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_CP043450	Mucilaginibacter rubeus strain P1 chromosome, complete genome	12 crisprs	DEDDh,csa3,WYL,cas3,PD-DExK	0	4	1	0

Results visualization

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CRISPR-Cas detection and classification

Crispr_ID: NZ_CP043450_1

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043450_1

266432-266526

Orphan

Consensus_repeat	Method
ATAAAGTACTTTGTATTTCAAAGT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043450_1

>merge|NZ_CP043450|1|266432-266526|CRISPRCasFinder
ATAAAGTACTTTGTATTTCAAAGTTAATATTTAAAAGAAAAGGCTTTAAGTAAGCCTGTGACAAATATAGCATAAAGTACTTTGTATTTCAAAGT

>NZ_CP043450|1|1|266432-266526|CRISPRCasFinder
ATAAAGTACTTTGTATTTCAAAGT	TAATATTTAAAAGAAAAGGCTTTAAGTAAGCCTGTGACAAATATAGC
ATAAAGTACTTTGTATTTCAAAGT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043450.1\|WP_112572369.1\|277058_280082_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|274948
NZ_CP043450.1\|WP_112572382.1\|263125_264538_-\|23S-rRNA-(uracil(1939)-C(5))-methyltransferase-RlmD	unknown	unknown	gnl\|CDD\|225174
NZ_CP043450.1\|WP_112572371.1\|273914_276809_+\|transcriptional-regulator	unknown	unknown	gnl\|CDD\|369392
NZ_CP043450.1\|WP_112572387.1\|261380_261881_+\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|140006
NZ_CP043450.1\|WP_112572564.1\|259143_260310_+\|DoxX-family-protein	unknown	unknown	gnl\|CDD\|225168
NZ_CP043450.1\|WP_112572391.1\|255890_257411_+\|GH3-auxin-responsive-promoter-family-protein	unknown	unknown	gnl\|CDD\|377019
NZ_CP043450.1\|WP_112572378.1\|267337_267751_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|225057
NZ_CP043450.1\|WP_112572367.1\|280093_281575_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|185760
NZ_CP043450.1\|WP_091220479.1\|266756_267338_-\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224228
NZ_CP043450.1\|WP_112572565.1\|258647_259139_+\|DUF1599-domain-containing-protein	unknown	unknown	gnl\|CDD\|377892
NZ_CP043450.1\|WP_112572560.1\|281692_283045_+\|DUF3131-domain-containing-protein	unknown	unknown	gnl\|CDD\|370812
NZ_CP043450.1\|WP_112572389.1\|260311_261370_+\|ABC-transporter-permease	unknown	unknown	gnl\|CDD\|223674
NZ_CP043450.1\|WP_112572567.1\|257600_258473_-\|dihydropteroate-synthase	unknown	unknown	gnl\|CDD\|273657
NZ_CP043450.1\|WP_112572562.1\|272855_273812_+\|rhodanese-related-sulfurtransferase	unknown	unknown	gnl\|CDD\|234663
NZ_CP043450.1\|WP_112572374.1\|268884_270075_-\|glycine-C-acetyltransferase	unknown	unknown	gnl\|CDD\|235893
NZ_CP043450.1\|WP_112572386.1\|261999_262512_-\|phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|235365
NZ_CP043450.1\|WP_112572384.1\|262597_262993_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112572380.1\|265084_266419_-\|cell-envelope-integrity-protein-CreD	unknown	unknown	gnl\|CDD\|377608
NZ_CP043450.1\|WP_112572376.1\|267747_268785_-\|phenylalanine--tRNA-ligase-subunit-alpha	unknown	unknown	gnl\|CDD\|234780
NZ_CP043450.1\|WP_112572373.1\|270205_272686_+\|carboxypeptidase-like-regulatory-domain-containing-protein	unknown	unknown	gnl\|CDD\|372685

Protein	Function_ID	Function_description	E-value
NZ_CP043450.1\|WP_112572369.1\|277058_280082_+\|TonB-dependent-receptor	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_CP043450.1\|WP_112572389.1\|260311_261370_+\|ABC-transporter-permease	gnl\|CDD\|223674	COG0601, DppB, ABC-type dipeptide/oligopeptide/nickel transport systems, permease components [Amino acid transport and metabolism / Inorganic ion transport and metabolism].	5.15534e-102
NZ_CP043450.1\|WP_112572371.1\|273914_276809_+\|transcriptional-regulator	gnl\|CDD\|369392	pfam07495, Y_Y_Y, Y_Y_Y domain. This domain is mostly found at the end of the beta propellers (pfam07494) in a family of two component regulators. However they are also found tandemly repeated in CTC_02402 without other signal conduction domains being present. It's named after the conserved tyrosines found in the alignment. The exact function is not known.	4.73692e-06
NZ_CP043450.1\|WP_112572387.1\|261380_261881_+\|AAA-family-ATPase	gnl\|CDD\|140006	PRK13949, PRK13949, shikimate kinase; Provisional.	1.57127e-54
NZ_CP043450.1\|WP_112572564.1\|259143_260310_+\|DoxX-family-protein	gnl\|CDD\|225168	COG2259, COG2259, Predicted membrane protein [Function unknown].	9.21113e-05
NZ_CP043450.1\|WP_112572391.1\|255890_257411_+\|GH3-auxin-responsive-promoter-family-protein	gnl\|CDD\|377019	pfam03321, GH3, GH3 auxin-responsive promoter.	9.00079e-162
NZ_CP043450.1\|WP_112572565.1\|258647_259139_+\|DUF1599-domain-containing-protein	gnl\|CDD\|377892	pfam07659, DUF1599, Domain of Unknown Function (DUF1599).	1.15425e-32
NZ_CP043450.1\|WP_112572367.1\|280093_281575_+\|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.	1.22205e-47
NZ_CP043450.1\|WP_091220479.1\|266756_267338_-\|TetR/AcrR-family-transcriptional-regulator	gnl\|CDD\|224228	COG1309, AcrR, Transcriptional regulator [Transcription].	5.45551e-14
NZ_CP043450.1\|WP_112572378.1\|267337_267751_-\|hypothetical-protein	gnl\|CDD\|225057	COG2146, {NirD}, Ferredoxin subunits of nitrite reductase and ring-hydroxylating dioxygenases [Inorganic ion transport and metabolism / General function prediction only].	5.87784e-07
NZ_CP043450.1\|WP_112572560.1\|281692_283045_+\|DUF3131-domain-containing-protein	gnl\|CDD\|370812	pfam10091, Glycoamylase, Putative glucoamylase. The structure of UniProt:Q5LIB7 has an alpha/alpha toroid fold and is similar structurally to a number of glucoamylases. Most of these structural homologs are glucoamylases, involved in breaking down complex sugars (e.g. starch). The biologically relevant state is likely to be monomeric. The putative active site is located at the centre of the toroid with a well defined large cavity.	6.93327e-99
NZ_CP043450.1\|WP_112572382.1\|263125_264538_-\|23S-rRNA-(uracil(1939)-C(5))-methyltransferase-RlmD	gnl\|CDD\|225174	COG2265, TrmA, SAM-dependent methyltransferases related to tRNA (uracil-5-)-methyltransferase [Translation, ribosomal structure and biogenesis].	2.92258e-121
NZ_CP043450.1\|WP_112572567.1\|257600_258473_-\|dihydropteroate-synthase	gnl\|CDD\|273657	TIGR01496, Dihydropteroate_synthase, dihydropteroate synthase. This model represents dihydropteroate synthase, the enzyme that catalyzes the second to last step in folic acid biosynthesis. The gene is usually designated folP (folic acid biosynthsis) or sul (sulfanilamide resistance). This model represents one branch of the family of pterin-binding enzymes (pfam00809) and of a cluster of dihydropteroate synthase and related enzymes (COG0294). Other members of pfam00809 and COG0294 are represented by model TIGR00284. [Biosynthesis of cofactors, prosthetic groups, and carriers, Folic acid].	2.57817e-107
NZ_CP043450.1\|WP_112572562.1\|272855_273812_+\|rhodanese-related-sulfurtransferase	gnl\|CDD\|234663	PRK00142, PRK00142, rhodanese-related sulfurtransferase.	4.23628e-156
NZ_CP043450.1\|WP_112572374.1\|268884_270075_-\|glycine-C-acetyltransferase	gnl\|CDD\|235893	PRK06939, PRK06939, 2-amino-3-ketobutyrate coenzyme A ligase; Provisional.	0
NZ_CP043450.1\|WP_112572386.1\|261999_262512_-\|phosphoribosyltransferase	gnl\|CDD\|235365	PRK05205, PRK05205, bifunctional pyr operon transcriptional regulator/uracil phosphoribosyltransferase PyrR.	1.16539e-24
NZ_CP043450.1\|WP_112572380.1\|265084_266419_-\|cell-envelope-integrity-protein-CreD	gnl\|CDD\|377608	pfam06123, CreD, Inner membrane protein CreD. This family consists of several bacterial CreD or Cet inner membrane proteins. Dominant mutations of the cet gene of Escherichia coli result in tolerance to colicin E2 and increased amounts of an inner membrane protein with an Mr of 42,000. The cet gene is shown to be in the same operon as the phoM gene, which is required in a phoR background for expression of the structural gene for alkaline phosphatase, phoA. Although the Cet protein is not required for phoA expression, it has been suggested that the Cet protein has an enhancing effect on the transcription of phoA.	3.39676e-179
NZ_CP043450.1\|WP_112572376.1\|267747_268785_-\|phenylalanine--tRNA-ligase-subunit-alpha	gnl\|CDD\|234780	PRK00488, pheS, phenylalanyl-tRNA synthetase subunit alpha; Validated.	0
NZ_CP043450.1\|WP_112572373.1\|270205_272686_+\|carboxypeptidase-like-regulatory-domain-containing-protein	gnl\|CDD\|372685	pfam13715, CarbopepD_reg_2, CarboxypepD_reg-like domain. This domain family is found in bacteria, archaea and eukaryotes, and is approximately 90 amino acids in length. The family is found in association with pfam07715 and pfam00593.	2.63004e-14

