMHGHSNVNNPNELSSPDSFARGMAGCSNYIGINLDIGHFTAAGFDAIDYIKQHHDRIYCIHVKDRKKNQGENQPLGQGDTPIGPVLRLIRDMHYPIPAHIEYEYKGGDSLVEVGKCLDYCKQQLKA
>NZ_CP054139.1|WP_173415887.1|3886616_3887924_-|Gfo/Idh/MocA-family-oxidoreductase
MEKEKDQAGNSAISRRKFLGSAAALSAFFIVPRHVLGGVGYLAPSDKITMGWIGAGRQGLYLQGAFLKTNEAQLVAVADVYKTKVDNFINITNKFYADAGQQSTYKGCTGYNNFTELLNRKDIDAVVIATPDHWHAAVAVRAAAAGKDIYCEKPLSLTVKEGRAMADAVRKYKRVFQTGSMQRSSGEFRQAVELIRNGYLGQIKNVKVSIGGPPVPYNLPEETLPEGLDWNLWLGPNEYVHYNRLLDPMIGDSAWGKWRDFKGLGGGDMTDWGAHMFDIVQWALDMDGTGPVSVNPPDADHQFLTYTYANGIVMTHENFGKPHSIQFNGTEGTLEIQRQKLVTTPASLATKTIGGNDKRVYFSDNHYKDFLDAIRKRSKPIADIETGHRSATVCNIGNIAYELGVPLKWDPAKERFDNDKANALLGRAMKKEWAV
>NZ_CP054139.1|WP_173415886.1|3885790_3886504_+|2-C-methyl-D-erythritol-4-phosphate-cytidylyltransferase
MSHISNPSSHISAYAIIVAGGSGSRMQSVVPKQFLLLNGRPVLMYTIEAFARSAYQPEIIVVMHPNYHIYWQELCAEHSFTIPHQIISGGDTRFHSVKNGLELVADDSLVAVQDAVRPITSTEIIDNAYTQAAEYGNAVVAVKSRDSIRSLRNGVSQSLLRDEIYLVQTPQTFKSGLLKKAYLQPFNDGFTDDASVVEKDGHMIHICDGDYQNIKITFPEDIAIAELLLKKQRHSER
>NZ_CP054139.1|WP_173415885.1|3885493_3885709_-|hypothetical-protein
MERLMINIPENKSALVKQLLKELGVSFKQEKTEKLSDLKKNLLEVSVWSDDDLKPIEDAKNHFQNLGSEKW
>NZ_CP054139.1|WP_173415894.1|3896502_3897348_-|esterase-family-protein
MKKLFRAGLVLFNLLLIAKLSIAAKVDTVETYSDAMHKKIKAVVIRPNDYDKLSAMPVVYLLHGFGGKYSDWPNNVPAIQELADNYHMMVVCADGNVSSWYLDSPVLSDWKYETYVGTELVAWIDNHYKTLKSRTGRAITGLSMGGHGALYLAFKHQDTFGAAGSTSGGVDIRPFPNNWKMAEKLGTYAEHPEYWEKNTVINMVNLLTPGHLSLIIDCGTEDFFYKVNCNLHDLLMLRNIPHDFYVRPGAHNWPYWQNSIKYQLLYFHDYFEAQLKAGAKK
>NZ_CP054139.1|WP_173415895.1|3897554_3898061_+|MarR-family-transcriptional-regulator
MNLYQRLGYLALGSRLRRLSEAFLSEITYAYQQEGIEFDAAWFPVFYLLSQNEALTIKELSEQTEVSHPAASQLITNLKQKGLVMATPGIDDARKQLITFTGKGRALLQQVLPVWDAIMLSMDEISRNQPGCDAMLPAITAFEQALQQHDLYNHISKNLNKQLTPADK
>NZ_CP054139.1|WP_173415896.1|3898057_3899617_+|histidine-ammonia-lyase
MNTTFHYGTEHLTIGICLDIAAGKTKGIIGDDARAAIRNSRGYVEQIVHEHHPVYGINTGFGPLCDTRISEEDTCLLQSNILRSHSVGVGNPIPQEIAKIMMITKVHALAQGFSGVAPETLDRLIWHIDNDIIPFVPEKGSVGASGDLAPLSHLCLPLIGLGEVFEHGQRVASDTVLKKHNLQPLILGPKEGLALINGTQFILAFAVKAVQRLNDALNRADLIGAMSLEGLMGSARPFDARLHNIRPYKGTKYVAKRLATLLDHSEINTSHANCDRVQDPYSLRCMPQVHGASRNAWLHLKELTEIELNSVTDNPVIFSADDTISGGNFHGQPMALPLDYATVAAAELGNIADRRCYLMSEGRYGLPKLLVNDAGLNSGLMIPQYTTAALVTENKTLCFPASADSVPTSLGQEDHVSMGSISGRKLHTVIDNLEYIQAIELLYATQAMDFRRPLRSTEVIEACHALVREHVPHIQNDRVFADDIKQLHQIITDGSFLALADAVAAKNHINLSHDEFGIY
>NZ_CP054139.1|WP_173415897.1|3899594_3901268_+|urocanate-hydratase
MTSSEFINTYANHPVYKAPTGTQLHAKSWQTEAPLRMLLNNLDGQVAENPEDLVVYGGIGQAARNPEALRKIIELLLELDEHHSLLVQSGKPVGIVRSHPEAPRVLIANSNLVPAWATWEHFNELRAKGLMMYGQMTAGSWIYIGTQGILQGTYETFVECGNQHFGGDLAGKLIVSAGLGGMGGAQPLAATMAGGVFLGADVDASRIQKRVDTQYIDRMTESYDEAIAWVKEAMAKKETLSVGLVSDAGDMLARLIKDGIVPDMLTDQTSAHDPLNGYIPDGLTLEKAASLRASDPHIYKLRSLKSMARHVGLMLQLQQMGAITFDYGNNLREFARQGGEPDAFNFPGFTPAYIRPLFCEGKGPFRWVALSGDPEDIYTTDRALMEAFPENKALINWLQKAQDKIAFQGLPARICWLGLGDREKAGLLFNDLVRTGKVKGPIVIGRDHLDCGSVASPNRETESMKDGSDAVSDWPLLNLMANASGGATWISFHHGGGVGMGYSQHAGMVIVADGTDRADTCLKRVLHNDPAMGIFRHADAGYDKAEEWAEKFGLKVW
>NZ_CP054139.1|WP_173415898.1|3901367_3902594_+|imidazolonepropionase
MKKLTGPFTQILPMTGLPIKGALKDEQMHIISQGGVLTENGRIVALGDFKKLRKENPSAQVEKITGQHVLLPGFVDCHTHICFGGNRAKDYAMRIQGKTYLEIARAGGGIWDSVTQTREASEAELIITLVQRAERHLSEGVTTIEVKSGYGLNIDNELKQLKAIKQAAGQTKASLIPTCLAAHMRPKDFNGSSIEYLTHVLQDLLPIIKQQELTNRVDIFIEESAFNTFDATKYLLAAKEMGFDITVHADQFTADGSTVAVEMGAVSADHLEASTKHEINLLANSDTVAVTLPGASLGLGMNYAPARKLLDGGACVAIASDWNPGSAPMGDLLMQAAVMSAAEKLSTAEVFAGLTFRAAKALNLNDRGVLTEGYRADMQTYPCADYREILYYQGKLKPDIIYVNGDLI
>NZ_CP054139.1|WP_173415899.1|3902706_3904350_+|glutamate-formimidoyltransferase
MTKLIECVPNFSEGVNLDIIKQITDEIESVDGVRLLNVDPGKATNRTVVTFVGEPNAVIEAAFLAIKKAGELIDMSRHKGEHPRMGATDVCPLIPISNISMEETAEYARKLAKRVGEELQIPAYLYEYAQADKSRSNLSVIRTGEYEGFFKKIKQPEWAPDFGPAEFDAKRGGTVIGARDFLIAYNVNLNTTSTRRANAIAFDVREAGRMVDGVNHPGTLKSVKGIGWFIEEYGIAQISMNLTNIAVTPLHIAFDEVCNKATARGIRVTGSELVGLVPLQTMLDAGKYFLRKQQRSVGVSESELIRIAIKSMGLDELAPFKPEERIIEYLLKNDSNNKLISMTLTGFANETASESPAPGGGSISAYVGSLGASLATMVANLSSHKKGWDDRWEEFSDWAEQGQRYKDELLQLVDLDTVAFNKIMEAFGLPKGTDEEKAARSKAIQHATKYAIEIPFKVMQAALNSMDVIEAMVQTGNPNSVTDAGVAALCARTAVLGAFMNVKINASGYKDKIFVDGIIANGNEIAKQAVAREARIVEMVDAKIGLS
>NZ_CP054139.1|WP_173415900.1|3904891_3905641_+|HAD-IIB-family-hydrolase
MKKLIIFDLDGTLAESKAAIDTEMADILTRLLQVARVAIISGGDWPQFEKQVLAHLPDKRWMKRLSILPTCGTKFYQFKKGWQPLYAENFTAEEKSTIINNLNAAVEQTGFKPRKTWGDQIEDRGSQVTFSALGQQAPLEQKKKWDPKFAKRKKIKKILNGTLSGFSVNMGGATSIDVTKPGIDKAYGIRKLKKVLDIKISQMIFIGDALFEGGNDYPARTTGADCIQVRDPEETKRVVDAITLCLDKK
>NZ_CP054139.1|WP_173415901.1|3905771_3906134_-|hypothetical-protein
MSKETTYLYRPVGPNELAKIEESGWKRFPKRLAQQPIFYPVMNEEYAVQIARDWNVPASGSGYVTKFAVDAQYLKKFEVQNVGGPIHNELWVPAEELEEFNDQIVGPIEVTQRFFRDEKE
>NZ_CP054139.1|WP_173415902.1|3906155_3906833_-|hypothetical-protein
MADIEVFKLNNCDPEEIEDIILKIEKSFRLNFKQGDFKDVKTFGDLCDIVMDRIEGESVNSCTSQQAFYKIRDAIIGTCSIDRDSLTLDTELSFIFPRRNRIYKVRQFRDQLGIRVNILGIKNWLGWFITVCFILSFGLLFINWLYALIAIAASIGMYRFSYLFGKELKINTVRQLTELVATEHYRLSRRNSKRYNKKEVVDTIKRIFINDLAVAESALNRDSAF
>NZ_CP054139.1|WP_173415903.1|3906967_3908869_-|acetate--CoA-ligase
MKITSFDEYKQIYQYSVNNPEQFWAGIAETFQWRKKWNKVLEWNFTEPRVRWFDGAKLNITENCLDRHLDTIGDKPAIIWEPNDPSEDFRVLTYKQLHSKVCQFANVLKNNGAKKGDRICVYMPMVPELAIAILACARIGAIHSVVFGGFSAQSIADRIQDADCNIVITADGGFRGAKDIPLKSIIDDALVQCPSVKRVIVLTRTRTPVAMIKGRDVWWEDEVKKVETQGNIDCPAEEMEAEDMLFILYTSGSTGKPKGVVHTCGGYMVYAGYTFDTTFQYQPDEVYFCTADIGWITGHSYIVYGPLSQGATSLMFEGVPTWPDAGRFWDITDKHKVNILYTAPTAIRSLMSFGDEPLKGKDLSSLKKLGSVGEPINEEAWHWFDEKIGHGKCPIVDTWWQTENGGHMITPIAGITPLKPGYASLPLPGVQPVLVDEKGNEIEGNSVSGNLCIKFPWPGMLRTTYGDHERCRQTYFATYPNMYFTGDGCLRDEDGYYRITGRVDDVLNVSGHRIGTAEVENAINMHSSVVESAVVGYPHDIKGQGVYAFVVSPNHQDDQELARKDIIMTVARIIGAIAKPDKIQFVSGLPKTRSGKIMRRILRKIAEGDTSNLGDTSTLLDPAVVEEIKAGAL

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Crispr_ID: NZ_CP054139_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP054139_7

3957531-3957604

Orphan

Consensus_repeat	Method
CCTATCTGGCGCGAGTATGCAGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP054139_7

>merge|NZ_CP054139|7|3957531-3957604|CRISPRCasFinder
CCTATCTGGCGCGAGTATGCAGCATTGGGCTGATTCGTGCCTAGCAAGCACCCTAACTGGCGCGAGTATGCAGC