>NZ_CP043450.1|WP_112572380.1|265084_266419_-|cell-envelope-integrity-protein-CreD
MIGEQFPKQTTTDWLKESATFKLIFIGVLALLLLIPSAFIQNLVTERASRQDEMAKEVSDSWSASQIIKGPVLVIPYRKGINITDTTKQTPVENLYILPDNLHIKASLATQILHRGIFDVAVYNTQVKVSGNFARLNLSSLGINTNQLILNKARFEFSVSDLKGLKSNPVIKTNQPILSAEPSFESVFGNGLQAPVDLSAVNDNEIPFDYTLDLKGSEGLSFLQLGKTTDVQVNSNWSSPSFDGNHLPDERKIDTGGFSAGWRMMYYNRPFPQQWTGSQKILDNDKKLANATFGVKLRLPVDQYQKTMRTSKYAIFIILLTFISLFLTEIIRKQPIHMFNYILIGAAMVIYYTLLLSFSEQVGYNMAYLIASVSTIMLISVFISSLLKNSRAALLFAFILAVFYAFIFVIIQLEDLALMVGSIALFIIIAVLMYFSRKINWDKN
>NZ_CP043450.1|WP_112572382.1|263125_264538_-|23S-rRNA-(uracil(1939)-C(5))-methyltransferase-RlmD
MSKANKPKFFENVQIIDIAEEGKGVGKADDFVLFVDKAVPGDIADVQVYRSKKNFGEGKITELKQASEYRTTAFCEHFGTCGGCKWQHMTYEAQLKFKQKSVVDALSRLAKINVEGIMPIVPSPADRYYRNKLEFTFSNKRWLYDGENKEDGTLNMNALGFHIPGRFDKILDVNHCYLQAEPSNSLRNEIRDFTVQQGYTYYDLRNHSGMLRNLVVRTSSTGEIMVIVVFAYAEQSEIDKLMGHVDARFPEITSLLYIVNQKKNDTIFDQDVIAFKGPEYIHEEMNGIKFRIGPKSFYQTNSVQALRLYEITRDFAGFKGDELVYDLYTGAGTIANFVAGHVREVVGVEYVPTAIEDAKVNSAINNITNTKFYAGDMKDVLVADFVAEHGKPDVIITDPPRAGMHPDVVARLMEIEAPKIVYVSCNAATQARDLLVLKEKYDTVKIQPVDMFPHTQHVENVVLLVLRDWR
>NZ_CP043450.1|WP_112572384.1|262597_262993_-|hypothetical-protein
MNPEELLNESNERNKPAADSPLISLERDLKYFNESIKEVAEEIINEGLSSYPILIAHQHELSLGELILDRHDLNSEWSIHASTLEEFVERDVIKPVLKERFVNSYKDPYQYMCVFVVVPEGANFVFFPYVK
>NZ_CP043450.1|WP_112572386.1|261999_262512_-|phosphoribosyltransferase
MPEKKLLILNKQQIQQKLDRMAYQILEDNFEEDEILIAGILPRGNHIAERLKTILDGIAPFKSRILTIELEKQSSSLSASIDFEVEECSNKVVILVDDVLNSGKTLAYGFGVFLDVPLKKLRTAVLVDRNHKSFPITTDFAGVALSTVIKEHVDVVLQEEDAEEDAVYLR
>NZ_CP043450.1|WP_112572387.1|261380_261881_+|AAA-family-ATPase
MKYFIVGFMGCGKTTWSRKLAAKWGYEFIDLDHVLEAKAGMSIAEYFSSFGEDAFRKLESQVLKETDYPENIVVSTGGGLPCFFDNMDWMKANGKTLYIKLSPKTLADRLENSKTIRPVLQGKKGDELVEFITGKLAEREDFYLQATNIVEGIDMSVEKLEEALGV
>NZ_CP043450.1|WP_112572389.1|260311_261370_+|ABC-transporter-permease
MIPYLFRKLVYGLAVMLGVVVVVFFLFNILPVDPARMTQGQRADVQSLQAVRKEFGLDKPVPVQFAYYLNDLSPLGIHLNTVDEQQRYGYVKLFPVSKSKVLALKWPYLRRSYQTRKDVASLLMEVIPNTLVLAAAAMIFAIIIGVFLGVASAVHKDTWIDKLALSFSTLGISAPSFFAGIIIAWIFGFVLSNYTHLNMSGSLYSYDPFKGEVITLKNLVLPVITLGLRPLAIIVQLTRNAMLDVLGQDYIRTAKAKGLSNRTIIYRHALKNAMNPVITAIANWFASLLAGSFFVEYIFGYNGLGKATVDALEMSDFPVVMGSILFIAFIFVVISILVDVIYVWIDPRVKLS
>NZ_CP043450.1|WP_112572564.1|259143_260310_+|DoxX-family-protein
MKKTSSNSAVIWIPRLLVGLLFIFSGLIKANDPLGFSYKLVEYFEVFHMTFLNGLALTMAIVLCALEMLLGFALLIGARAVKVAWGLLLLIIFFGFLTFYSAFFKVVQTCGCFGDAIPLTPWQSFSKDMVLLALVLILFVKRKQITPLFNAKVGDKWLICAAIVSIGFGEYTYNFSPIIDFLPYKIGANLPDEMKIPPGAPLDEFELTYHLKNKKTGATKVMNDKEYLKSNIWKDANWEVIGDPENRLVKKGYEPKIRDLAIQDAQRNDYTKELLSSPFYSLFIVAYDLSETDKDAINRLNALAINLTDNYNIRTILLTSNSAADAKAFAKEHKLISEVFYADGVPLKSMVRSNPGVLLMKNGTVINKWHYHSVPKYEDIVKQYLQKQ
>NZ_CP043450.1|WP_112572565.1|258647_259139_+|DUF1599-domain-containing-protein
MKKTRDYGTAWRILRPQSITDQIFIKAQRIRTLEEKKISKVGDDITGEYIGIVNYCVIAMMQLECGPEMSTELNPDHVSEMFDAKVNETKELMFAKNHDYGEAWRDMRISSLTDLILMKLLRVKQIEDNKGLTEASEGVKANYQDMLNYAVFALIKLNVHLGK
>NZ_CP043450.1|WP_112572567.1|257600_258473_-|dihydropteroate-synthase
MVKDTFFRKKVTLNAGGKLIDLSSPKVMGIINITPDSFFADSRKPSIDEALLQAQKMLTDGATFLDIGAYSSRPGAVDISAQEETDRLLPVVEAIAAQFPEAIMSIDTFRAGVAESAINGGAHIINDISGGTLDIDMFTTVARLNVPYILMHMKGTPQTMNQMADYDDVFGEVFDYFVSKYSELKRLGVHDVILDPGFGFAKKAEHSYALMSRMNEFDLLGLPILTGISRKRMVYGLLGNTAEEALNGTTVLNTIALMKGTSILRVHDVKEAVEAVRIWEAVEGPPEAGQ
>NZ_CP043450.1|WP_112572391.1|255890_257411_+|GH3-auxin-responsive-promoter-family-protein
MTLFNSVFTWFMKKRIHQIELFMKYPNEVQEEWFEQLVSVAENTEWGKKYHYKSIENLSQFKERVPIQNYDTLKPFIERMLKGEKNVLWPSEIRWFAKSSGTTSDRSKFIPVSEEALEECHFKGGKDLLTIYFNNQPNPRMFTGKILTLGGSHQISQLSPDTSFGDLSAVIMKNLPMWAEFHRTPHLDIALLENFEEKIEKIAHATKDVNVTSISGVPTWNLVLFKRILEITGKKNLLEVWPNLEMYFHGAVNFTPYREQFKKLIPNEEMYYLENYNASEGFFGIQDTKEPGDMLLMLDYGIFYEFLPLEHLYDENPETLTLDEVELNKNYALIISTNAGLWRYMIGDTIKFSSLAPFRIQITGRTKHFINAFGEEVIIDNAERALEEACTQTGAIIREYTAAPVYFNGDDCGAHEWIIEFEKKPAEFERFVDLLDETLRRINSDYDAKRFKDLALRRPVVRRAPDGTFFNWMREKGKLGGQHKVPRLANDREYVDAILKMMELVG
>NZ_CP043450.1|WP_091220479.1|266756_267338_-|TetR/AcrR-family-transcriptional-regulator
MEADKIKDSIKRAAQELFRKFGYHKTSVNEIAKKAKIAKATIYKYFDSKEAVLHVLLMDYIKASVDDLVQVNSNDIDEEAYLNNLIMKTCRLSYTVCNEFIGWDFIRESTNSQDFLKNLSNELEELLMASFIQLPGIRKHETYQQRLRFLIKCSKSIVFSFAFTSVSDSDVRKNFVSFQKEILPYLVKAAVSV
>NZ_CP043450.1|WP_112572378.1|267337_267751_-|hypothetical-protein
MRKLTIILLVVISCFSCGKASDNVPSVPVNFQAALGTPALSPLNVSGGAVAINGYGVAGLIIYRKVNGTYAAYDRCSSYQPEKKCAVTIDNTGFTVTDPCSGSKFSLEDGTPVKAPATKALRSYRVAVTQFEIQVTN
>NZ_CP043450.1|WP_112572376.1|267747_268785_-|phenylalanine--tRNA-ligase-subunit-alpha
MMQAQIDQYTAEINAFSPANADELEAFRIKFLGTKGIIKDLFEQFKSVSPEEKRTFGKVLNEFKQLAEAKYNELKENIGSGAQSKGNDLDLTLPGDGFTVGSRHPLSLVRNEIIDIFKRLGFVVAEGPEIEDDWHNFSALNFPDEHPARDMQDTFFIKKNNGKDDIALRTHTSSVQVRMMEAGKPPFRAIMPGRVYRNEAISARAHCFFHQVEGLYVDENVSFSDLKQTLYHFVQELYGEGTRVRFRPSYFPFTEPSAEMDISCTICGGAGCNMCKHSGWVEILGCGMVDPNVLENCGIDSKKYTGFAFGMGMERIANLKYVIRDLRLFSENDVRFLKQFQTEML
>NZ_CP043450.1|WP_112572374.1|268884_270075_-|glycine-C-acetyltransferase