>NZ_CP054139|7|6|3957531-3957604|CRISPRCasFinder
CCTATCTGGCGCGAGTATGCAGC	ATTGGGCTGATTCGTGCCTAGCAAGCAC
CCTAACTGGCGCGAGTATGCAGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP054139.1\|WP_173415947.1\|3958960_3959875_+\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|225375
NZ_CP054139.1\|WP_173415945.1\|3957092_3957500_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173415948.1\|3960076_3961285_+\|aminotransferase-class-III-fold-pyridoxal-phosphate-dependent-enzyme	unknown	unknown	gnl\|CDD\|99735
NZ_CP054139.1\|WP_173415938.1\|3948760_3950017_+\|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme	unknown	unknown	gnl\|CDD\|235596
NZ_CP054139.1\|WP_173415939.1\|3950066_3950522_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173415953.1\|3967426_3967948_-\|acyl-CoA-thioesterase	unknown	unknown	gnl\|CDD\|224523
NZ_CP054139.1\|WP_173415941.1\|3951242_3952835_+\|FAD-dependent-monooxygenase	unknown	unknown	gnl\|CDD\|366675
NZ_CP054139.1\|WP_173415940.1\|3950525_3951236_+\|SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|381176
NZ_CP054139.1\|WP_173415951.1\|3966294_3966624_+\|L-rhamnose-mutarotase	unknown	unknown	gnl\|CDD\|377501
NZ_CP054139.1\|WP_173415952.1\|3966757_3967276_-\|O-acetyl-ADP-ribose-deacetylase	unknown	unknown	gnl\|CDD\|394878
NZ_CP054139.1\|WP_173415943.1\|3955444_3956428_-\|aldo/keto-reductase	unknown	unknown	gnl\|CDD\|381312
NZ_CP054139.1\|WP_173415954.1\|3968456_3970364_-\|molecular-chaperone-DnaK	unknown	unknown	gnl\|CDD\|234715
NZ_CP054139.1\|WP_173415955.1\|3970846_3971248_-\|T9SS-type-A-sorting-domain-containing-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173415949.1\|3961636_3964465_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379297
NZ_CP054139.1\|WP_173415936.1\|3947458_3948163_+\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|212491
NZ_CP054139.1\|WP_173415942.1\|3952954_3954868_-\|gliding-motility-associated-C-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|372639
NZ_CP054139.1\|WP_173415950.1\|3964945_3966298_+\|L-fucose:H+-symporter-permease	unknown	unknown	gnl\|CDD\|340952
NZ_CP054139.1\|WP_173415937.1\|3948249_3948564_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173415944.1\|3956550_3956955_-\|EVE-domain-containing-protein	unknown	unknown	gnl\|CDD\|376640
NZ_CP054139.1\|WP_173415946.1\|3957877_3958438_+\|transposase	unknown	unknown	gnl\|CDD\|376616

Protein	Function_ID	Function_description	E-value
NZ_CP054139.1\|WP_173415947.1\|3958960_3959875_+\|alpha/beta-hydrolase	gnl\|CDD\|225375	COG2819, COG2819, Predicted hydrolase of the alpha/beta superfamily [General function prediction only].	8.09946e-24
NZ_CP054139.1\|WP_173415951.1\|3966294_3966624_+\|L-rhamnose-mutarotase	gnl\|CDD\|377501	pfam05336, rhaM, L-rhamnose mutarotase. This family contains L-rhamnose mutarotase which is a glycosyl hydrolase that converts the monosaccharide L-rhamnopyranose from the alpha to the beta stereoisomer. In Escherichia coli this enzyme is the product of the rhaM gene (also known as yiiL). The tertiary structure has been solved, in complex with L-rhamnose, and the catalytic mechanism determined. His22 is the proton donor. The enzyme naturally exists as a dimer.	3.86362e-41
NZ_CP054139.1\|WP_173415953.1\|3967426_3967948_-\|acyl-CoA-thioesterase	gnl\|CDD\|224523	COG1607, COG1607, Acyl-CoA hydrolase [Lipid metabolism].	6.50375e-61
NZ_CP054139.1\|WP_173415938.1\|3948760_3950017_+\|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme	gnl\|CDD\|235596	PRK05764, PRK05764, aspartate aminotransferase; Provisional.	1.69158e-76
NZ_CP054139.1\|WP_173415954.1\|3968456_3970364_-\|molecular-chaperone-DnaK	gnl\|CDD\|234715	PRK00290, dnaK, molecular chaperone DnaK; Provisional.	0
NZ_CP054139.1\|WP_173415941.1\|3951242_3952835_+\|FAD-dependent-monooxygenase	gnl\|CDD\|366675	pfam01494, FAD_binding_3, FAD binding domain. This domain is involved in FAD binding in a number of enzymes.	2.56193e-87
NZ_CP054139.1\|WP_173415940.1\|3950525_3951236_+\|SAM-dependent-methyltransferase	gnl\|CDD\|381176	cd11649, RsmI_like, uncharacterized subfamily of the tetrapyrrole methylase family similar to Ribosomal RNA small subunit methyltransferase I (RsmI). RsmI, also known as rRNA (cytidine-2'-O-)-methyltransferase, is an S-AdoMet (S-adenosyl-L-methionine or SAM)-dependent methyltransferase responsible for the 2'-O-methylation of cytidine 1402 (C1402) at the P site of bacterial 16S rRNA. Another S-AdoMet-dependent methyltransferase, RsmH (not included in this family), is responsible for N4-methylation at C1402. These methylation reactions may occur at a late step during 30S assembly in the cell. The dimethyl modification is believed to be conserved in bacteria, may play a role in fine-tuning the shape and functions of the P-site to increase the translation fidelity, and has been shown for Staphylococcus aureus, to contribute to virulence in host animals by conferring resistance to oxidative stress.	5.69542e-144
NZ_CP054139.1\|WP_173415952.1\|3966757_3967276_-\|O-acetyl-ADP-ribose-deacetylase	gnl\|CDD\|394878	cd02908, Macro_OAADPr_deacetylase, macrodomain, O-acetyl-ADP-ribose (OAADPr) family. Macrodomains are found in a variety of proteins with diverse cellular functions, as a stand-alone domain or in combination with other domains like in histone macroH2A and some PARPs (poly ADP-ribose polymerases). Macrodomains can recognize ADP-ribose (ADPr) in both its free and protein-linked forms, in related ligands, such as O-acyl-ADP-ribose (OAADPr), and even in ligands unrelated to ADPr. This family includes eukaryotic macrodomain proteins such as human MacroD1 and MacroD2, and bacterial proteins such as Escherichia coli YmdB; these have been shown to be O-acetyl-ADP-ribose (OAADPr) deacetylases that efficiently catalyze the hydrolysis of OAADPr to produce ADP-ribose and free acetate. OAADPr is a sirtuin reaction product generated from the NAD+-dependent protein deacetylation reactions and has been implicated as a signaling molecule. By acting on mono-ADP-ribosylated substrates, OAADPr deacteylases may reverse cellular ADP-ribosylation.	1.74691e-99
NZ_CP054139.1\|WP_173415943.1\|3955444_3956428_-\|aldo/keto-reductase	gnl\|CDD\|381312	cd19086, AKR_AKR11C1, AKR11C family of aldo-keto reductase (AKR). Bacillus subtilis uncharacterized oxidoreductase YqkF is a founding member of aldo-keto reductase family 11 member C1 (AKR11C1). It may function as oxidoreductase. This family also includes Bacillus halodurans AKR11C1, an NADPH-dependent 4-hydroxy-2,3-trans-nonenal reductase.	8.52774e-99
NZ_CP054139.1\|WP_173415949.1\|3961636_3964465_-\|hypothetical-protein	gnl\|CDD\|379297	pfam13620, CarboxypepD_reg, Carboxypeptidase regulatory-like domain.	0.00127224
NZ_CP054139.1\|WP_173415936.1\|3947458_3948163_+\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|212491	cd05233, SDR_c, classical (c) SDRs. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes 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 prostaglandin dehydrogenase (PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, PGDH numbering) and/or an Asn (Asn-107, PGDH numbering) 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. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase 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. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.	9.4153e-49
NZ_CP054139.1\|WP_173415944.1\|3956550_3956955_-\|EVE-domain-containing-protein	gnl\|CDD\|376640	pfam01878, EVE, EVE domain. This domain was formerly known as DUF55. Crystal structures have shown that this domain is part of the PUA superfamily. This domain has been named EVE and is thought to be RNA-binding.	2.32559e-59
NZ_CP054139.1\|WP_173415942.1\|3952954_3954868_-\|gliding-motility-associated-C-terminal-domain-containing-protein	gnl\|CDD\|372639	pfam13585, CHU_C, C-terminal domain of CHU protein family. The function of this C-terminal domain is not known; there are several conserved tryptophan and asparagine residues.	8.42522e-26
NZ_CP054139.1\|WP_173415950.1\|3964945_3966298_+\|L-fucose:H+-symporter-permease	gnl\|CDD\|340952	cd17394, MFS_FucP_like, Fucose permease and similar proteins of the Major Facilitator Superfamily of transporters. This subfamily is composed of L-fucose permease (also called L-fucose-proton symporter) and similar proteins such as glucose/galactose transporter and N-acetyl glucosamine transporter NagP. L-fucose permease facilitates the uptake of L-fucose across the boundary membrane with the concomitant transport of protons into the cell; it can also transport L-galactose and D-arabinose. Glucose/galactose transporter functions in the uptake of of glucose and galactose. The FucP-like subfamily belongs to the bacterial fucose permease, eukaryotic Major facilitator superfamily domain-containing protein 4 (FucP/MFSD4) family of the Major Facilitator Superfamily (MFS) of transporters. MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	2.92823e-142
NZ_CP054139.1\|WP_173415948.1\|3960076_3961285_+\|aminotransferase-class-III-fold-pyridoxal-phosphate-dependent-enzyme	gnl\|CDD\|99735	cd00610, OAT_like, Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to ornithine aminotransferase, acetylornithine aminotransferase, alanine-glyoxylate aminotransferase, dialkylglycine decarboxylase, 4-aminobutyrate aminotransferase, beta-alanine-pyruvate aminotransferase, adenosylmethionine-8-amino-7-oxononanoate aminotransferase, and glutamate-1-semialdehyde 2,1-aminomutase. All the enzymes belonging to this family act on basic amino acids and their derivatives are involved in transamination or decarboxylation.	9.64604e-148
NZ_CP054139.1\|WP_173415946.1\|3957877_3958438_+\|transposase	gnl\|CDD\|376616	pfam01797, Y1_Tnp, Transposase IS200 like. Transposases are needed for efficient transposition of the insertion sequence or transposon DNA. This family includes transposases for IS200 from E. coli.	0.000290632