MYNTLQPVLQQELTDIENAGLYKKERIITSPQGADITVQGGAEVINFCANNYLGLSGNAKVIQAAKDAMDTHGYGLSSVRFICGTQDIHKELEKKIAEFLGTEDTILYAAAFDANGGVFEPLFNDQDAIISDELNHASIIDGVRLCKAQRYRYKHDDMADLEEKLKATQELRHRIIVTDGAFSMDGTIAQLDKICDLADKYNALVMIDESHCSGFMGKSGRGTHEHHNVMGRIDIITGTLGKALGGASGGFTSGRKEIIDMLRQRSRPYLFSNTLAPAITGASIAVLDMLSETTELRDKLETNTQYFRKKMTEAGFDIKPGVHPIVPVMLYDAKLAQEFAAKMLDEGIYVIGFYYPVVPQGKARIRVQISAAHDMHHLDKAIEAFTKVGKELGVLK
>NZ_CP043450.1|WP_112572373.1|270205_272686_+|carboxypeptidase-like-regulatory-domain-containing-protein
MRKYILLLIIAFSVITASAQQSLLTGKITDKNGQVIPFVSIYIRNSTYGTTANENGVYQFKLNPGTYNVIYRYVGYTEKIEQVTIADHDQEHNVQMADEQFSTERVSETYRKNRDAADTIIKQVIKKRKYYMEEATSFSCAVYVKGVQKLLSVPKSLIGQEVQRTLDLDSNGRGILYQSESLSEYNFQKPDKIREITIANRMAGQNTAFGYKKASDLQANFYENVFIIPGLASRGFVSPVAAYGPRFYNYKLLGTSVENGHTIDKIRITPKHSHGQYFQGDIYIVEGDWRIYSVDFFIDNKVSNLNLVDTLNIRQQYIAITDSVWMPASTQYNFKGAVLGFKFGGYYAAVYNNYKINPTFPDGFFTGEILKIDTVANSKKPEYWENARPIPLTAYETRDYKKKDAFEEYKKTDRYLDSLQHHKNHINYPGYLIFGYAASNKSARDSLYIYPFIQTFYYNTVEGFGINAKVSYIRTYDDFHSLTITPAVRYGFSNKIFSANVAAEYLNDPFHAAKFYADFGSDVLDLNNVGTRSLYFNTLSTLLSENNYVKYYRSHYGDFGYQREVVNGVLLKGGLSYSSRSQLYNTSFSKIKDIKDREFTSNNPLAPPGTPADDHSFLFPDNQALVFNASALFTFDQRYETRPTGKFNLPSRYPMVKVNYRKGFKNIFGSDVDYDFASVDVSQDHIQVGLSGYSSFKISGGGFFNNKKLYYMDYNHFLGNQGTTFDPTYVGSFHFLPFYTYSTNGAFLEAHYQHNFAGSLFNHIPFLRKAKLEEIIGANYLTTKNNRNYREFYIGVQRLIFRVDYGISYAGNQKYIQGFRIFYGIR
>NZ_CP043450.1|WP_112572562.1|272855_273812_+|rhodanese-related-sulfurtransferase
MEMYNTLLYYCYSTIDNAEQFAADHLKFCKSLGLTGRIIVADEGLNGTVSGSVEACKTYMDTVHADERFAKTEFKIDEVDTPSFVKMHVRYKSEIVHSGLRDPNVIDPKQKTGIHLEPKEFLAMKDRDDVVVLDVRSNYEHSLGKFKNAVTLDIDNFRDFPDMINQLAQYKDKKILTYCTGGIKCEKASALLLHEGFPEVYQLHGGIIKYGKEAGGEDFEGKCYVFDNRLSVDVNNVNPVVISTCFNCGKTTPKMINCANPECNEHFTQCDECGTAMDGCCSDACKEHPRKRVYDGTGYYVKVPQPVNVNKSKLQPIA
>NZ_CP043450.1|WP_112572371.1|273914_276809_+|transcriptional-regulator
MRKTLCIIIVLVFISVWPAWSVDIKSVGVPYIQNYTKATYQFGNQNWSVTRDEHDIMYFGNAEGLLTFDGKYWQQYHMPNGLIVRSVSADGKGRVYAGGYGEFGYWHNDGKGILKYTSLINLVPKKFLPVTEEIWKIYCDNNRVLFQSFGAIYIYSAGKIEVVKTHEPYLFLFKSGNRFFVEQLTKGLFELKGSKTEYIEGSNILGASGVLSILPFQQGKYLIGTAKNGLFIYDGKTVKPWANQANDFLTTYQLNNGAAIAGKYFAYGTILNGIVIIDTMGRVVQHINKASGMQNNTVLSLYTDASQNLWAGLDNGIDRIEVNSPLYFYFDKTGKFGTVYSSIIFDKKIYLGTNQGLFYSDWLPDSHNSPFQTFDFKLIPGSQGQVWDLSLQDNRLLCGHNDGTYQVNGASIKKISDITGGWNIKKMAPDMLMQGTYTGLVIYRKDAAGNWQYSHKLAGFSEPSRYVERDAKGQIWVSHAYKGIYKLTLSADQRTVVSHVYYDQKHGLPGSYNINVFDLDNRTVFSSDSGFYVYDDITDRFYKYQQLNSKLGTFATSSKIIKAIGKKYWFINQGRVGLADMSVTGKLTIDTNRFSILNGQMVQHYETINRINNSTYLISVDDGFVILNDADAQLPNMVKIPNVLIRRIENVTDKVSLISEAAEDSNNIEIPYAENNIRISYSLPYYTQAKIRFQYYLEGYSHQWSEWAPQSQKEFTNLNQGTYNFKVRAKINDQYQSAVSTITFTVLPPWYAGKIAMVFYVLLAVLLFYVIRYYYGLKLKKHQQQIQQKLQKEKEEFLKQEAIANEQHIVNIKNEQLQADLASKSRELANSAMNIVYKNELLQKISDELTHLKGGDGKKLADEQLRRIQKVIDEGMSDDRDWNIFETSFNEAHENFFKKLKAGHPDLVPNDLKLCAYLRMNMNSKEIASLLNISLRGVEIRRYRLRKKLNLEHDKNLTEFLIEL
>NZ_CP043450.1|WP_112572369.1|277058_280082_+|TonB-dependent-receptor
MKRIFTISGLMLLLLLCYDAAFAQNVTIKGKITDGKTGEALIGVSVSVKGTTIGTQTDVNGAFTLKTPGNATLSVAYIGYATQEVAVNGQTTINVALQPQTNELQQVVVIGYGTQRKLDVTGSIATVKGADVAKQASPNALSGLQGKVSGVQITNSGTPGKSPDITIRGLGTIYGNTKPLFVVDGVWYDDISFLNPQDIESFSILKDASSTAIYGIRAANGVVLIGTKRGTKGKPVINYNGYVGLQAVTNQVKMANASEYATAVNELSALNGGSPIFTNPASYGTGTDWYKQILRKAFTTNHEASISGGTDKYTYNYSFGYLNQDGIAKTNNYQRYTVHLSNDFKPTKNVKFGYTASALSDVSRDVNSAIFHQLFGAAPTLPVRKADGSYGDPNDYNTGDGNNYNPQATIDFFNQRTKNKRFTYNAYGEVTFLKNFKFKSSFGGDISQNEVRAFTPEYMATLRQQSNKTNLDINHTDVRNWIWENTLTYDVKIKDHKITALVGYSAQNNRTRQIDGKADYVPYVKNGSIRSSFPDTTNVNFFATPGSQIHTRALSQFARVNYSFRDKYLLNASIRRDGASQFYGDHTYGYFPSVGAGWVITNEEFMKDQKVFSNLKLRGSWGKVGNSGVPINPTVQVIATDPYLTGLFGNPLTTYPGASINSIVPPSIVWERTVSSDFGIEGGLIDNKLTFEADYYNRETQDAIFAIPVAGSLGTNNSSLIGNQASIRNRGWEFSLGWRDNPSKDFNYSVSANLGINNNKVLNVVTGQNPIYDGGEGIANGALATRTVVGQPIGQFYGYKVTGIFQTTQEVANSKQKGAAPGDFIYQDTNNDGILDSRDRVALGSPLPKYNYGINTSFTYKNFDLALDFQGVAGVSVYNANIAYRFGNENFTQDFYQNRWHGAGTSNTYPSVNVGKTANAAPNSFYVESGAYFRMRNAQLGYTIPGDFLKKLNISKVRIYANAQNAINLFGYKGFSPEIGGDVGSRGIDASVYPLFATYNFGVNVTF
>NZ_CP043450.1|WP_112572367.1|280093_281575_+|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKNSTKYSRKVVALGLIASIISFQSCKKSFLNVDPAQNTAATQFFKTQDDATKAVSAMYANLREWNNIAFAPIAVESMGSDDVEKGSTASDATFFNDYHNFTITSGDAQLGGFWRGQYQTINFANQILTNVPGITMDETLKARYLAEAKFIRAYAYFRLVRAFGDVPLRLTLPKSASEYNLPRTAKAQVWAAIETDLNDAANVLPQTYSAADIGHATKGAAIALHAKVAMYLKKWTDVLNYTNQVMGMGYSLFPDYEQMFRTNHKNNQESVFEVQCALIPNNPDASNSQYSQVQGVRGVTGGGWGFNVPSAGLAAAYETGDPRRDATIIFRGETTPEGDKIPATGDNPMYNQKSYVPFSMYVSGFNEGCQQNKIVLRYADVLLMNAEANNELGNSAAALIPLEQVRARARGSNAAILPKVTTTDQATLRTAIYQERRVELAMEFERYFDVIRQGRGTAVFGSRGWTAGKNEVWPVPQTEIDLSGGALTQNPGY
>NZ_CP043450.1|WP_112572560.1|281692_283045_+|DUF3131-domain-containing-protein
MKKLLITPVLMLAAICCFAQKAAKKSEDGIKPVGIIKNLTDSALLDVVQRQTYRYFWDFGHPVSGLARERSNTSFDYGSEVVTTGGSGFGIMSLIVADSRKWITHDQAVDRMVKIVNFLYKADAFHGAFPHWLNGETGKVIRFGRKDDGADIVESAYLFQGLLCARQYFTADDPKERRIRDVINWMWGEMEWNWFTRDGRDYLYWHWSPNNGWAMNFPIHGFNECLITYVLAASAERYPVGANVYHNGWAQSDFFKNGRTFYGFKLPLGFDYGGPLFFSQYSFLGLNPKGLKDQYADYWEQNKNHTLINHAYCVDNPKKFKGYGENCWGLTASDNFEGYNAHSPTNDLGVITPTAALSAFPYTPEYSMKALRHFYYDLGDKIWGEYGFTDAFSESHNWYAKSYLAIDQGPIVVMIENYRTGLLWKLFMSCPEVQGGLKKLGFESPAIAKN