>NZ_CP054139.1|WP_173415945.1|3957092_3957500_+|hypothetical-protein
MNLKKAYYYLFYKFYKFGEASPSLFPNDLTAAFAIDWLEALLLASIGFYLMPLTGRNGHLSVFSFQVLLPLLVIFLINHFAFIHDKRWKKYIDEFDRFPQKKNNKGTWFVIGIIAFIIINFGFSVYVMKQVPITP
>NZ_CP054139.1|WP_173415944.1|3956550_3956955_-|EVE-domain-containing-protein
MNHWLVKSEPVKYSWEKFNKDGRTFWDGVRNYQARNNLREMKEGDLVLFYHSNEGKAVVGIAKVVREFYQDPTTEDPNWVVVDLSPVQTLKTPVTLETIKADGQLKNVSLVRQGRLSVMPLKVEEFDRILELGS
>NZ_CP054139.1|WP_173415943.1|3955444_3956428_-|aldo/keto-reductase
MHYRKFKDTDIAEVGLGTWQLGSADWGVVDEEAAFGILQAYVNAGGNFIDTADVYGMGVSETVIGKFLKTTDKQIHVATKLGRRGDAPNGWPQNFTYDAMRRAVEDSLKHLDVPHLFLEQLHCIPTEEMRAGKVFDYLRKLQSEGLIQHFGASVETSEEALICLEQEGLSSLQIIFNLFRQHVADEVFAKAEEKGVGIIVRVPLASGLLTGRFNADTQFAAKDHRNYNANGEAFNAGETFSGIDFKEGVKLAEEIKTLLPDERTAQWAIRWILDHPEVTTVIPGASKISQVDGNVAASALPALPAETHRALRALYDEKIFKQIRGHF
>NZ_CP054139.1|WP_173415942.1|3952954_3954868_-|gliding-motility-associated-C-terminal-domain-containing-protein
MRYLILLIICYLFAVSVGYAQSQTCNGSLGDPIVNIDFSNSNPIPNLTNYTYTSGTPNDGYYTITKSTAGMFDWWAATDHTGNGYMMVVNANVSKTNYFFQQKITGLCPGTTYEFAAWLLNMAKTVKTATPNITFQITDALGNQTLINTGDLPPSISAKDWKQYGILFTTPAVGGDITLTMINNGAGGTGNDIAVDDITFRPCGPVISSSFPVLSSQNASGCAGTAQSYKMIAQIPAGGYPNPMYQWQVNSNGTWTDITGATTTDYTANFTAVTAVAGTYQYRMASANGGNITSPTCRVVSNVLTLTISDIPSVSAPPSVSVCEGQPFSLTLRSGSDPNNTYTWTRSKGGYSSSSANLSIPNVQLSDDDTYTVTVKNAAGCTATASTILKVSPKVTASVSNANFTICEGDKAQLSASGGTTYSWSPAVGLDNPNIANPQANPTKTTTYTVTVSNATACSATAQVTVNVTNKPQISAGADQKMTEGQTITLNGSVDANATSYYWTPSTGLSDPNALRPTARPTEDITYTLHATSGAPCYFETTADVFIRVYKKVVVPNTFTPNGDGINDTWNIVALETYPESYTQVFNRLGRVVYQTHGYAKQWDGSTGGVPLPEGVYYYKIDLKPGTVLSGWVAIVR
>NZ_CP054139.1|WP_173415941.1|3951242_3952835_+|FAD-dependent-monooxygenase
MQISGQHTSVLIAGAGPSGLMMAAQLLRYGIQPVIIDSRQGPTSHSKALAVQARSMEIYRQMGIVDKVLKDGKPAKGITFYDDGKPGAQLLMDSVSDGTTPYPFILMYPQSSNERTLLDYLTMNCCPVYWDTTLTHITQTTDKATATLEANGKTQTLTADWVIGADGAHSPVRKSLNIPFNGDTYKSLFYLIDGKLADRYDIDLIRVFLSTKGLAGFFPMPQEGYYRIIGNLPDGVNEDGSELELNDVLPSLSAIVGRGISVEECRWLITYKLHHRMADNFRLGRCFLIGDAAHIHSPVGGQGMNTGLQDAYNLAWKLAMVINQKANANLLDTYPEERMPVAKRLLKTTDSAFKFAMSKGILSRTFKKYIMTRLLHFMWSKERIRKFFFLTVSQTGITYRDSKLNLHLSNAKKIKAGDRLPCLTIFDEKKQEETDLHQWCFKPGFTLIILGKLIEEDLFKVARWLTQTYNGSINFYYLPPSEKNQHVFDAFEVGKGRHRSILVRPDMHIGFMNDAVDPDRMDRYLSPLTP
>NZ_CP054139.1|WP_173415940.1|3950525_3951236_+|SAM-dependent-methyltransferase
MPAGTLYLIPVPLADEAAGKSFTPYLVDTINQISEYIVENEKTARRFLKEAGLKTPQSELLIHDYGKHNRDKNDNDFFKGLLAGKDVGLMSEAGCPGVADPGAEIVAEAHRKGIKVVPLVGPSSILLALMASGFNGQSFTFHGYLPIDKADRARRLKELENQAERHKQTQLFIETPFRNNPMLEEILRTCKPATRLCIACNLTAADEMVKTQSIAAWKKQTPDLHKKPTIFLLFHP
>NZ_CP054139.1|WP_173415939.1|3950066_3950522_+|hypothetical-protein
MKKLCLFIACSLLVLASCKKKADEIDTSTASVNVALLTTKAWIISGNDANPATNPKGGTINYAPISACYTDDTYTFNTDGTMLVDNGTVHCNGAEAATSTYNYSVDKVNNTITVDGNTFRLAEISAIQFKYYSVVSTPAGNQFTVYIFQHN
>NZ_CP054139.1|WP_173415938.1|3948760_3950017_+|aminotransferase-class-I/II-fold-pyridoxal-phosphate-dependent-enzyme
MSISKLAQNLRGSEIIKIAGEINELKKQGQNIANLTIGDFDSNLYPIPAELKAGIVGAYGHNQTNYPPADGVLDLRESVSEFLQKRLGLTYQANEILISGGSRPLIYSIFLAIVDPGDTVVFPAPSWNNNHYSDLTSANAIIVQTTPENNFMPTAAELAPHLKGATLLALCSPLNPTGTMFTKKDLEEICDLVIAENKTRAAGEKPLYILYDQIYSQLTFGTHQHYNPVTLRPELRDLTIFVDGASKCFAATGVRVGWGFGPAKIIDNMKAIVGHMGAWSPKAEQVAMADYLRHDDQVDAYLGDLKTKIQASLAALHEGFQQLKADGLNVDSIEPMGAIYLTVKVDYAGKTTPDGTVIKDSADVNFYLIKEAKVALVPFSAFGTDEGMCWFRASVGASSLQDIQQMIPRIKDALLKLK
>NZ_CP054139.1|WP_173415937.1|3948249_3948564_+|hypothetical-protein
MLKDLTIKQELLAQLMSDISEKYYAAGWAQDLEYVLWDAVINGERKYGHDIITIREIETLISLSNEAKCWIVFDDHAEETAISLEVWRKKFNNDISNNAKLLNS
>NZ_CP054139.1|WP_173415936.1|3947458_3948163_+|SDR-family-NAD(P)-dependent-oxidoreductase
MNIIITGASSGVGFEAVLELCLSGKHKVIALARSQDKLTKLLEIALGLNPDAVLYPLVFDIVHDDYHGLQQFIQTRFEGKVDVLINNAGVLINKPFADMDEADFVEMLQSNYIGHVRMIQSTLPLMAEDSHIVNIGSMGAFQGSAKFAGLSAYSASKAALHTLTECLALELADRKIKVNCLALGSAQTEMLEQAFPGYESPVMAFEMGKYIADFALTGQRFFNGKILPVAVTTP
>NZ_CP054139.1|WP_173415946.1|3957877_3958438_+|transposase
MSVKYKFRDQEKLYFISFAVVNWIDLFIRNDYKDIMLNSWKYCQTHKGFEIYGWCIMTSHVHMIIGSNGAKLEDIMRDMKKHTSIALKAAIQNHPGESRREWMLWMMERAGRKNSQNINFQLWQQDNHPIEIYDFRILHQKLDYIHNNPVVAGIVDKPQDYLYSSARDYYGLPGMVDIILVDPLVA
>NZ_CP054139.1|WP_173415947.1|3958960_3959875_+|alpha/beta-hydrolase
MRKLLALLIFVSTITFAQTPKVSSGTIQHIEKFPSKFVPARNVDIWLPDGYSINKKYAVLYMHDGMALFDAAIMWNKQEWGVDETMGRLLAEHKIKDCIVVGIWNGNADRHHEYFPQKPFESLPAQVQDSLYDIGSTAGKLLSAKVNSDDYLKFIVRELKPYIDSHYPTLKDQGNTFIAGSSMGGLISLYALCEYPKVFGGAVCLSTHWPGTFALDNNPIPVAFMAWYGKHLPSARSHKIYFDHGDQTLDALYAPYQKQADSLMLAKGYTQGKNFLSKFYPGADHSENSWGKRLDVPLVFLLGR
>NZ_CP054139.1|WP_173415948.1|3960076_3961285_+|aminotransferase-class-III-fold-pyridoxal-phosphate-dependent-enzyme
MLTHRQLFLANNAQTTNFPLLLEFERAEGVYLYDKDGKAYIDLIAGIGVSNTGHGHPYVIDAIKAQLDKYLHLMVYGEYVQSPQVKFAEKLVSLLPDDLQSVYFVNSGAEAVEGAMKLAKRYTGRSQVLACYGSYHGSTQGALSIMGNEEYKQAYRPLVPGTGFIRFNEPADLDLITNETACVFVETVQGEAGIRVADVEYMQALSARCKATGTLLVLDEIQAAMGRTGKLFAFEHYGIVPDILLLAKALGGGMPLGAFIASNEVMSALKENPILGHITTFGGHPVCCAAGLASLEVLLNENLIDTVASKEALFRQLLVHPAIKEVRGKGLMLAIELADFDTNKKIIDRCIANGVITDWFLHCSNSMRIAPPLIITEEQIREACGVILEAMDHGIARSSGGL
>NZ_CP054139.1|WP_173415949.1|3961636_3964465_-|hypothetical-protein
MSIILLLGLSLFAKAQTPQSGIKDVMAKIDSFNYHMPAEKLYMQFDKPYYAVGDTIWFKAYLLNANLNYSPLSSRLYVEVLNDSSKVIRRMAFQMGVGISWGNISLEGMREGSISIRAYTNWQRNFGQDYFFTRAFYISNPQKQTWLVAANSQLSDANNIKMNVKLSSLDNQTTGLKQMQMRVLDGKKVLFKGNAQTTAEGLLDLNFPLPDKTPVKNLVLVAQDKADPKKQVAIPVNTRRAKDVDVQFMPEGGYMVAGLPAHLGFKAIGDDGKGVNISGKIVNAAGEEVVTLQSAYKGIGTVDLAPQAGDVYTAKLTLPGGQTKDVPLPAIKPSGTEIRVRNIATRDSMDVSVFMSADLVKPGSAYYLVGQARGVVCFGASIPTARAFATVHVAKSSFPTGIVHFTLLNAQNQPLNERLTYVDHHDNLKIGVSTAQSTYAARDSIPVKISVRDAAGKPIIGSFSLAVTDDTQVKTDSANNDNITSRFLLTSDLKGFVEDPAYYFTGDKNAWQALDALLLTQGWIGYDWNQIKAIPKPTFQPEYQYTVNGRVGNLLNKPVANAQVVLLARGRYNYIKDTLTNAEGRFTFRNFPSIDSVTFVLEAQNKRHKVINSGITVDENLAPDIIKENTPRATPWYVNSDAAMLNFVKTNPSYHTELDKAQYGPQGRLLKTVTIRDRAMVKGSQNLNGAGEADQVIDEETIVNANKMSLADLLEQKVTGFHTGYLSKPGGGRGSGIPKAPPELMYMLKDKKVSFSFDGVYLNRFYQPMDTDGPAMPNEFYNYVKQYLDYFTAEDIKGIEVMYTMRRTNNYNTQNLTPEELMAESPAGARGSATAYIEITTRAGNGPFTQHAAGIYVYKPLKNTLPAIFYRPRYPVKNAPAKFADLRSTIHWEPTVVTNKDGEATVSFYAADKPATYTLTLEGGDLKGSVGYQTQKITIGGK
>NZ_CP054139.1|WP_173415950.1|3964945_3966298_+|L-fucose:H+-symporter-permease
MASLTNKSYRFAFILITSLFFLWGFAHNLDPILIPHLKRSFTLTTLQASLVDSAVFVAYFVMALPAGAIMRNYGYKSGIITGLLLFALGSFLFIPAANTQQYIFFLGALFIIACGLTILETAANPYASLLGDPETATQRLNFSQSFNGFAAFMAPIVGANLILTRGATDEQLSHMTEAVRKATLASEASTVKMPYMILAIILLLIAAAFYFTKLPEIKDDNQEASSKSLFHAFKHKHLSWGVAAQFFYVGAQVCVFSFFILFASKTIPAGTPKDLLVTIMEKIFVFFHVVSESSATTYYSYYLSAAGLMFMVGRFVGTFIMKYLKPNTLLAIYAAINVLLCIVAMNSHGTTPVYCVIAIAFFMSIMFPTIFSLGIHNLGGDTEYGSSLIVMSIVGGAILPPVFGYITDKTDNIQYGYIVPLVCFAVVMLFGLIGYKTTQKEVANTPDPIL
>NZ_CP054139.1|WP_173415951.1|3966294_3966624_+|L-rhamnose-mutarotase
MKRYCLALDLVNDPTLIAEYEAYHQNVWPEIKASITTSGITDMEIYRFGNRLFMIMEVDDTFSFERKGAMDAGNLKVDEWEQLMWKYQQAIPGAKPGEKWVLMDRIFKL
>NZ_CP054139.1|WP_173415952.1|3966757_3967276_-|O-acetyl-ADP-ribose-deacetylase
MNSKIKLIKGDITKQHVDAVVNAANSSLMGGGGVDGAIHRAGGKQILDDCMDIINRQGRCKTGEAVITTGGKLPARYVIHTVGPVWNGGHKNEPELLANCYRNSLQLAVDKGIKTIAFPNISTGIYHYPKAEAAQVAINAVNNFLKDNDSIAEVTFVCFDEENFALYKDLLG
>NZ_CP054139.1|WP_173415953.1|3967426_3967948_-|acyl-CoA-thioesterase
MNAKSPKESYTIMNELVLPNDTNTLNNLMGGRLLHWMDIAAAISGQKHCNRTVVTASVDNVSFKQPIKLGDVVSIEAKVTRSFNTSVEVRLDVWAQNIPSGTRVKSNEAYYTFVALDAEGKTVPVPELQPETEDEVSLYEGALRRRQLRLILGGKMNPDDATELKALFFAAKQ
>NZ_CP054139.1|WP_173415954.1|3968456_3970364_-|molecular-chaperone-DnaK
MSKIIGIDLGTTNSCVAVMEGNEPVVIANSEGKRTTPSVVAFVDNGERKVGDPAKRQAITNPTKTIYSIKRFMGNQFNEVTKEAERVPYKVVKGDNNTPRVEIGDRKYTPQEISAMILQKMKKTAEDFLGQEVTEAVITVPAYFNDAQRQATKEAGEIAGLNVKRIINEPTAAALAYGLDKAHKDMKIVVFDCGGGTHDVSVLELGDGIFEVKSTDGDTHLGGDDFDQVIIDWLADEFKNDEGIDLRKDPMALQRLKEAAEKAKIELSSTTQSEINLPYVTAVDGMPKHLVKSLTRAKFEQLADSLIKRTIEPCKTALKNAGYSTSDIDEIILVGGSTRIPAIQEAVQKFFGKSPSKGVNPDEVVAIGAAIQGGVLTGEVKDVLLLDVTPLSLGIETMGGVMTKLIEANTTIPTKKSETFSTASDSQPSVEIHILQGERPMASANRTIGRFHLDGIPPAPRGVPQIEVTFDIDANGILHVSAKDKATGKEQKIRIEASSGLTDAEIKKMKDEAEANAEADRLEKEKVEKLNSADALIFSTEKQLKEYGDKIPADKKSSIEDGLKKLKDAYAAKDLDTIESAQTELNAAWQAASEDMYKASAEGAQPGPDAGAGPQGGGQQGNADSVTDVDFEEVK
>NZ_CP054139.1|WP_173415955.1|3970846_3971248_-|T9SS-type-A-sorting-domain-containing-protein
MKALIKSSAIVAVLALLSSAVFAAENPTKKAEPAAAKKDVVVFTALAQDKGVGVIIHKADVSKTSVAIYDAEGNVVMKDIQAKNGNDVLKGYVLSALENGKYTIKVTSNNEVTKRVVNVYNDENNQKAFLFEL