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Crispr_ID: NZ_CP043450_2

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043450_2

456830-456902

Orphan

Consensus_repeat	Method
TTTTTTGATTGCGTTGATTTCGC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043450_2

>merge|NZ_CP043450|2|456830-456902|CRISPRCasFinder
TTTTTTGATTGCGTTGATTTCGCTGATAATGGCATATTTTGACTGTTGACTTTTTTGATTACGTTGATTTCGC

>NZ_CP043450|2|2|456830-456902|CRISPRCasFinder
TTTTTTGATTGCGTTGATTTCGC	TGATAATGGCATATTTTGACTGTTGAC
TTTTTTGATTACGTTGATTTCGC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043450.1\|WP_146749995.1\|458577_459522_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112569226.1\|451802_452633_+\|5-dehydro-4-deoxy-D-glucuronate-isomerase	unknown	unknown	gnl\|CDD\|179169
NZ_CP043450.1\|WP_112575990.1\|447533_449063_-\|glutamine-hydrolyzing-GMP-synthase	unknown	unknown	gnl\|CDD\|234614
NZ_CP043450.1\|WP_112569242.1\|461239_462379_+\|cystathionine-gamma-synthase	unknown	unknown	gnl\|CDD\|366438
NZ_CP043450.1\|WP_112569236.1\|457062_458544_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112569248.1\|464932_466300_+\|tRNA-uridine-5-carboxymethylaminomethyl(34)-synthesis-GTPase-MnmE	unknown	unknown	gnl\|CDD\|235392
NZ_CP043450.1\|WP_112569224.1\|450921_451536_-\|DUF386-domain-containing-protein	unknown	unknown	gnl\|CDD\|377217
NZ_CP043450.1\|WP_112569252.1\|470856_473955_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|274948
NZ_CP043450.1\|WP_146750157.1\|446317_447577_-\|amino-acid-ABC-transporter-substrate-binding-protein	unknown	unknown	gnl\|CDD\|380492
NZ_CP043450.1\|WP_112569240.1\|459622_461095_+\|proline--tRNA-ligase	unknown	unknown	gnl\|CDD\|236327
NZ_CP043450.1\|WP_112575988.1\|445148_446321_-\|RsmB/NOP-family-class-I-SAM-dependent-RNA-methyltransferase	unknown	unknown	gnl\|CDD\|223222
NZ_CP043450.1\|WP_112575991.1\|449138_449936_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|187576
NZ_CP043450.1\|WP_112569232.1\|454998_456783_-\|DUF885-domain-containing-protein	unknown	unknown	gnl\|CDD\|377577
NZ_CP043450.1\|WP_112575992.1\|450047_450566_+\|lipocalin-family-protein	unknown	unknown	gnl\|CDD\|381213
NZ_CP043450.1\|WP_112569244.1\|463271_463565_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112569250.1\|466607_470039_-\|SUMF1/EgtB/PvdO-family-nonheme-iron-enzyme	unknown	unknown	gnl\|CDD\|224182
NZ_CP043450.1\|WP_112569246.1\|463646_464705_-\|nucleoid-associated-protein	unknown	unknown	gnl\|CDD\|377262
NZ_CP043450.1\|WP_112569230.1\|453946_454726_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112570009.1\|462467_463259_+\|TIGR02757-family-protein	unknown	unknown	gnl\|CDD\|378237
NZ_CP043450.1\|WP_112569228.1\|452664_453480_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|236216

Protein	Function_ID	Function_description	E-value
NZ_CP043450.1\|WP_112569252.1\|470856_473955_+\|TonB-dependent-receptor	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_CP043450.1\|WP_112569226.1\|451802_452633_+\|5-dehydro-4-deoxy-D-glucuronate-isomerase	gnl\|CDD\|179169	PRK00924, PRK00924, 5-keto-4-deoxyuronate isomerase; Provisional.	0
NZ_CP043450.1\|WP_112575990.1\|447533_449063_-\|glutamine-hydrolyzing-GMP-synthase	gnl\|CDD\|234614	PRK00074, guaA, GMP synthase; Reviewed.	0
NZ_CP043450.1\|WP_112569248.1\|464932_466300_+\|tRNA-uridine-5-carboxymethylaminomethyl(34)-synthesis-GTPase-MnmE	gnl\|CDD\|235392	PRK05291, trmE, tRNA uridine-5-carboxymethylaminomethyl(34) synthesis GTPase MnmE.	0
NZ_CP043450.1\|WP_112569224.1\|450921_451536_-\|DUF386-domain-containing-protein	gnl\|CDD\|377217	pfam04074, DUF386, Domain of unknown function (DUF386). This family consists of conserved hypothetical proteins, typically about 150 amino acids in length, with no known function.	8.93211e-46
NZ_CP043450.1\|WP_146750157.1\|446317_447577_-\|amino-acid-ABC-transporter-substrate-binding-protein	gnl\|CDD\|380492	cd06268, PBP1_ABC_transporter_LIVBP-like, periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily. Periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily. They are mostly present in archaea and eubacteria, and are primarily involved in scavenging solutes from the environment. ABC-type transporters couple ATP hydrolysis with the uptake and efflux of a wide range of substrates across bacterial membranes, including amino acids, peptides, lipids and sterols, and various drugs. These systems are comprised of transmembrane domains, nucleotide binding domains, and in most bacterial uptake systems, periplasmic binding proteins (PBPs) which transfer the ligand to the extracellular gate of the transmembrane domains. These PBPs bind their substrates selectively and with high affinity. Members of this group include ABC-type Leucine-Isoleucine-Valine-Binding Proteins (LIVBP), which are homologous to the aliphatic amidase transcriptional repressor, AmiC, of Pseudomonas aeruginosa. The uncharacterized periplasmic components of various ABC-type transport systems are included in this group.	6.84864e-06
NZ_CP043450.1\|WP_112569240.1\|459622_461095_+\|proline--tRNA-ligase	gnl\|CDD\|236327	PRK08661, PRK08661, prolyl-tRNA synthetase; Provisional.	0
NZ_CP043450.1\|WP_112575988.1\|445148_446321_-\|RsmB/NOP-family-class-I-SAM-dependent-RNA-methyltransferase	gnl\|CDD\|223222	COG0144, Sun, tRNA and rRNA cytosine-C5-methylases [Translation, ribosomal structure and biogenesis].	3.66225e-31
NZ_CP043450.1\|WP_112575991.1\|449138_449936_-\|SDR-family-oxidoreductase	gnl\|CDD\|187576	cd05266, SDR_a4, atypical (a) SDRs, subgroup 4. Atypical SDRs in this subgroup are poorly defined, one member is identified as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is related to, but is different from, the archetypical SDRs, GXGXXG. This subgroup also lacks most of the characteristic active site residues of the SDRs; however, the upstream Ser is present at the usual place, and some potential catalytic residues are present in place of the usual YXXXK active site motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, 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.	4.0164e-61
NZ_CP043450.1\|WP_112569232.1\|454998_456783_-\|DUF885-domain-containing-protein	gnl\|CDD\|377577	pfam05960, DUF885, Bacterial protein of unknown function (DUF885). This family consists of several hypothetical bacterial proteins several of which are putative membrane proteins.	6.23473e-80
NZ_CP043450.1\|WP_112575992.1\|450047_450566_+\|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.	5.07839e-60
NZ_CP043450.1\|WP_112569250.1\|466607_470039_-\|SUMF1/EgtB/PvdO-family-nonheme-iron-enzyme	gnl\|CDD\|224182	COG1262, COG1262, Uncharacterized conserved protein [Function unknown].	6.08395e-47
NZ_CP043450.1\|WP_112569246.1\|463646_464705_-\|nucleoid-associated-protein	gnl\|CDD\|377262	pfam04245, NA37, 37-kD nucleoid-associated bacterial protein.	3.01923e-30
NZ_CP043450.1\|WP_112570009.1\|462467_463259_+\|TIGR02757-family-protein	gnl\|CDD\|378237	pfam09674, DUF2400, Protein of unknown function (DUF2400). Members of this uncharacterized protein family are found sporadically, so far only among spirochetes, epsilon and delta proteobacteria, and Bacteroides. The function is unknown and its gene neighborhoods show little conservation.	1.66544e-127
NZ_CP043450.1\|WP_112569242.1\|461239_462379_+\|cystathionine-gamma-synthase	gnl\|CDD\|366438	pfam01053, Cys_Met_Meta_PP, Cys/Met metabolism PLP-dependent enzyme. This family includes enzymes involved in cysteine and methionine metabolism. The following are members: Cystathionine gamma-lyase, Cystathionine gamma-synthase, Cystathionine beta-lyase, Methionine gamma-lyase, OAH/OAS sulfhydrylase, O-succinylhomoserine sulfhydrylase All of these members participate is slightly different reactions. All these enzymes use PLP (pyridoxal-5'-phosphate) as a cofactor.	0
NZ_CP043450.1\|WP_112569228.1\|452664_453480_+\|SDR-family-oxidoreductase	gnl\|CDD\|236216	PRK08277, PRK08277, D-mannonate oxidoreductase; Provisional.	5.80876e-118