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Crispr_ID: NZ_CP054139_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP054139_8

5491463-5491548

Orphan

Consensus_repeat	Method
AGTTAAAAACTTGCCCGAATATTAC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP054139_8

>merge|NZ_CP054139|8|5491463-5491548|CRISPRCasFinder
AGTTAAAAACTTGCCCGAATATTACCACAGGTTACGCTGCGCTAAACCTGCGGCAGCAAGGAGTTAAAAACTTGCCCGAATATTAC

>NZ_CP054139|8|7|5491463-5491548|CRISPRCasFinder
AGTTAAAAACTTGCCCGAATATTAC	CACAGGTTACGCTGCGCTAAACCTGCGGCAGCAAGG
AGTTAAAAACTTGCCCGAATATTAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP054139.1\|WP_173417222.1\|5490904_5491453_-\|transposase	unknown	unknown	gnl\|CDD\|376616
NZ_CP054139.1\|WP_173417225.1\|5494993_5495536_-\|30S-ribosomal-protein-S16	unknown	unknown	gnl\|CDD\|237744
NZ_CP054139.1\|WP_173417218.1\|5485946_5487515_-\|CotH-kinase-family-protein	unknown	unknown	gnl\|CDD\|378045
NZ_CP054139.1\|WP_173417220.1\|5488889_5489888_-\|family-43-glycosylhydrolase	unknown	unknown	gnl\|CDD\|350095
NZ_CP054139.1\|WP_173417224.1\|5493680_5494691_-\|pectinesterase	unknown	unknown	gnl\|CDD\|178051
NZ_CP054139.1\|WP_173417230.1\|5503763_5504600_+\|helix-hairpin-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|224472
NZ_CP054139.1\|WP_173417228.1\|5501125_5501827_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173417216.1\|5483332_5483788_+\|DUF1569-domain-containing-protein	unknown	unknown	gnl\|CDD\|378981
NZ_CP054139.1\|WP_173417223.1\|5492358_5493666_-\|DUF1593-domain-containing-protein	unknown	unknown	gnl\|CDD\|377887
NZ_CP054139.1\|WP_173417219.1\|5487749_5488523_+\|cupin-domain-containing-protein	unknown	unknown	gnl\|CDD\|380339
NZ_CP054139.1\|WP_173417227.1\|5497518_5500836_+\|carboxypeptidase-regulatory-like-domain-containing-protein	unknown	unknown	gnl\|CDD\|379297
NZ_CP054139.1\|WP_173417899.1\|5491663_5492164_+\|5'(3')-deoxyribonucleotidase	unknown	unknown	gnl\|CDD\|284381
NZ_CP054139.1\|WP_173417217.1\|5483791_5485717_+\|redoxin-family-protein	unknown	unknown	gnl\|CDD\|239264
NZ_CP054139.1\|WP_173417221.1\|5490148_5490535_+\|DoxX-family-protein	unknown	unknown	gnl\|CDD\|379266
NZ_CP054139.1\|WP_173417226.1\|5495795_5497124_+\|signal-recognition-particle-protein	unknown	unknown	gnl\|CDD\|236780
NZ_CP054139.1\|WP_173417229.1\|5501932_5503690_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|153248
NZ_CP054139.1\|WP_173417213.1\|5480262_5480958_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|238877
NZ_CP054139.1\|WP_173417214.1\|5480983_5482513_-\|glycoside-hydrolase-family-28-protein	unknown	unknown	gnl\|CDD\|227721
NZ_CP054139.1\|WP_173417215.1\|5482615_5482942_-\|RNA-binding-protein	unknown	unknown	gnl\|CDD\|240845
NZ_CP054139.1\|WP_173417231.1\|5504596_5505124_+\|adenine-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|235028

Protein	Function_ID	Function_description	E-value
NZ_CP054139.1\|WP_173417222.1\|5490904_5491453_-\|transposase	gnl\|CDD\|376616	pfam01797, Y1_Tnp, Transposase IS200 like. Transposases are needed for efficient transposition of the insertion sequence or transposon DNA. This family includes transposases for IS200 from E. coli.	1.3163e-05
NZ_CP054139.1\|WP_173417225.1\|5494993_5495536_-\|30S-ribosomal-protein-S16	gnl\|CDD\|237744	PRK14521, rpsP, 30S ribosomal protein S16; Provisional.	1.74879e-73
NZ_CP054139.1\|WP_173417218.1\|5485946_5487515_-\|CotH-kinase-family-protein	gnl\|CDD\|378045	pfam08757, CotH, CotH kinase protein. Members of this family include the spore coat protein H (cotH). This protein is an atypical protein kinase that phosphorylates CotB and CotG.	1.7752e-47
NZ_CP054139.1\|WP_173417220.1\|5488889_5489888_-\|family-43-glycosylhydrolase	gnl\|CDD\|350095	cd08981, GH43_Bt1873-like, Glycosyl hydrolase family 43 protein such as Bacteroides thetaiotaomicron BT_1873. This glycosyl hydrolase family 43 (GH43) subfamily includes Bacteroides thetaiotaomicron VPI-5482 endo-arabinase (Bt1873;BT_1873), as well as uncharacterized enzymes similar to those with beta-1,4-xylosidase (xylan 1,4-beta-xylosidase; EC 3.2.1.37), beta-1,3-xylosidase (EC 3.2.1.-), alpha-L-arabinofuranosidase (EC 3.2.1.55), arabinanase (EC 3.2.1.99), xylanase (EC 3.2.1.8), endo-alpha-L-arabinanase and galactan 1,3-beta-galactosidase (EC 3.2.1.145) activities. These are inverting enzymes (i.e. they invert the stereochemistry of the anomeric carbon atom of the substrate) that have an aspartate as the catalytic general base, a glutamate as the catalytic general acid and another aspartate that is responsible for pKa modulation and orienting the catalytic acid. Many of the GH43 enzymes in this family may display both alpha-L-arabinofuranosidase and beta-D-xylosidase activity using aryl-glycosides as substrates. A common structural feature of GH43 enzymes is a 5-bladed beta-propeller domain that contains the catalytic acid and catalytic base. A long V-shaped groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller.	4.37509e-125
NZ_CP054139.1\|WP_173417224.1\|5493680_5494691_-\|pectinesterase	gnl\|CDD\|178051	PLN02432, PLN02432, putative pectinesterase.	3.00064e-20
NZ_CP054139.1\|WP_173417230.1\|5503763_5504600_+\|helix-hairpin-helix-domain-containing-protein	gnl\|CDD\|224472	COG1555, ComEA, DNA uptake protein and related DNA-binding proteins [DNA replication, recombination, and repair].	1.29772e-13
NZ_CP054139.1\|WP_173417216.1\|5483332_5483788_+\|DUF1569-domain-containing-protein	gnl\|CDD\|378981	pfam12867, DinB_2, DinB superfamily. The DinB family are an uncharacterized family of potential enzymes. The structure of these proteins is composed of a four helix bundle.	0.00162441
NZ_CP054139.1\|WP_173417223.1\|5492358_5493666_-\|DUF1593-domain-containing-protein	gnl\|CDD\|377887	pfam07632, DUF1593, Protein of unknown function (DUF1593). A family of proteins in Rhodopirellula baltica that are predicted to be secreted. Also, a member has been identified in Caulobacter crescentus. These proteins mat be related to pfam01156.	4.82605e-92
NZ_CP054139.1\|WP_173417219.1\|5487749_5488523_+\|cupin-domain-containing-protein	gnl\|CDD\|380339	cd02209, cupin_XRE_C, XRE (Xenobiotic Response Element) family transcriptional regulators, C-terminal cupin domain. This family contains transcriptional regulators containing an N-terminal XRE (Xenobiotic Response Element) family helix-turn-helix (HTH) DNA-binding domain and a C-terminal cupin domain. Included in this family is Escherichia coli transcription factor SutR (YdcN) that plays a regulatory role in sulfur utilization; it regulates a set of genes involved in the generation of sulfate and its reduction, the synthesis of cysteine, the synthesis of enzymes containing Fe-S as cofactors, and the modification of tRNA with use of sulfur-containing substrates. This family belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.	2.1612e-11
NZ_CP054139.1\|WP_173417227.1\|5497518_5500836_+\|carboxypeptidase-regulatory-like-domain-containing-protein	gnl\|CDD\|379297	pfam13620, CarboxypepD_reg, Carboxypeptidase regulatory-like domain.	6.64712e-20
NZ_CP054139.1\|WP_173417899.1\|5491663_5492164_+\|5'(3')-deoxyribonucleotidase	gnl\|CDD\|284381	pfam06941, NT5C, 5' nucleotidase, deoxy (Pyrimidine), cytosolic type C protein (NT5C). This family consists of several 5' nucleotidase, deoxy (Pyrimidine), cytosolic type C (NT5C) proteins. 5'(3')-Deoxyribonucleotidase is a ubiquitous enzyme in mammalian cells whose physiological function is not known.	1.61884e-44
NZ_CP054139.1\|WP_173417217.1\|5483791_5485717_+\|redoxin-family-protein	gnl\|CDD\|239264	cd02966, TlpA_like_family, TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.	2.30895e-29
NZ_CP054139.1\|WP_173417221.1\|5490148_5490535_+\|DoxX-family-protein	gnl\|CDD\|379266	pfam13564, DoxX_2, DoxX-like family. This family of uncharacterized proteins are related to DoxX pfam07681.	9.81479e-10
NZ_CP054139.1\|WP_173417226.1\|5495795_5497124_+\|signal-recognition-particle-protein	gnl\|CDD\|236780	PRK10867, PRK10867, signal recognition particle protein; Provisional.	0
NZ_CP054139.1\|WP_173417229.1\|5501932_5503690_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|153248	cd07986, LPLAT_ACT14924-like, Lysophospholipid Acyltransferases (LPLATs) of Glycerophospholipid Biosynthesis: Unknown ACT14924. 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 Pectobacterium carotovorum subsp. carotovorum PC1 locus ACT14924 putative acyltransferase, and similar proteins.	1.07689e-75
NZ_CP054139.1\|WP_173417213.1\|5480262_5480958_-\|hypothetical-protein	gnl\|CDD\|238877	cd01839, SGNH_arylesterase_like, SGNH_hydrolase subfamily, similar to arylesterase (7-aminocephalosporanic acid-deacetylating enzyme) of A. tumefaciens. 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.	1.89915e-18
NZ_CP054139.1\|WP_173417214.1\|5480983_5482513_-\|glycoside-hydrolase-family-28-protein	gnl\|CDD\|227721	COG5434, PGU1, Endopygalactorunase [Cell envelope biogenesis, outer membrane].	3.78162e-73
NZ_CP054139.1\|WP_173417215.1\|5482615_5482942_-\|RNA-binding-protein	gnl\|CDD\|240845	cd12399, RRM_HP0827_like, RNA recognition motif in Helicobacter pylori HP0827 protein and similar proteins. This subfamily corresponds to the RRM of H. pylori HP0827, a putative ssDNA-binding protein 12rnp2 precursor, containing one RNA recognition motif (RRM), also termed RBD (RNA binding domain) or RNP (ribonucleoprotein domain). The ssDNA binding may be important in activation of HP0827. .	6.64206e-19
NZ_CP054139.1\|WP_173417231.1\|5504596_5505124_+\|adenine-phosphoribosyltransferase	gnl\|CDD\|235028	PRK02304, PRK02304, adenine phosphoribosyltransferase; Provisional.	2.20632e-78

>NZ_CP054139.1|WP_173417222.1|5490904_5491453_-|transposase
MSRNYKFHNQQNPYFITFSVVNWIDVFTRIVYKEILLDSIKYCIANKGLEVYAWCIMSNHVHMVIGTRQLPMEAIVRDMKKHTSKEIVKAIRENPQESRQKWMIWMFEQEGAYNPANQYHQFWQQGVHPIELFSNEVMQQKVDYIHHNPVKAGWVSEPQHYLYSSARDYAGEKGLLDITLMV
>NZ_CP054139.1|WP_173417221.1|5490148_5490535_+|DoxX-family-protein
MSKKAINIIYWISTGLILAMMLFSAASSFMENPDGAKMLAAIGYRPYVLHLLAVAKVLGVIAILTPGFPRLKEWAYAGFMFDLIGATYSFYASGFAFKDWAFMLVLIAVLACSYIFYHKRLALKGSVA
>NZ_CP054139.1|WP_173417220.1|5488889_5489888_-|family-43-glycosylhydrolase
MKNIKLTLLACLLLPIITFAQGMRQMEPKKNIPLDSIRLSDPFIMADSKTNMYYMTGTGGLLWKSKDMKLWDGPYRVTQTDPNSWMGPRPMIWAAELHEYKGKYYYFATFTNRDVKIDTVKGNVIERRACHILVSDKPDGPYVPMQDPTYLPANKPTLDATFWIENGKPYMLYCYEWLQNWNGTVEKIALKPDLGGSIGEGKVLFRASDSPWSREKDENGKDRPNKVTDGPYVFQTKTGKLGIIWTSWVYNVYTQGVAYSASGKLDGPWVQEKNPITPPDFGHGMLFTDLNGKQLMCIHSHKSVNGKYIRIPHLFEVDLSGDKLVVGKEYKP
>NZ_CP054139.1|WP_173417219.1|5487749_5488523_+|cupin-domain-containing-protein
MMKNLLLLGMLIIAAGVAAQQKPVPSGVYHVADAPVVKSGDRESRKFAEGSTAELSYFRVHSSTQYKGAAPKPPHAQTDIEELIFVTEGTMKFTMGDKSQVLKKGSIVLVPPHTMQATENAGDGPLTYYVLMFRSNKPMDLERCAKAGGPVMLSADSLKYVPSAKGGGIKYFDRPTAMSEKLEMHITELKGRGPSHDPHTHVDTELILMLEGECEESINGKTYRGTAGDFFLMNSNELHGITNIQDKPCRYLAIRWK
>NZ_CP054139.1|WP_173417218.1|5485946_5487515_-|CotH-kinase-family-protein
MIKRYALLVLIALSVWCCKKGTTTIDGEEIKPVVKPDSAGITSAVIQAKNNTGKIAADVTCTISGTDITALVPDRMLVKKLALTFTTRTANTTVKVGDTTQVSGVTITDYTKPVILNVTSATGDVKTYTVKFKVFTGLPVLYITSASAISSKDNYVKGSVIIDANQGFTQEVNSMTMQIKGHGNSTWALPEFKKKPYKIKFDSKIMMLGMAAAKDWILLANYDDKTLMRNYLALQLGKRLGADFTPDCRFVEVVLNGEFVGNYLLTTSVEVNSNRVAIKELSDKNTSDSEITGGYLVELDQKLDGASWFRTTKNLPFVVKSPDAPTAKQLDYIHNYFQAAEDALFSADFKDPDKGYAKYINPDSFITWYFTNEIFENDARDFSSIFYYKDRDGKLNMGPIWDFDLSAGNINYTPAQNPTGIWFIRDATWMIRLAQDPTYDLKVRAKWAQIREKEVKQIFTDIDQTAAYLKLSQQENFKKWPILDQYVWPNAVWLGTYDKEVAYMKDFLQQRINWMDANMGSW
>NZ_CP054139.1|WP_173417217.1|5483791_5485717_+|redoxin-family-protein
MMQKFVKAALFVWLTGCAQTLLAQNPLTSSPAFPERGQEVTITYHAGSPGAKIPAGAKNISLVFTYSTFYELPYKLPLVQHGNDWSVTFKLQRYATFATFYVQSDNIIDKPADNKHYNIAVYTNGKRVENGYLHEAYSLSAQMGRSALVHDMQRQLLQTELENYPDNYEAKIRLITNGIAGTKDAAEKKKLYEQGEQMIAGYFAQAPTVMGRINKVTMGYLILGENSRVDSVHRVVVNKYPNSDAAMDLLTEIVNKEKDTTKRIIKLEQALKTAKDPRGDGAKSLHSDLFDYYAARKNAPKALYHARFFRNDTSPHRARTLKEIAETLTKNHLAPDTALKYAGQALAIVDTYPVGIIRYFPEFGYIPAYVADSTRAKQVGMARASLLSIAAINHISKGHTITAIKEADEAVTLSDDKQTLNNIAWVYERQHQPEKAFNTYWKILLKEPGDSLALKASRKNYQAYKGSADGYKERLAELEKIQKQQMTRLVKKELLNLPGPQLLAITDLQGHPLDKESLKGKVVIMDFWATWCVPCMEELPYLQKVYTKYKDNPRVVFMVINSGSKNTLADAQNWAKQHSNYTFPLFYNGDSNIGDKVGFNLIPTIAVLDRSGKMQLRTIGFEGAVLEQKLSAGIDLLLEGM
>NZ_CP054139.1|WP_173417216.1|5483332_5483788_+|DUF1569-domain-containing-protein
MKSVFNPADVAELTGRINNLTPATQPQWGKMSVSQMLAHCNVSYEMVYDPEKHPKPKGLMKFIVKAFVKKVVVGPKPYKRNTPTAPAFIIKDDRSFETEKARLTDYLNQTQQLGETHFDGKESHSFGPLTVGEWNTMFYKHLDHHLMQFGV
>NZ_CP054139.1|WP_173417215.1|5482615_5482942_-|RNA-binding-protein
MVKLYVGGFPLDTTEMELVQLISLHATVSTIKIVRDKKTRISKGYAFLEITERAGLDAAVDALDGYMLHGKELRLNMVEEAPPAPVRSYVKVAPRTGPPKKMRPRRNT
>NZ_CP054139.1|WP_173417214.1|5480983_5482513_-|glycoside-hydrolase-family-28-protein
MKKKYLLLALLLSGLSAAFATEAPQKLMVAPGTLSATSATLIWDKPVKYDDIVRYHIILNGKEAGTTAKGNYILNGLSPVKTYSCAVRSEDRDGKLSAPSAPVKFNTQHQGKTFNVTDFGAKGDGATINTKAIQKAIDACPVNGTVLIPEGTFMSGALYLKSHMTLQIAKGGVLKGSVSDVDYLPFINNRFEGWEMKTYASLINAGIMNNKGGYTVDDLHIKGEGTISGGNSPLAKNMMDHGGLRVRGRLICLLNCRDVEIQGLNIQDSPCWTIHYIYSKGVTCHDLKIVSTAHNGDGLDPDSSDDSYIFNCSFSTGDDCIAIKSGKNPEGFTIGKPTRNVRITDCDFIKGHGISIGSEMSGGVSDVLVQDCKAGALLNGMQIKGTKERGGYVKNVTVADCQLLKITIFTALNYNNDGAAAPEPPTFANFTFRNIDLSKASVAKGPVMDLNGFKDDAHKLKDCSFTNIITPDNARIVIKDAERLNFTNVKSASGAKPVYEANNSTNVVY
>NZ_CP054139.1|WP_173417213.1|5480262_5480958_-|hypothetical-protein
MKNKMRLMVVLLSLLPFLSHAQGTALSDKKLNIFTLGDSNGTFPHSWPIQLKTALPNATVFNISKSGRTIGFINLNDTTANSLMVIDGNLKKAADATGDRPYDFVVMELGTNDAKAIFDPRQQEVPGNLETLIKKIKNCPYPTINKAKIIIISPPPYGSKTDTQEKYIGGNKRVEAMSKSFEKIAKKNGCLFVNGHKTPGLDMETMSTDGLHMDAVASRKLIEPVVALMVK
>NZ_CP054139.1|WP_173417899.1|5491663_5492164_+|5'(3')-deoxyribonucleotidase
MDEVLADPIGKFIDIYQREHGYTYTLDQMHGKEFRDLLPEELQPTLREYINRKGFFRDLELIPDSREVVEQLCQKYDVFIVSAAMEFPNSLEDKLHWLGDHFPFIPWTNIIFCGYKIVKADIMIDDRIRNFSGFDGRKLLFTSPHNIAITEYERVNTWDEVAVLLL
>NZ_CP054139.1|WP_173417223.1|5492358_5493666_-|DUF1593-domain-containing-protein
MIFKVNIKAIIFACLCFILTGLAYAQQPVPVKPRILISTDIGGTDPDDNQSMIHFLIYSHLFDTEGLVSSPSYGAGNKEEILKMIGLYEKDLPKLQQHQKGYPTPDALRAICKQGRKGAAPYKGYLTATEGSDWIIKCAKKEDTRPLWVLVWGGLEDVAQALHDAPEIASRIRVYWIGGPNKKWSANSYAYIAANFPKLWFIECNSSYYGFFSGNGSPENLKPANYYNNFISNAGYMGAAFKSYYKGIPKMGDTPSLLYMMDGDPKNPLRESWGGSFIKFNHSARIVYDRATTITDTVPTFSTVEFHFKGPKINISPDSACFTLTMQAGIGEQKWDGFYNGNGDYVIRYCPKQTETLNYKVSSKIPGFEPLQGKLVISNLWPGQPHQTDYRLGSNWYTDKPDASLYDGIWQGSQTVLKWRSDIMLDWGKRWAWLK
>NZ_CP054139.1|WP_173417224.1|5493680_5494691_-|pectinesterase
MTRICTIILLLIAPLCQAAKTRIVVDPSGKGDFRTIQQALQSLPDSAAEDRLIFIKNGFYREQLSIRKNHITLQGESKTGTVISGSISHLIYTCQHPGDKNSAVMNIDGNDITLRDLTVENTYGHDAADSVFIDCTNAQTGKPEKTKVVKTAHQFTLKTGTATRLKVINCIVRSYGQDTVSPWSGTGMYYFKDCTLIGGTDFYCPRGWAYAENCTFIVNVPGAIAIWHDGSKGRDIKSVFRNCYFKGEQHFQLGRYHHEASFYLIDCHFDKNMMDKPIYKAETAKPMVWESTVYYSNAHTDGPKFNWLKDNLYQAPGAPKAGDINAAWTFNRKWNP
>NZ_CP054139.1|WP_173417225.1|5494993_5495536_-|30S-ribosomal-protein-S16
MATKIRLQRHGKKGKPFYYIVVADSRAPRDGRFIERLGSYNPNTNPATIDINFDKTLDWVNNGAQPTDTCRAILSYKGVLYKKHLQGGLKKGALTEEQVEAKFAAWLEGKDSKITGKKDSLSTAKEAAKKAALAAEAKRNADKAAAIAAKNTPPAEEVEEAPVAEAEEAPAADEAAESAE
>NZ_CP054139.1|WP_173417226.1|5495795_5497124_+|signal-recognition-particle-protein
MFENLSDKLDRAFKVLKGQGTITEINVAETMKEIRKALLDADVNYKTAKAFTDEVRQKAIGQNVLTSISPGQLLTKIMNDELTDLMGGSTADLNFPATPTIILIAGLNGAGKTTFSGKLANFLKTQKNKKPLLVAGDVYRPAAITQLQVLGEQIGIPVYADLESKDPIGIARAGVAQAKQNGNNVVIIDTAGRLAIDEAMMVEIEQVKAAVNPHEILFVVDAMTGQDAVNTAKVFNDRLDFTGAVLTKLDGDTRGGAALSIKSVVNKPIKFIGTGEKMEALDVFHPDRMASRILGMGDVVSLVERAQQQFDEKEAAELQKKIRKNKFDFNDFYGQIQQIKKMGNMKDLMGMIPGVGKMMKDVEVGDDAFKNIEAIIQSMTKFEKENPDAINQSRRTRIAKGSGTNIAEVNRLLKQFEDMRKVMKQMSNPAAMANMMRRMPKM
>NZ_CP054139.1|WP_173417227.1|5497518_5500836_+|carboxypeptidase-regulatory-like-domain-containing-protein
MKKLYFIIFSVLILGIANEANAQITTGVISGKVTDAKGGTLPGVTISVVNTSTGTRYGNQTNADGRYTITNVNPGGPYVITASFVGYKKQELTGITVNLGNATYNFQLLDESTALKEVVVKSTGGTTKTGASTRINPNQLRTMPSLSRSLQDLTRLTPQSNNNSFQGTNYRYNNVTLDGAINNDAIGFSPSLGGQNNVSGQVGSSTRTSPISLDAIQDIQVYIAPYDIKIGNVLGGSINAVTRSGTNTVTGSIYGFGRGAFMIGANRLPTNVGGDNASEPSAFHDFQFGGRLGLPIVKDKLFLFTNEEFARRQDPVIFAAGSAGSAGILSEQDAIDITKAFKSYTGGLDPGVYGNTTIFSNSNKFFNRLDWNINDKNQLTLRNNTITSTATNLERDQQNFRFSGIDYTSHNNSNSTVAELKSRFSNSVSNSFLLGYSNVHDYRDPNSSPALPQIEITGRTPGTTIFLGTDREAAIFDMHQKTFEITDNFTLNTGKHTFTFGTHNELYNITYNFVNSWNGRDAYSSIDAFTGAFNSNPATVTAFTPLRVRANFNYTNNTRDYILANPSAQFKVNLLSLYAQDEIQAADNFKLTGGLRIDYAGVPNKQPLSAKTTGAAVDPNYGTTFTYTKPSEIQNKYLDNIEFNGRLSFNYDINGDQSAVIRGGTGTFTGRVPFAWFGYAFYNNGNTYGAYDKNNINTTTNTITPGTNPTQAPANGGLGFVNQQVPAPNTSATGPTQVDMIDNNFKMPQVWRSSLAFDYKTQDQWRFSIEGIYTSVIHDLKFQQTNTTDQVTYYPYDVQKQQPIFVNTKPSANFTNAYLLSNTSEGKRYSITGQVGKTWPMGLNAEFSYTYGQSKDITNGIRNSMESNWQLNQALNPNSPTLAFSNFDVRHRIVANLSYKLTYGADKKNSSNFALFFNAASGTPYSFGFLPSAIDGTGQQVSLAYIPSVGETIKFFSTTPNTPSAAEQAMANAFDQYINADQYLSTRRGKFTERNGARTPWNTSADFRFTQDFSVGSGAKKQMLTFTFDIINLTNLLNRNWGHYYFSPNTFNSTSSIGLTRNVTPSFANAATTYPTYKFVNPGVPYAVDPFQSRYQMQFGVRYTF
>NZ_CP054139.1|WP_173417228.1|5501125_5501827_+|hypothetical-protein
MKKPSPKAVAPRLNCDKAGCLLCCRAGLLLIMLLPAFKTHAQDFFPEQKDYAVSVGTDLELPGKNLSDYRKAVAANVGIMRLLDRFTVGVNFSYREFSPITPVVVEQIDPAHQSTSTYSSYSTFLFYLSGAYNVSLSEKVKAYGGLNVGVGYNTSSILYQQDDTNLYFGGGVKQLYAAPKLGLSYAINNNVDVEIHAAYNLLAQTGNLTNPTTHVTRTSFSSLTTGLGLMFKF
>NZ_CP054139.1|WP_173417229.1|5501932_5503690_-|GNAT-family-N-acetyltransferase
MKIITKEEFAKATKLDKLKMPGLAALLMEIMKINQVNDLFAQAQPKQGPEFVDAILEGVGVTIDFDERELKNIPSDGAFIAIANHPYGGIEGMVLLKILCMARPDAKLMANFLLKKIPNLSDYFIAVNPFENIDHSSSISGLKSTLELLKNGTPIGIFPAGEVSTYKIEQQQVTDRKWHPVVGKIIAKAKVPVVPIYFHGNNGLLFNLLSMIHPALRTAKLPSELFNKHGHTIKLRIGKPIHIADVPDSNNPTKLLNYLRAKTYALGTGLEEEKKLFSPRNLFKIKQDPEEVAFETDRSIIEREVEPLREDHLVWTEKNYEVYIAPTSLIPNIIREIGRLREITFREVGEGTNKSIDLDEYDIYYHHLFIWDVETKLIVGAYRIGLGDEIFYSRGKKGFYTAEVFKIKGQFTSVLKRSLELGRSFIRAEYQGKALPLFLLWKGILKYLIDNPRYRYLIGPVSISNTFSKFSKSLIVDYITKNHFDHDMAQYVRPRKKFKVDFSKIDTDLLMAGADDSLKGLDSIISEVETRNMKVPVLLRQYIALNAKIICFNIDPKFADCLDGFLVLDLHNVPHEMLEKLGKNL
>NZ_CP054139.1|WP_173417230.1|5503763_5504600_+|helix-hairpin-helix-domain-containing-protein
MSLSPKKYFSVTKKEWNGLVVLMILIALVLVAPYVYQSFHKNETIDVKDFNAAVARLKGTGLVDSNTTANATPFRFNPNNLPPQQWAKLGLTEQQIGTIKNYEAKGGHFNSKADLKKMYSISAEDYKRLAPYIDLPEKAGYVEKTNAVVEINSADTLKLMQIRGIGSGYARLIIRYRDRLGGFYKKEQLKEVAGLDSLTYQDIIPFIKVDEAKIIKIDLNKATQNSLAVFPYLSYKQRNAIVEYRNQHGDYKELADLKNIPIIDDVLLRKIEPYISLK
>NZ_CP054139.1|WP_173417231.1|5504596_5505124_+|adenine-phosphoribosyltransferase
MIAEEIKKAIRDIPDFPKPGIVFKDITPILKDAALCDRILDAFAEQLKDTKIDVVAGVESRGFLFGLSLAGRLGVPFIPVRKAGKLPFTIKQKAYKLEYGTATIELHTDAFEPGQHILIHDDLLATGGTVTAASELIQEMGGIVAGFSFVVGLGFLNGRERIAPINDNILVLADY