>NZ_CP043450.1|WP_112569232.1|454998_456783_-|DUF885-domain-containing-protein
MNKNLLKSAGILMLLTGIGINTRAQQSAETKAWVAKSNEYTKIIIDLDKKYSPEYGSSQGLAEYDSDIAVPTLQNIMAERKDEEAVVAKLTEALKTEKNTFIQQDINIIITHLKLGFRQQDFELSRQVPFLNASSTIYSGLETLLDDQTPEARRQAAVMRIRKYAGLEKGYKPLATIYMERVQQQMAGKNMIYPSKQRMETDLSRNASIVSGIAELCTKYKVTGWEQPYATLKKQLEGYDKWVKANVLVKARTDFRLPPEEYAMNLESYGIDIPPAKVAEMAHALFNELQNEMKPIAEQIAKKRNLPSGDYRAVIRELKKEQIHGDSIIPLYEQHLKDIEGIIREHQLVTLPNRPAIIRLATAAETAQGPAPHMVPPPFLNNTGQRGVFVLPLNMPASPGEKATDKYDDFTFDAASWTIIAHEARPGHELQFDKMVEEGVSQARALYAFNSTNVEGWGLYSEYITRPYMPLEGQLVSLDYRLLRAARAFLDPELQAGKITQQQALDVLMNDVVQSRAFARQEVERYTINAPGQANSYFYGFTKMIALRKDTETALGSKFNALHFHDFILSQGILPPALIREAVMNDFVPKEKAL
>NZ_CP043450.1|WP_112569230.1|453946_454726_+|hypothetical-protein
MKLKSSLITLFTLAGFAASAQTVTLDYYFNHEVHKGANGQPERFHYLWDETDNNGFKIFGEAFTSRGAKLDTLGSAPTLENLKGSSVYIIVDPDTKKESPNPNYIQENDIEQIAAWVKKGGVLLMMANDSVNVELPHFNNLAAKFGMHFNNDLQNHVIDDAHFEDGAVYVKNNPVLKTATKVFMKDACSIGLSGPAVSVLKNKEGATIIASAKYGKGTVIAVGDPWLYNEYVNGRLPAGYENDKAANDVAQWLLKQARK
>NZ_CP043450.1|WP_112569228.1|452664_453480_+|SDR-family-oxidoreductase
MDNQFSLAGKVIVVTGGTGILGKAFIDGIVEAGGAVGILGRNAEVAEERANAINQAGGKAIALVADVMNEAELVAAKDKLLAAFGRIDGLVNGAGGNMPEGVLQPDEDIFKMNIEGMKKVMDLNLWGTLIPTQVFGEAIAQTGKGSIVNISSMNSKRAITKVLGYNMGKAAVDCYNQWFAVELANRHGDKIRMNALAPGFFLTEQNRNLLTKPEGGYTQRGELVIKQTPFKRFGQANELKGALVWLLSDASAFVTGSMICVDGGFSIFGGV
>NZ_CP043450.1|WP_112569226.1|451802_452633_+|5-dehydro-4-deoxy-D-glucuronate-isomerase
MKTIHSVHPSDFKSYDTTTIRERFLIDKQVQPDQINCTYTHYDRMIVGMANPVNKTLELPNYPNLRAEYFLERREIGIINVAGAGVITADGQAFEMNKLDCLYIGKGTKSVTFESKDASAPAVFYLLSSPAHALYPTTQLTHADAVKVELGSIATANKRTINKYIHLEGVRSCQLVMGLTILHEGSVWNTMPAHVHDRRMEAYFYFDVPAGQKIFHYMGEGQETRHITMDNYDAVVSPPWSIHSGSGTSNYSFIWGMAGENLDYTDMDAIAITDLK
>NZ_CP043450.1|WP_112569224.1|450921_451536_-|DUF386-domain-containing-protein
MKHLTTYKYIMLLILFSLTAAGASAQQQDITAKSAKTWVKSRVWANGLKLKLNSSTNDVEFAKQYAANKAAWDKAFEFLRERNLETIEPGKYTIDGDNVYAMITEGPSKEPEQAAWESHQNYIDVQYVIKGKEKIGVAAIESLTVTKPYDAEKDFANYSGEGKYYTATPEEFFLFFPSDGHRPNMKVNGYDKVKKLVIKVREIK
>NZ_CP043450.1|WP_112575992.1|450047_450566_+|lipocalin-family-protein
MKKEIIATSVALGLTALALQATRCKPLQTVPYVDLKKYVGSWFEIAALPQCFESGCTFTSAAYGLAKDGSIVVKNRCIKDNKIKIAEGRAVVADKTSNAKLEVQFQWPFKGKYWIIALADDYSYAMVGHPNRNYLWIISRRSTLDEQIYNQLVVQAAEQGFDVRKLVKTVQV
>NZ_CP043450.1|WP_112575991.1|449138_449936_-|SDR-family-oxidoreductase
MPGITNISILGCGWYGSALAKALLASGMQVKGSTTSAAKLDDLAAMGIKPYLINFLPNQEIYDADFFNCEVLWIAIPPKTRGGEAGIFLDKIKSIIEAIKRHQIKNVVFISSTAVYADSNKHVNEQTDPQPNTESGRILLEAENLFLAESRFKATIIRFAGLFGPARNPGRFFAGKKDIPNGDAPVNLIHLDDCIGISKAILAKQAFGYLFNGCSPDHPAKADFYTRAAIDSGLEKPEFIRELNEWKIVDSLNTSAILDYQYSGL
>NZ_CP043450.1|WP_112575990.1|447533_449063_-|glutamine-hydrolyzing-GMP-synthase
MQEKILILDFGSQFTQLIARRVRELNIYCEIHPFNHYPEIDSTVKGIILSGSPYSVRQEDAPHFDFEKFHTTRPILGVCYGAQYVAHFHGGEVLPSSTREYGRANLEYIKQDNPLFKDVPGGSQVWMSHGDTIATIGDNFEVIASTDSVKVAAYQVTGTQTYGIQFHPEVTHSIDGKQLLQNFLVDICGCKQDWTPDSFIETTVAALREKLGDDKVVLGLSGGVDSSVAAVLLHHAIGKNLHCIFVDNGLLRKDEFEQVLESYKHMGLNIKGIDAKQRFYDALAGLTDPEKKRKAIGRVFIEVFDDAAHEVQDVKWLGQGTIYPDVIESVSVKGPSATIKSHHNVGGLPDFMKLKVVEPLNTLFKDEVRKVGKALGIDPNILGRHPFPGPGLAIRILGDITPEKVAILQEADAIYINNLRAAGVYDKVWQAGSIFLPVQSVGVMGDERTYENVICLRAVESVDGMTADWCHLPYDLLAKISNEIINNVKGINRVVYDISSKPPATIEWE
>NZ_CP043450.1|WP_146750157.1|446317_447577_-|amino-acid-ABC-transporter-substrate-binding-protein
MISVQNHRPPLSGNKWLPFFCIALLLAACSPKTRPVATTVKKPTDNTEKKPGNTTEKPAEKASEQKVANIAMLLPLNLEHLNPAQKYSPLQISQANIAVEYYQGFKLALDSLTAYGNNYKLQIFDSRDEAMQAHDLALNAFVRSSDLIVGPVFPDGVKAFSGALSYSKGPILSPLSPANPATINSKNLITAIPPLEYHAWGAAEYLNRTVKPKKIFILRSGFNQENDYAVNFKKAIDSLSKKKIKVTNVYVVRGKLSSLLPQLSKTEKNVFVIPATDQAFLGVTLRSLDTLNKHYPVMVFGHPSWEKFSFLKPQLLQRLNTHITSTEKINYKAGATTTFLRNYRRAYHVEPTEYAIKGFDEGLYFGRQLFADKGLSSIEGTDFTGLHNSFHFIKKPGQGWINTHVNILMYTNFELKQVE
>NZ_CP043450.1|WP_112575988.1|445148_446321_-|RsmB/NOP-family-class-I-SAM-dependent-RNA-methyltransferase
MKAINQLKTFQRILGEYPADTPLSKFLPGFYRQNKQMGSTDRRVANRLVYNYFRLGRALPDVPEDERLLVAEFLCNTQTNSYLQNFKPEWAACIGFSDDDKLALVKTSYPDFKLEDVFPWSSQLSEGIDKEAFLKSFFCQPDLFIRVRNGYDHLVKAELTKAQVVFKDEGNGCYSLPNGTRLETIFAKQHWFEVQDYSSQQTGNYFKPQRWDSWWDACAASGGKSLLLHEDEPNIKLVVSDIRESILANLDERFQLAGLTKYQKKALDLTQNIDSVMHDYAFDGIILDAPCSGSGTWGRTPEMIAQFDNHKIEFFQKLQKSIAQNVVKYLKPGKPLIYITCSAFKGENEDVVDYLVNELGLKLEEKAVLKGYERKADTMFVARLSPSPIV
>NZ_CP043450.1|WP_112569236.1|457062_458544_-|hypothetical-protein
MKIKYLLSVIAIVAITKDSFAQYSQDAIRFSTFQTGSTSRIKAIGNAGTAIGGDLSSISGNPAGLGFFTHSEVSLTPEYDNSKINSSFFGQAGSANRNDLNMSNAAVVLYQQLNTTHKDKSKGWLSINYGAGYSRTNNFYENVAYGGTNQTSSISDYYAGIAKREVSQYGSVNPNGLDGWAYDHVLIDNFGPATDPNSYSSTVNVPVRQLAGITRTGGQSEFNLSFGANYSNKLYVGLGLAITDIRYNSNSAFTENGNAVITNGGAPTDFSSTFLQSQATKGSGFNAKLGIIYKPVQAVRLGFVFTSPTFYNIDDSYTEGLQTQYTGGSSYRNVSEPYQLSYNLRTPLKLAGGASVFIGKYGFISGDVEYIDYTTTHLSSNDSYTADGDNSDIKSLYRSTVNLHVGAEINVNSLVYLRGGYSQQGNPMKDLGSDIKTVSGGIGVHFGAYFIDATYARVTGRQTLFPYDVGATSPFADLKKTNNNAFLTLGYRF
>NZ_CP043450.1|WP_146749995.1|458577_459522_-|hypothetical-protein
MKRNIAIGMFIIGAMALSSCSTTKLASTQSNDDVYFSDARAGDEPVYAQQPAYNQTPAAQDGYSDDDDDYFYYDDYATRINRFSYFSPFGYYDDFYSAYNNYPYYNYGLGYGGLGYYGGPGYYSGWDLGYGYGGYGYGWGLGYGYGGLGLGYGYGYGGWGHGYYGGGYGYGGGYGGYYGGGYASSGTARPYRGNGNPFAGSGGRPVSSAVSGIGYVPGGRNRPLGSRTNTYSTYSTGSNGSNSYNNNTGTRYARPARTDAAPTRDSQPVYRQPQVERASQPQPSYTPASSSSSGGSSRSTGSSSGGGGGRPSRP
>NZ_CP043450.1|WP_112569240.1|459622_461095_+|proline--tRNA-ligase
MSKGVISKDEDYSQWFNDLVIKSDMAEYSPVRGCMIIKPYGYSIWEKIQAVLDEMFKETGHSNAYFPLLIPKSFFSKEASHVDGFAKECAVVTHYRLKNDGEGNIIVDEEAKLEEELIIRPTSETIIWNTYKGWIQSYRDLPILVNQWANVMRWEMRTRLFLRTSEFLWQEGHTAHATAEEAIAETEQMLDVYADFAENWMALPVVKGRKTANERFAGALDTYCIEALMQDGKALQAGTSHFLGQNFAKAFDVKFTNKENKLDYVWATSWGVSTRLIGALIMAHSDDAGLVLPPKIAPIKVVVVPIYKHQEELDNISAYVAALSKELKAKGISVKFDNRDTHRPGAKFAEYELKGVPLRVAIGSRDMQNGTVELARRDTKTKETVNQEGLAQVIENLLEEIQQNIYKKAFDFRAGNTKEVDTWEEFKRVLDEEPGFISAHWDGTSETEQKIKEETKATIRCIPLNNKQEEGKCIFTGKPSTQRVLFARAY
>NZ_CP043450.1|WP_112569242.1|461239_462379_+|cystathionine-gamma-synthase
MKFATKAIHAGQEPDPTTGAIMTPIYQTSTYWQKSPGDNKGYEYSRGTNPTRKALEDCLAALENAKFGLAFSSGMGATDAVMKLLAPGDEVITGNDLYGGSYRIFTKIFANYGVKFHFLDLSDPEIVRAHVNDKTKLVWIETPTNPTMRIVDVEAIGKITKEKNLLFVVDNTFASPYLQNPIDMGADIVMHSVTKYIGGHSDVVMGALMLNDEELYKKLWFIYNACGATPGPMDSFLVLRGIKTLHLRMKAHCENGRQIAEFLKDHPKVEKIYWPGFTDHPNHDIAKKQMRDFGGMISIVLKDADLQETFRIASSFKVFSLAESLGGVESLINHPVSMTHGSIPKAEREKAGVVDNLLRLSVGVEDIEDLLEDIKQALS
>NZ_CP043450.1|WP_112570009.1|462467_463259_+|TIGR02757-family-protein
MTENLKAFLDAKVAQYNRPEFIENDPVTIPHMFSQKQDIEIMGFWAATLAWGQRVTIIKKCKELIALMDGAPYDFIINHEEPDLKRLLKFKHRTFNDVDTLYFIAFFRQHYERFGSLEDAFLPPGPQKREHGLAVEHALNSFRSYFFSLPDFPHRTKKHVSSPSQKSTCKRLNMFLRWMVRKDDNGVDFGIWSRIKPADLICPLDLHVDRVSRKLNLINRKQTDWQTAVELTQRLREFDPNDPVKYDFALFGLGIEERWGVQF
>NZ_CP043450.1|WP_112569244.1|463271_463565_-|hypothetical-protein
MSALKNVLITLSFLLILAGCSVKHYTIGMSESEFKNSEKYNLELVEETSQHAVYRRVASADAQMKPLSYHYYYFNSGTLVRTELIETNKPDIVLLSK
>NZ_CP043450.1|WP_112569246.1|463646_464705_-|nucleoid-associated-protein
MVTFFEASLETISVHHVGNQSQEEMYALSEQPLELKDDVIPNLLMQYFLKPFEKANEVYHLMHSSGDLQLNELHHFATQVFDDNTKFHEASEKIAKHLYKVTNHPNIKGGELYVVYFNKVQIEGNPLNAIGIFKSENKETYLKVYPDKGGFQVDYEQDAININKLDKGVLIFNIEKENGYKVVVVDKTNTGQEAARFWKDDFLQLKIRNDSFNQTNNTLGIYKNFITEKIDEEFEMSKADKIDLLNRSMKYFKEKETFDMEEFSNEVIGNEQAIESFKNFKNQYEEEFDSPIADNFIISENAVKKQARVYKSVLKLDKNFHIYIHGDKELIEKGFDDGRAMNYYKVYFKEEA
>NZ_CP043450.1|WP_112569248.1|464932_466300_+|tRNA-uridine-5-carboxymethylaminomethyl(34)-synthesis-GTPase-MnmE
MTDNTDTIVALATPNGVGAIAVIRLSGPDAISIANSVFKGKDLSKQASHTIHFGSIADGDLILDEVLVSLFVGPRSYTRENVVEISCHASGYIVESIIKLFIKKGARSAKPGEFTLRAFLNGQLDLSQAEAVADLIASNSKASQQVALQQLRGGFSTQLQALREQLVNFASLIELELDFAEEDVEFANRDQLKNLIHEITRIVGRLINSFELGNAIKNGVNTVIAGRPNAGKSTLLNALLNEERAIVSHIPGTTRDTIEEVLNIQGINFRLIDTAGIREATDAIEQIGVQRTMEKISQSALLIYVFDAAEITIEELNKDIESLQKPGITMLVVANKADLLNPEQLSALPHTDRAIIISAKEKRHIDELKHKIYSSAVKDQLSGDETLITNIRHLEALQKTEEALIRVLGGIDGSITSDFLSMDIKQALHYLGEITGVVTTDDLLENIFSKFCIGK
>NZ_CP043450.1|WP_112569250.1|466607_470039_-|SUMF1/EgtB/PvdO-family-nonheme-iron-enzyme
MSARQTKKYDVFLSHNSLDKPIVEEIAQWLVKESYKVWFDKWELIVGEAWQEELELGLSHSACCIIFFGSNKLSPWQNEEMRVALSAKASNRSIRVIPVLLPLAKNEEKESQLPAFLQRLTWVKFENNIYEAEPLRRLKCGIDGIPPGRPSKISNKRTSEKNPFKGLEAFGEKDKEYFFGRDFFIQKLKNHIDLYKLLILTGPSGSGKSSIILAGLVPLLRESNLITAIFTPRIDPINELTVALKRSIETKQTGESLKKELKNSESGEALYFFLRHFTSEDKKMLLIVDQFEEIFTQTTEDLRIQFINLLLKARDDENVRIILTMRSDFIGNCAVYPNLNLLVNDHLVQIGPMSEDELRAAIVEPSMLENLRLEEGLVDRIISDSKGASSELPLIEYALSELWRKRQGNTLTNIAYKSIGGVEGALVNRADAEYNLLSPSEQQLLRRMISLRLIQPGDGAMDTKRKASKTELHSMGEEKSVEKMIQLWTGKNLRMMTVYEDPISKQVYVELAHETLIRNWGKIQEWMQEDRETSKIINKIRLLAIDYTNLGEDYLLHGTQLQHVIKFSDILSGRLTETEEKFIKDSIERERTLKAREFKTAQDLKNAKSRSLTLLVITLIIIFLGLTTVTILFYSKKQTLNEYERLADSERINRAKTEAEKLWPLGPKSIEPLNQWIINYSFLINRLKLHQAALDRLRLSALQYTHKEKLADFFPEITALKNAVEAETKIKSRLMYAKEKEKPPLKKQLKEEEERIAKLRSDTAGRRTWNFGDDLEKQFRHDILSKLVVALTDFSAKNGLFADIKARLNKSKKIKKSTIDDFKAQWAQVNMRLARSKKYMNLRLSPQLGLIPLGPDPKSGLEEFIDWQTNEKELPERAETGSFTIKPSTGIIFVLIPEGEFYMGAQKKTPSLTNYDRQALENEMPVRKVKLKAFFLSKYEMTQGQWLRITGKNPSFHKPGYIRQPMPSPVTLSHPVEQVSWNEAKSTLSKLGLDLPTEAQWERAARADLNLIYAGTSKISELSRFSNIGGIEAKKVWPDLKSTYKDSWLIHSPVGSFEPNNFGLYDMTGNVFEWCKDQYSDYSIPPRNGDGLRISGETARIDRGGGFAYDQLSARIASRNKVDPDYKDYFLGVRPVRLISYLK
>NZ_CP043450.1|WP_112569252.1|470856_473955_+|TonB-dependent-receptor
MKKKVPPKKLGMYLLCCIMLLCYQHVFAQQKRSIIGHVTDEHGQALPGVSILLEGTGLGTSTDQNGFYKISVPDANAKLSFSFVGYTKKIVSVTKDWNGDVSLTPDKNAGSLGEVVVIGYGSRKKANLTGAVSTVKGTELEKSPVANVSNTLAGAVPGLIVNTRSGEPGADDASILVRGKGTLGNTSPLVVIDGIPDRGFNRLDPADIESFTVLKDASGAIYGARAANGVILITTKRGTAGKATLSFTSNFSITQPTRVPKMLSSWQYAQAANEYDDLVGQQHEYTADDIQKYRDGSDPLGHPNTNWWDAVMRKWATQTNNTLTLRGGSDKVKYYISGQHLYQNSIYNSGADYYKNDNARANIDIAATDNFKIGVDVMYRSEFKNGEAPGYDANGIFQQLWNAYPYLTPVYPNGKVGVGIGGGPATSMVYILNQDLGYTHNTYDFLQTKTSFSWALPKVTPGLHLDGYFAYDVNSRAYKGFNAMPPPAYSYNKITTNYDEYTSTVPPNLSISNYQTKSRLTNIKLGYERKFGKHGIEAFVAYEQQQQTYTELDAYRTGFLSNNVQELFAGSTEGQTNNSATTQFARQNFISRLSYNYDDRYLLDYNMRYDGSPNFPAGKRFGFFPSVSAAWRISQEPFFHSSVIDDLKLRGSWGKTGNDAVASFQYLQTYGLQAGQISQYLGAGYYYGPNATQTPGFTLGPTPNANITWEVATTTNIGFDAQLFHAFSVSVDAFRSSRRNILVPPSASVPDYTGLTLPDVNLGKVDNKGIELDLGYSKKLGNDFSFNINGNLTYAVNKVVYGAEPANVPDYQRVTGHPIDSWLLYQADGIFQNTAELNAYPHPVGTGVGDIRYKDVNHDGVINDLDKVRNTLSNTPQILYGLTLGGRYKNFDFTVFFQGQARAQAILKPNGLNMAEEFFDGRWLKEGDNNYPRTFNGPTSRTFGSNAYPSTFWLRNDSFLRLKNVELGYSFSKELLSKIKVKGARVFVSGNNLFSFDKFGPSFDPESATGTVNDGRIYPQQRIINLGVNVTF