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Crispr_ID: NZ_CP054139_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP054139_9

5647576-5647674

Orphan

Consensus_repeat	Method
TAGCGATGGGTTTCAAACCCATCGCTA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP054139_9

>merge|NZ_CP054139|9|5647576-5647674|CRISPRCasFinder
TAGCGATGGGTTTCAAACCCATCGCTACGGTAGGAATAAAAATATGAATTTTAGGCCTTGTAGCATGTATTATAGCGATGGGTTTCAAACCCATCGCTA

>NZ_CP054139|9|8|5647576-5647674|CRISPRCasFinder
TAGCGATGGGTTTCAAACCCATCGCTA	CGGTAGGAATAAAAATATGAATTTTAGGCCTTGTAGCATGTATTA
TAGCGATGGGTTTCAAACCCATCGCTA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP054139.1\|WP_173417347.1\|5653654_5654575_+\|ribosome-small-subunit-dependent-GTPase-A	unknown	unknown	gnl\|CDD\|234631
NZ_CP054139.1\|WP_173417338.1\|5641246_5642572_-\|amidohydrolase	unknown	unknown	gnl\|CDD\|349917
NZ_CP054139.1\|WP_173417345.1\|5649543_5650521_-\|homoserine-kinase	unknown	unknown	gnl\|CDD\|234920
NZ_CP054139.1\|WP_173417334.1\|5637674_5638199_-\|DUF177-domain-containing-protein	unknown	unknown	gnl\|CDD\|376863
NZ_CP054139.1\|WP_173417909.1\|5639364_5639955_-\|crossover-junction-endodeoxyribonuclease-RuvC	unknown	unknown	gnl\|CDD\|234587
NZ_CP054139.1\|WP_173417340.1\|5643891_5644173_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173417351.1\|5656117_5656828_+\|DUF4349-domain-containing-protein	unknown	unknown	gnl\|CDD\|379526
NZ_CP054139.1\|WP_173417337.1\|5640689_5641124_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173417349.1\|5655192_5655558_-\|GxxExxY-protein	unknown	unknown	gnl\|CDD\|275083
NZ_CP054139.1\|WP_173417346.1\|5650706_5653157_-\|bifunctional-aspartate-kinase/homoserine-dehydrogenase-I	unknown	unknown	gnl\|CDD\|181856
NZ_CP054139.1\|WP_173417348.1\|5654678_5655137_+\|D-tyrosyl-tRNA(Tyr)-deacylase	unknown	unknown	gnl\|CDD\|376833
NZ_CP054139.1\|WP_173417342.1\|5647094_5647526_-\|IS200/IS605-family-transposase	unknown	unknown	gnl\|CDD\|376616
NZ_CP054139.1\|WP_173417343.1\|5647701_5647932_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173417336.1\|5640018_5640681_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP054139.1\|WP_173417350.1\|5655783_5656116_+\|nucleotide-pyrophosphohydrolase	unknown	unknown	gnl\|CDD\|212138
NZ_CP054139.1\|WP_173417341.1\|5644316_5647043_-\|beta-propeller-fold-lactonase-family-protein	unknown	unknown	gnl\|CDD\|225926
NZ_CP054139.1\|WP_173417344.1\|5648060_5649365_-\|threonine-synthase	unknown	unknown	gnl\|CDD\|236418
NZ_CP054139.1\|WP_173417335.1\|5638501_5639269_+\|SMI1/KNR4-family-protein	unknown	unknown	gnl\|CDD\|378155
NZ_CP054139.1\|WP_173417910.1\|5657016_5657646_-\|methyltransferase-domain-containing-protein	unknown	unknown	gnl\|CDD\|226975
NZ_CP054139.1\|WP_173417339.1\|5642637_5643633_-\|phosphotransferase	unknown	unknown	gnl\|CDD\|270702