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Crispr_ID: NZ_CP043450_3

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043450_3

1343334-1343482

Orphan

Consensus_repeat	Method
GATATTTTACCGGTTGCATCTACAGAAATTGTTGTTCCGTCGGGGAT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043450_3

>merge|NZ_CP043450|3|1343334-1343482|CRISPRCasFinder
GATATTTTACCGGTTGCATCTACAGAAATTGTTGTTCCGTCGGGGATTACACCGCCCAGTTTCGTTGTCGTAGCTGCTTGTAAGGTATAAGAATTGGGAGCTGATATTTTACCGGTTGCATCTACGGAAATTGTTGTTCCGTCGGGGAT

>NZ_CP043450|3|3|1343334-1343482|CRISPRCasFinder
GATATTTTACCGGTTGCATCTACAGAAATTGTTGTTCCGTCGGGGAT	TACACCGCCCAGTTTCGTTGTCGTAGCTGCTTGTAAGGTATAAGAATTGGGAGCT
GATATTTTACCGGTTGCATCTACGGAAATTGTTGTTCCGTCGGGGAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043450.1\|WP_146750081.1\|1327041_1330329_-\|PAS-domain-S-box-protein	unknown	unknown	gnl\|CDD\|274362
NZ_CP043450.1\|WP_112574030.1\|1346837_1347302_+\|polyketide-cyclase	unknown	unknown	gnl\|CDD\|176903
NZ_CP043450.1\|WP_112574040.1\|1333122_1334715_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|380159
NZ_CP043450.1\|WP_112574044.1\|1326372_1326912_+\|DUF3347-domain-containing-protein	unknown	unknown	gnl\|CDD\|378730
NZ_CP043450.1\|WP_112574031.1\|1346515_1346857_+\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|223713
NZ_CP043450.1\|WP_112574045.1\|1325117_1326365_+\|FtsX-like-permease-family-protein	unknown	unknown	gnl\|CDD\|182528
NZ_CP043450.1\|WP_112574038.1\|1338052_1339249_+\|alpha/beta-hydrolase	unknown	unknown	gnl\|CDD\|225375
NZ_CP043450.1\|WP_112574039.1\|1334747_1337762_-\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|274948
NZ_CP043450.1\|WP_112574025.1\|1352402_1353131_+\|ATP-dependent-Clp-protease-proteolytic-subunit	unknown	unknown	gnl\|CDD\|184722
NZ_CP043450.1\|WP_112574036.1\|1342327_1342927_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|371327
NZ_CP043450.1\|WP_112574027.1\|1349329_1350313_+\|c-type-cytochrome	unknown	unknown	unknown
NZ_CP043450.1\|WP_112574028.1\|1348516_1349239_+\|DUF2807-domain-containing-protein	unknown	unknown	gnl\|CDD\|371327
NZ_CP043450.1\|WP_112574026.1\|1350619_1351978_+\|trigger-factor	unknown	unknown	gnl\|CDD\|272913
NZ_CP043450.1\|WP_112574041.1\|1332032_1333061_-\|SusF/SusE-family-outer-membrane-protein	unknown	unknown	gnl\|CDD\|240566
NZ_CP043450.1\|WP_112574033.1\|1344733_1345588_+\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|180446
NZ_CP043450.1\|WP_112574029.1\|1347791_1348400_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|371327
NZ_CP043450.1\|WP_112574042.1\|1330460_1331747_+\|citrate-synthase	unknown	unknown	gnl\|CDD\|99867
NZ_CP043450.1\|WP_112574034.1\|1344002_1344593_+\|TetR/AcrR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224228
NZ_CP043450.1\|WP_112574032.1\|1345626_1346370_+\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|187585
NZ_CP043450.1\|WP_112574037.1\|1339469_1341365_+\|RecQ-family-ATP-dependent-DNA-helicase	unknown	unknown	gnl\|CDD\|223588