Protein	Function_ID	Function_description	E-value
NZ_CP054139.1\|WP_173417349.1\|5655192_5655558_-\|GxxExxY-protein	gnl\|CDD\|275083	TIGR04256, conserved_hypothetical_protein, GxxExxY protein. Members of this protein family average about 130 residues in length and include an almost perfectly conserved motif GxxExxY. Members occur in a wide range of prokaryotes, including Proteobacteria, Perrucomicrobia, Cyanobacteria, Bacteriodetes, Archaea, etc.	1.94285e-51
NZ_CP054139.1\|WP_173417346.1\|5650706_5653157_-\|bifunctional-aspartate-kinase/homoserine-dehydrogenase-I	gnl\|CDD\|181856	PRK09436, thrA, bifunctional aspartokinase I/homoserine dehydrogenase I; Provisional.	0
NZ_CP054139.1\|WP_173417345.1\|5649543_5650521_-\|homoserine-kinase	gnl\|CDD\|234920	PRK01212, PRK01212, homoserine kinase; Provisional.	1.91162e-111
NZ_CP054139.1\|WP_173417350.1\|5655783_5656116_+\|nucleotide-pyrophosphohydrolase	gnl\|CDD\|212138	cd11531, NTP-PPase_BsYpjD, Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain putative pyrophosphatase YpjD from Bacillus subtilis and its bacterial homologs. This family includes a putative pyrophosphatase Ypjd from Bacillus subtilis (BsYpjD) and its homologs. Although its biological role has not been described in detail, BsYpjD shows significant sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, BsYpjD contains a single MazG-like domain.	1.86132e-39
NZ_CP054139.1\|WP_173417909.1\|5639364_5639955_-\|crossover-junction-endodeoxyribonuclease-RuvC	gnl\|CDD\|234587	PRK00039, ruvC, Holliday junction resolvase; Reviewed.	8.50337e-73
NZ_CP054139.1\|WP_173417351.1\|5656117_5656828_+\|DUF4349-domain-containing-protein	gnl\|CDD\|379526	pfam14257, DUF4349, Domain of unknown function (DUF4349). This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 282 and 353 amino acids in length. There is a single completely conserved residue D that may be functionally important.	4.07197e-51
NZ_CP054139.1\|WP_173417334.1\|5637674_5638199_-\|DUF177-domain-containing-protein	gnl\|CDD\|376863	pfam02620, DUF177, Uncharacterized ACR, COG1399. This family is nearly universally conserved in bacteria and plants except the Chlorophyceae algae. Thus far, mutantional analysis in bacteria have not established a function. In contrast, mutants have embryo lethal phenotypes in maize and Arabidopsis. In maize, the mutant embryos arrest at an early transition stage.It has been suggested that family members specifically affect 23S rRNA accumulation in plastids as well as bacteria.	3.05902e-14
NZ_CP054139.1\|WP_173417347.1\|5653654_5654575_+\|ribosome-small-subunit-dependent-GTPase-A	gnl\|CDD\|234631	PRK00098, PRK00098, GTPase RsgA; Reviewed.	5.63699e-165
NZ_CP054139.1\|WP_173417348.1\|5654678_5655137_+\|D-tyrosyl-tRNA(Tyr)-deacylase	gnl\|CDD\|376833	pfam02580, Tyr_Deacylase, D-Tyr-tRNA(Tyr) deacylase. This family comprises of several D-Tyr-tRNA(Tyr) deacylase proteins. Cell growth inhibition by several d-amino acids can be explained by an in vivo production of d-aminoacyl-tRNA molecules. Escherichia coli and yeast cells express an enzyme, d-Tyr-tRNA(Tyr) deacylase, capable of recycling such d-aminoacyl-tRNA molecules into free tRNA and d-amino acid. Accordingly, upon inactivation of the genes of the above deacylases, the toxicity of d-amino acids increases. Orthologues of the deacylase are found in many cells.	1.13081e-85
NZ_CP054139.1\|WP_173417342.1\|5647094_5647526_-\|IS200/IS605-family-transposase	gnl\|CDD\|376616	pfam01797, Y1_Tnp, Transposase IS200 like. Transposases are needed for efficient transposition of the insertion sequence or transposon DNA. This family includes transposases for IS200 from E. coli.	1.69745e-29
NZ_CP054139.1\|WP_173417338.1\|5641246_5642572_-\|amidohydrolase	gnl\|CDD\|349917	cd05667, M20_Acy1-like, M20 Peptidase aminoacylase 1 subfamily. Peptidase M20 family, uncharacterized subfamily of bacterial proteins that have been predicted as N-acyl-L-amino acid amidohydrolase (amaA), thermostable carboxypeptidase (cpsA-1, cpsA-2 in Sulfolobus solfataricus) and abgB (aminobenzoyl-glutamate utilization protein B), and generally are involved in the urea cycle and metabolism of amino groups. Aminoacylases 1 (ACY1s) comprise a class of zinc binding homodimeric enzymes involved in the hydrolysis of N-acetylated proteins. N-terminal acetylation of proteins is a widespread and is a highly conserved process that is involved in the protection and stability of proteins. Several types of aminoacylases can be distinguished on the basis of substrate specificity. ACY1 breaks down cytosolic aliphatic N-acyl-alpha-amino acids (except L-aspartate), especially N-acetyl-methionine and acetyl-glutamate into L-amino acids and an acyl group. However, ACY1 can also catalyze the reverse reaction, the synthesis of acetylated amino acids. ACY1 may also play a role in xenobiotic bioactivation as well as the inter-organ processing of amino acid-conjugated xenobiotic derivatives (S-substituted-N-acetyl-L-cysteine).	0
NZ_CP054139.1\|WP_173417341.1\|5644316_5647043_-\|beta-propeller-fold-lactonase-family-protein	gnl\|CDD\|225926	COG3391, COG3391, Uncharacterized conserved protein [Function unknown].	4.71609e-12
NZ_CP054139.1\|WP_173417344.1\|5648060_5649365_-\|threonine-synthase	gnl\|CDD\|236418	PRK09225, PRK09225, threonine synthase; Validated.	0
NZ_CP054139.1\|WP_173417335.1\|5638501_5639269_+\|SMI1/KNR4-family-protein	gnl\|CDD\|378155	pfam09346, SMI1_KNR4, SMI1 / KNR4 family (SUKH-1). Proteins in this family are involved in the regulation of 1,3-beta-glucan synthase activity and cell-wall formation. Genome contextual information showed that SMI1 are primary immunity proteins in bacterial toxin systems.	6.40122e-08
NZ_CP054139.1\|WP_173417910.1\|5657016_5657646_-\|methyltransferase-domain-containing-protein	gnl\|CDD\|226975	COG4627, COG4627, Uncharacterized protein conserved in bacteria [Function unknown].	1.92871e-11
NZ_CP054139.1\|WP_173417339.1\|5642637_5643633_-\|phosphotransferase	gnl\|CDD\|270702	cd05153, HomoserineK_II, Type II Homoserine Kinase. This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).	3.80231e-44

>NZ_CP054139.1|WP_173417342.1|5647094_5647526_-|IS200/IS605-family-transposase
MPQSYSALWVHLIWSTKNRQPILTPDLRKELFNVTNSISKEYEIYLDCINGIEDHVHLLVRLRTDQTVADVVKTIKGNTWEHFKEIPDQYITWQDGFAAFSVSPANLKAVRNYIYRQQIHHKNKSFTDELKEIKAGIRLQDKS
>NZ_CP054139.1|WP_173417341.1|5644316_5647043_-|beta-propeller-fold-lactonase-family-protein
MSSYKTIAPAIIMALALSACHQPNRTHALKNADQVNQHNSYDDSTLRQTNLPVLMPYNRIIDPAGEVLRYGEDTQENHSLDLKAIPGTDLVAVEDRYGMSVVSISDHKVIDRWLYTADAKYRGQMSTFSGLEVYKTADGKVKILWGSANAGNKQSFVMEAGWDGQKLSLSKSFAIKPEGESPLALPNKVLMAQQDGINYLYVVLNGNNQLLKINWDKQELTWAKPTGVAPYGMAKVGNKIYLSNWAGPQVTDKNAEAAGVPYGKAYTNAQTGATSRGTVSVFDANSGNVIKEIETGLHPNDVIASADGRFIYVANGNSDNISVINTTDDKIAETIDVSLHPGDKGFIGDTPNAITLSDDGRTLYVSNGLDNAVAVVQLSGKSATKGSGSSMIKGFIPTEAYPAGLIIKNNTLVVTNLEGEGSRINAKDMKRKPSDLPATNGDAFNSHRQLATVSFIPLPDDKTLETYTKRVNQLNLAYRAELARLMPRKDVAPVPVPERIGEPSVFQHVIYIIKENRTYDQVLGDVKAGNGSPDLCIFGEQVTPNEHQLVKDFLLMDNYYVSGKSSAEGHQWTDAAMVTDYLEKNVRAWFRSYPHVQEDALVYDKKGFIWNNAADHGKTVRIYGEACTPHFKKGLTWLPIYNDYMAGKMLEFNNTSTISRVRPMLSPTYPGYDDHDINDQIRASAFIKELNDYEKQPGDKLPQLMVMALPADHTGGTTPRLPTPRAMVADNDLALGRIVEAVSKSRFWKNTVIFVTEDDSQAGWDHVSAYRTTGFVISPYSRLKQTVHTNYNQTCIVRTIEQILGIPPMNSVDATALPMFNCFTQRPDNSFVYTHVANQVPLNEMNAKLSMLKGIDLYYARQSMRPEFKHIDGGNDDLMNRIIWNSVKGKKPYPKKYAGHDTGDDDDD
>NZ_CP054139.1|WP_173417340.1|5643891_5644173_-|hypothetical-protein
MKTVNITGTLQNQQGSAVIITVSGPDHHAMTYTFYSDFNLPLAVIPGDYYISVSAFTSGPFTIDISGDCQNLMPEVPFVFKGIRQTFYLNVAK
>NZ_CP054139.1|WP_173417339.1|5642637_5643633_-|phosphotransferase
MSTIFPATYSTLCPVALAKYITDKYGFANTDCRLLVRGVGDTYLVNTLSDKYILRVYRSSHRNLPQIQAEVDLLLTLNKAGVPVSHPLTDKSGDAIQAVEAIEGIRHAVLFTYAHGTVVRQMSTTQLQVLGREMARMHQVSAGVNPAGTRCGFDFDTTLYQPLEMVKPNFADLAEDYQWLQETAGRAVNVLTNLSAGGFTSGYCHFDFLPKNFHFDSDAITFFDFDFMGYGWLVNDIATFHQHLCLDIYTGRATQEAASEAYDIFLEGYQQVRPLSEQEKAAVPYLGLGFWLFYMGFHTTHDQFFAFTQASHLKGIINYLRSFVATTWNIS
>NZ_CP054139.1|WP_173417338.1|5641246_5642572_-|amidohydrolase
MKKLFLLSFSLISLSALAQTDASKTLVAKKADAIEAKVIAWRRDFHEHPELGNHEVRSAEIIAKHLQSLGIEVKTGVATTGVVGILKGGKPGPVVALRADMDALPVTERVKLPFASKVKTMYNGAETGVMHACGHDSHMAILMGAAEVLAVMKNDLHGTVKFIFQPSEEGVLPAELKDGKKSGAEQMVAEGVLENPKVDAVFGLLIQSYQPAGTITYRPGGDMAAVNDMQIIVKGRSAHGAYPWSSVDPVVTAAQIVNNLQTVVSRNLHITDNPAVVTIGAINGGNRSNIIPEAVTMLGTIRTFSPGDEKMIIERIKTIATKTAEANGATVEIKIPYSSHYPVTYNNPELVAKMLPTLEATAGKSNVLLRNAETGAEDFSFYEEKVPGIFLHLGGLPKGSDPTKAPAHHTPDFFIDESGFTLGVKALCNLAIDYMNMPKGK
>NZ_CP054139.1|WP_173417337.1|5640689_5641124_-|hypothetical-protein
MKLNGLITYTDTYSHVLNCFGRPDSITSINVDKTDSTNNTWRVYFKNSSFIKYGDSVNLERIDLATLPGIFVTCGKFRLNRTSTIDSLKFFHPAEMNSELTADEQTRYTLWGIADKTDLDYSFWMLYFDKSTRRLLFMKHISFS
>NZ_CP054139.1|WP_173417336.1|5640018_5640681_-|hypothetical-protein
MPELLTYRKFNDLALANNLAEILAAHHIEYVLEESPDLFNPSFATRTEMSREYWVKISSDDFDRANQVIEAYEGRYADEADLDHYLFGFDDDELMEIINKPDEWSAFDYALAKKILKERGVVIDAAREKEIGEKRMQELKKPEHSEHFWVMVGYFFALFGGVLGFFIGWHLWKSKKTLPNGEQVFVYSPGDRNSGKWIFYLSVVGLIAATYKLYILAPPY
>NZ_CP054139.1|WP_173417909.1|5639364_5639955_-|crossover-junction-endodeoxyribonuclease-RuvC
MQQAPQKERIILGIDPGTAVMGYGLVKESGNKLELISLGVVKMASLDDHMLKLQRIFEKTVALIDNYKPDCLAIEAPFYGKNIQVMLKLGRAQGTAIAAALSRNLPICEYAPRKIKQSITGNGNATKEQVAAMLQTLLKFKETPEFLDATDGLAVAVCHSFQRITTGRGNKISYSGWESFVKENTQRVASPLKVKK
>NZ_CP054139.1|WP_173417335.1|5638501_5639269_+|SMI1/KNR4-family-protein
MINIDEIINYLRENHTEISIELKPGASAELIMQVEEIYKLKLPDDVRKFYEFTNGFELLDDHIFNIISLEDIIDNKTQYNDAYINIAEYLIYSDVWSLIIDPADHNNYQITNSDHTNNKEITLTKSLADFLHHFIIGGLFEKEGLYHWYNELLVEKLTSSPGNLAGTFYFEELFRITGRGPVMSGQITSGKLSASNLFWFENDDYKTIIDIESIELGRNAKGGFVGLMLSKYIHHSTEKKIKKLRGSTINIYRFN
>NZ_CP054139.1|WP_173417334.1|5637674_5638199_-|DUF177-domain-containing-protein
MKSLRTYAIPFTGLKLGKHEFDYVITDAFFDDFEYSLVKKANLQCKVDLEKQETMLILNFSIKGDIQLTCDKCLAGYPQQVDIHEQQIAKFSDEPVDEDEEVIALGKNDHEINVAGLMYEYINVAVPFIATCGKPGATPYCDKDMLNRLTELSASDEQTEQLNDPRWDALKNIK
>NZ_CP054139.1|WP_173417343.1|5647701_5647932_-|hypothetical-protein
MVPYANKQGDSGVAAYEAAPGSITVQFVGGDIYLYTNNSAGAINIKQMKHLAERGSGLSTFISQCVKDGYESKLNS
>NZ_CP054139.1|WP_173417344.1|5648060_5649365_-|threonine-synthase
MNLYSTNNTALNVSFKEAVFNSMPQDKGLYMPVAINPLPQEFIANLDQYTLPEIAFTVAKHMLAGAIPDADLKALIDDAINFEAPVVELEENVYVLELFHGPSLAFKDFGARFMSRVMGYFLEAGEKQLDVLVATSGDTGGAVALGFLGVPNTRVTILYPKGKVSDIQELQLTTNGQNIRALEVDGTFDDCQALVKQAFTDAQLNEAFRLTSANSINIARLIPQTFYYFNAYAQLLKQGKSKVVFAVPSGNFGNIGAGLLAWKMGLPVQQFIAATNANDTVPEFLKTGVYQPKPTVATLSNAMDVSSPSNWVRIADLFKNDTAELKKLITGYSFNDEDTVKAIVKIFGAYKYVACPHTAIAWLALTDWLDKQDDDVTGVFLSTAHPCKFPDVFPEQIGKAVEVPAQVKTLQEKPRLATPLKADFNEFKSYLLNN
>NZ_CP054139.1|WP_173417345.1|5649543_5650521_-|homoserine-kinase
MDTQLQELTQTETAKPGTSIQIFAPATVANVVCGFDVLGFAVNAPGDEVVMRVTDKPGISISKITGDNGRLPMDPAKNTVSVSVRHYLESIGRTDLGLDIELHKKMPIGSGLGSSSASTVAGLFAAKTLLDDQRDVAQLLPFAMKGEEMACGHGHADNVAPALMGGFVLIRSYEPLDVVRLPHPKDLWCAIVFPDVDVPTREARQIIRNKINMKDAVTQWGNVAGLVSGLFMNDIGLIGRSMKDVLVEPVRSMLIPGFYQMREQAMELGAVSFGISGSGPSVFAFTRDEQTAHNITHKLQQYLTGMKINSNAYVSTINDAGPRVI
>NZ_CP054139.1|WP_173417346.1|5650706_5653157_-|bifunctional-aspartate-kinase/homoserine-dehydrogenase-I
MKVLKFGGTSVGSAKSISTVIDILKTEDRSQGSPVVVLSAMSGVTNLLVEMAENAASGKEFTAHLAELEARHFAVVKELLDVQQQNPVFTRLKLYFNQLEDLLQGVLTLRELTAKTRDLILSYGERCSTLLVSRIAMQYFDGCLFVDATEVVKTDSAHGQAKVNMELTGMLIKDLYLANHDKILFVTGFISSNDAGQVTTLGRGGSDYTAAIFGSVLNASSIEIWTDVNGMMTADPRMVKKAFSLPELTYTEAMELSYFGAKVIYPPTMIPAFLKKIPIVIKNTFDTTFEGTVIRHDCKASNLAIKGISSVNRISIINLEGSGMVGKAGFSGRLFSLLAREQINVILITQSSSEHSITFAVQPDDAEKAKALIEQEFELELAARKLEHPVIEEELSILAIVGENMKQTPGMSGKLFHALGRNGVNVRAIAQGSSEYNISVIISGSDLAKALNAVHDAFFSQLNKTLHAFCLGTGNIGKTLFNQLNQHKGFLEENNGIQVKIAGISNTRKMSFDTDGFDLDTWESTLQAKGEQADLAGFVARMKSMNLPNCVFVDNTASPLPIAFYEEIFKSNISVVTCNKIGNSGKYSQYKAFHDAARLHGVDFFYETNVGAGLPIIRTLKDLMGSGDRLQRIEAILSGTISFIFNNFKGDANFHDVVKLAQEKGYTEPDPRDDLRGTDFMRKMLILARDAGYKMEAEDVQIDNILPQASLDAATVEDFYATLKSENAFFDNLKNEAESGNKVLRYIGKLENGKASISLQMVDAEHPFYTMSGSDNIIAFNTDRYKERPMVVKGPGAGAEVTAAGVFADLINVGAN
>NZ_CP054139.1|WP_173417347.1|5653654_5654575_+|ribosome-small-subunit-dependent-GTPase-A
MQGLIIKSTGSWYQVQTPDGKRYEARIKGKFRIKGLTTTNPIAVGDQVDFEFEPGSDNAVINNLHPRKNYIIRKSINLSKQAQIIAANLDQAFLVVTLASPRTSLGFIDRFLVTAEAYDIPAVLIYNKLDLFSDEGLEILAEHKSIYENIGYPCYEVSALVGTNINQVKELIKDKTTLFSGHSGVGKSSLINALLPDLSLRTGEVSDWSDKGMHTTTFAEMHQLPEGGFIVDTPGIRELGVIDIEQGELSHFFPEMRERLNQCRFNNCRHVNEPGCAIIAAVEEGEMELSRYESYLSIYHGHDTRA
>NZ_CP054139.1|WP_173417348.1|5654678_5655137_+|D-tyrosyl-tRNA(Tyr)-deacylase
MRAVLQRVSSASCTVDGNITGQIGMGFLVLLGIEDADTPDDLQWLAQKITNMRVFGDEQGLMNKALADVGGDILLISQFTLFAQTKKGNRPSFIRAARPDKAIPMYKQMIKALGELIGKPIATGIFGADMKISLVNDGPVTIVMDTRDKENH
>NZ_CP054139.1|WP_173417349.1|5655192_5655558_-|GxxExxY-protein
MLFKDESYKIIGACFEVHKVLGHGFKEVVYKDALELELTRLDIPFQREKPFTITYKEQILKHLFIADFIVYNNIILEIKNAGYIGEPYIKQTLNYLKASGVRLGLVVNFGTPSMEFQRVVF
>NZ_CP054139.1|WP_173417350.1|5655783_5656116_+|nucleotide-pyrophosphohydrolase
MTIQQAQQLVDNWIKTTGIRYFNELTNTAILMEEVGEVARIMARQYGEQSFKKSDTEVNLADEMADVLFVLICLANQTGIDLTQALEKNLEKKSIRDADRHRDNEKLKPK
>NZ_CP054139.1|WP_173417351.1|5656117_5656828_+|DUF4349-domain-containing-protein
MKKLFLIPCLCLTLLSCGHHAERPSAVRIVDVSLARPPSDEARKPVSPSDTARKLVKDGDIKFETADIQQTRKQIITSLQKVGGYVYEENEHNNSDENRKEYILRTRIPAKSFETFLDNASATAIQVDSKNISIRDVTTQYIDMATRLRNKLLLETRYRDLLTKATRMSDILQVEGKLDTIRSDIESEQGQLNYLNRQVAYSTLLITFYTKNKVQANNSDTVAYQLKKSLGQGWIC
>NZ_CP054139.1|WP_173417910.1|5657016_5657646_-|methyltransferase-domain-containing-protein
MYVHYGCGQCAPPEWRNFDVSPTLRIQKTPVLGWVMKNALGQVFDKNVKYGDVTEGLPGIADNSADGVYCSHVLEHMSLADFRKAVANSYKMLKPGGRFRLIMPDLKVLVDDYIADKAKGDAEASIRFIKRTLMAMEERPRNLKAVSKLAYGYLNHLWLWDKEATISELQKAGFKTIREIEFNDSEDPMFKLVENRKRFDLCVKLEAVK

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Self-targeting detection

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_ID	Protospacer_location	Mismatch	Identity

MGE targeting detection<

CRISPR_ID	Spacer_Info	Spacer_region	Spacer_length	Hit_phage_ID	Hit_phage_def	Protospacer_location	Mismatch	Identity

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

3040977 : 3048445

Caulobacter_phage(66.67%)

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_173415288.1\|3040977_3041553_+	TerD family protein	K4JRX3	Caulobacter_phage	1.3e-26	36.1
WP_173415289.1\|3041571_3042243_+	TerD family protein	K4JRX3	Caulobacter_phage	2.3e-19	28.3
WP_173415290.1\|3042248_3042965_+	HAD-IA family hydrolase	NA	NA	NA	NA
WP_173415291.1\|3042936_3043782_+	hypothetical protein	A0A291LAE0	Escherichia_phage	3.1e-29	28.5
WP_173415292.1\|3043771_3044326_+	TerD family protein	K4JRX3	Caulobacter_phage	1.4e-33	41.7
WP_173415293.1\|3044329_3044944_+	TerD family protein	K4JRX3	Caulobacter_phage	1.5e-17	33.2
WP_173415294.1\|3045172_3046378_+	toxic anion resistance protein	NA	NA	NA	NA
WP_173415295.1\|3046387_3047350_+	hypothetical protein	NA	NA	NA	NA
WP_173415296.1\|3047626_3048445_+	DUF475 domain-containing protein	A0A068EP98	Bacillus_phage	1.1e-31	43.2

DBSCAN-SWA_2

4152136 : 4160201

Enterobacteria_phage(33.33%)

tRNA

Protein_ID	Protein_Def	Hit_ID	Hit_Def	E-value	Identity
WP_173416118.1\|4152136_4153549_+	HD domain-containing protein	A0A125SJA9	Acidianus_tailed_spindle_virus	3.4e-28	32.3
WP_173416119.1\|4153593_4154250_+	hypothetical protein	NA	NA	NA	NA
WP_173416120.1\|4154298_4155210_+\|tRNA	tRNA (adenosine(37)-N6)-dimethylallyltransferase MiaA	NA	NA	NA	NA
WP_173416121.1\|4155293_4156220_-	NAD-dependent epimerase/dehydratase family protein	M1HWW2	Paramecium_bursaria_Chlorella_virus	2.2e-108	60.7
WP_173416122.1\|4156228_4157368_-	GDP-mannose 4,6-dehydratase	M4QRT5	Synechococcus_phage	1.9e-122	62.1
WP_173416123.1\|4157403_4158261_-	glucose-1-phosphate thymidylyltransferase RfbA	H9NC64	Sphingomonas_phage	2.7e-97	62.1
WP_173416124.1\|4158257_4159115_-	dTDP-4-dehydrorhamnose reductase	I7HXC9	Enterobacteria_phage	3.5e-44	40.7
WP_173417835.1\|4159148_4160201_-	dTDP-glucose 4,6-dehydratase	I7HTA3	Enterobacteria_phage	3.7e-88	49.1

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_CP054139

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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