Protein	Function_ID	Function_description	E-value
NZ_CP043450.1\|WP_146750081.1\|1327041_1330329_-\|PAS-domain-S-box-protein	gnl\|CDD\|274362	TIGR02956, sensor_protein_TorS, TMAO reductase sytem sensor TorS. This protein, TorS, is part of a regulatory system for the torCAD operon that encodes the pterin molybdenum cofactor-containing enzyme trimethylamine-N-oxide (TMAO) reductase (TorA), a cognate chaperone (TorD), and a penta-haem cytochrome (TorC). TorS works together with the inducer-binding protein TorT and the response regulator TorR. TorS contains histidine kinase ATPase (pfam02518), HAMP (pfam00672), phosphoacceptor (pfam00512), and phosphotransfer (pfam01627) domains and a response regulator receiver domain (pfam00072). [Signal transduction, Two-component systems].	1.21319e-88
NZ_CP043450.1\|WP_112574030.1\|1346837_1347302_+\|polyketide-cyclase	gnl\|CDD\|176903	cd08894, SRPBCC_CalC_Aha1-like_1, 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.	3.52426e-64
NZ_CP043450.1\|WP_112574040.1\|1333122_1334715_-\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	gnl\|CDD\|380159	NF033071, SusD, starch-binding outer membrane lipoprotein SusD. SusD (Starch Uptake System D) is an outer membrane lipoprotein that binds starch and participates in a TonB-dependent nutrient uptake complex. Related proteins from similar TonB-dependent complexes that import other, usually multimeric nutrient substrates include RagB and NanU.	2.61337e-143
NZ_CP043450.1\|WP_112574044.1\|1326372_1326912_+\|DUF3347-domain-containing-protein	gnl\|CDD\|378730	pfam11827, DUF3347, Protein of unknown function (DUF3347). This family of proteins are functionally uncharacterized. This protein is found in bacteria. Proteins in this family are typically between 169 to 570 amino acids in length.	2.16114e-40
NZ_CP043450.1\|WP_112574031.1\|1346515_1346857_+\|helix-turn-helix-transcriptional-regulator	gnl\|CDD\|223713	COG0640, ArsR, Predicted transcriptional regulators [Transcription].	1.10023e-11
NZ_CP043450.1\|WP_112574045.1\|1325117_1326365_+\|FtsX-like-permease-family-protein	gnl\|CDD\|182528	PRK10535, PRK10535, macrolide ABC transporter ATP-binding protein/permease MacB.	1.10618e-39
NZ_CP043450.1\|WP_112574038.1\|1338052_1339249_+\|alpha/beta-hydrolase	gnl\|CDD\|225375	COG2819, COG2819, Predicted hydrolase of the alpha/beta superfamily [General function prediction only].	6.63266e-40
NZ_CP043450.1\|WP_112574039.1\|1334747_1337762_-\|TonB-dependent-receptor	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_CP043450.1\|WP_112574025.1\|1352402_1353131_+\|ATP-dependent-Clp-protease-proteolytic-subunit	gnl\|CDD\|184722	PRK14514, PRK14514, ATP-dependent Clp endopeptidase proteolytic subunit ClpP.	7.18393e-119
NZ_CP043450.1\|WP_112574036.1\|1342327_1342927_+\|hypothetical-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).	2.2514e-09
NZ_CP043450.1\|WP_112574028.1\|1348516_1349239_+\|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).	4.41187e-40
NZ_CP043450.1\|WP_112574026.1\|1350619_1351978_+\|trigger-factor	gnl\|CDD\|272913	TIGR00115, tig, trigger factor. Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY). The central domain of trigger factor has peptidyl-prolyl cis/trans isomerase activity. This protein is found in a single copy in virtually every bacterial genome. [Protein fate, Protein folding and stabilization].	2.45584e-53
NZ_CP043450.1\|WP_112574041.1\|1332032_1333061_-\|SusF/SusE-family-outer-membrane-protein	gnl\|CDD\|240566	cd12967, CBM_SusE-F_like_u1, Uncharacterized subgroup of the CBM-SusE-F_like superfamily. The CBM SusE-F_like superfamily includes starch-specific CBMs (carbohydrate-binding modules) of SusE and SusF, two cell surface lipoproteins within the Sus (Starch-utilization system) system of the human gut symbiont Bacteroides thetaiotaomicron. These CBMs have no enzymatic activity. The precise mechanistic roles of SusE and SusF in starch metabolism are unclear. Both proteins have an N-terminal domain which may belong to the immunoglobulin superfamily (IgSF), followed by two or three tandem starch-binding CBMs. SusF has three CBMs (CBM-Fa, -Fb, and -Fc; F denotes SusF, and they are labeled alphabetically from the N- to C- terminus). SusE has two CBMs (CBM-Eb and -Ec, corresponding to CBM-Fb and -Fc). Each starch-binding site contains an arc of aromatic amino acids for hydrophobic stacking with glucose, and hydrogen-bonding acceptors and donors for interacting with the O-2 and O-3 of glucose. These five CBMs show differences in their affinity for various different starch oligosaccharides, and they also contribute differently to binding insoluble starch. Proteins in this group are present in the species of the Gram-negative Bacteroidetes phylum.	2.60077e-23
NZ_CP043450.1\|WP_112574033.1\|1344733_1345588_+\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|180446	PRK06180, PRK06180, short chain dehydrogenase; Provisional.	6.25716e-107
NZ_CP043450.1\|WP_112574029.1\|1347791_1348400_+\|hypothetical-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).	9.69393e-07
NZ_CP043450.1\|WP_112574042.1\|1330460_1331747_+\|citrate-synthase	gnl\|CDD\|99867	cd06114, EcCS_like, Escherichia coli (Ec) citrate synthase (CS) GltA_like. CS catalyzes the condensation of acetyl coenzyme A (AcCoA) and oxalacetate (OAA) to form citrate and coenzyme A (CoA), the first step in the citric acid cycle (TCA or Krebs cycle). The overall CS reaction is thought to proceed through three partial reactions and involves both closed and open conformational forms of the enzyme: a) the carbanion or equivalent is generated from AcCoA by base abstraction of a proton, b) the nucleophilic attack of this carbanion on OAA to generate citryl-CoA, and c) the hydrolysis of citryl-CoA to produce citrate and CoA. There are two types of CSs: type I CS and type II CSs. Type I CSs are found in eukarya, gram-positive bacteria, archaea, and in some gram-negative bacteria and are homodimers with both subunits participating in the active site. Type II CSs are unique to gram-negative bacteria and are homohexamers of identical subunits (approximated as a trimer of dimers). Some type II CSs including EcCS are strongly and specifically inhibited by NADH through an allosteric mechanism. Included in this group is an NADH-insensitive type II Acetobacter acetii CS which has retained many of the residues used by EcCS for NADH binding.	0
NZ_CP043450.1\|WP_112574034.1\|1344002_1344593_+\|TetR/AcrR-family-transcriptional-regulator	gnl\|CDD\|224228	COG1309, AcrR, Transcriptional regulator [Transcription].	4.62934e-14
NZ_CP043450.1\|WP_112574032.1\|1345626_1346370_+\|SDR-family-oxidoreductase	gnl\|CDD\|187585	cd05324, carb_red_PTCR-like_SDR_c, Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs. PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. 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, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-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.	7.71619e-85
NZ_CP043450.1\|WP_112574037.1\|1339469_1341365_+\|RecQ-family-ATP-dependent-DNA-helicase	gnl\|CDD\|223588	COG0514, RecQ, Superfamily II DNA helicase [DNA replication, recombination, and repair].	5.20157e-148

>NZ_CP043450.1|WP_112574036.1|1342327_1342927_+|hypothetical-protein
MKTTSIAIATVMFMVLGFANIASAKTAKNDAAVVLTDISKINKIEVYGNVELYISSGPADEIKVYNRYYSENALVQSQKGVLRISSYKNEKLVVWVTANQLSAISAYDNADIKSFGSFSGIDLDVKLNNNASASLNLDTYSASITLSGNAKAELKGNTNEYSLTRNVTSNVNSNGLAYAHATETLNKETKPRVDEFATL
>NZ_CP043450.1|WP_112574037.1|1339469_1341365_+|RecQ-family-ATP-dependent-DNA-helicase
MTIEEILKQYWNHDTFRPMQAEIIQSVLLGNDTLALLPTGGGKSVCFQVPALAKEGICIVVSPLIALMKDQVENLRAKGINAISIVSGMGRREIDLALDNCIYGSVKFLYLSPERLLSELVRERVKYMKVNLFAIDEAHCISQWGYDFRPPYLHIADLRELHPNVPVLALTATATADVKADIQEKLKFKNPVVYQQSFERSNISYVVQYEEDKFRKMLDVVRGVKGSGIVYVRSRKETFEIAKFLSDNGIRADYYNAGLSVDQRAEKQEAWKNNRVQVIVATNAFGMGIDKPDVRFVIHKDIPESLEAYYQEAGRGGRDGNKAFGVLLYNPADKLKQEKMFELNFPSIDEIKQVYHHLANYFQLAYEAGEGLSFDLDLGEFCSRYKLDAIKTLNALKFLERDEYLAFNESVFLPSRFQFEVVNEQLYNFQIQNAGWDPFVKTLLRSYGGAFENYVRIKEFDIARRTGLSVQQVIEGMLQLQQYGLLSYMQQTDKPQVTYLKPRVQGSHLIIDRKYIEQRKEVYRQKMEAVFDYAIHKRCRSQMLLAYFDETDSRKCGVCDVCLEEKRKVNQDEIFDNITTEIVQLLSISNPDIGNLITGINIGTEKEKMETIRLLLDAGKIKTDGEAYYLS
>NZ_CP043450.1|WP_112574038.1|1338052_1339249_+|alpha/beta-hydrolase
MQPISGNVPGNVTDFNCFMMMKKIIFCAFLVFGQNFLLFSQVKISFFTGKIQAPKSPLERLFLAGDFNGWNPADKTWELVKNGNGNYALSKELPVGLIHFKITRGSWNTVECDATGKSIDNRSLVIKSDTNVKLDIAGWQDSFAPAEKKHTATARVHIISENFEIPQLGRERRVWIYLPAGYDTGSKKYPVIYMHDGQNLFDEYTSSYGEWGIDEIMDKMPEQEESIIVGIDHGGDYRLTEYNPYDSKYGKGRGDDYVQFLVKNLKPYIDAHYRTESDATHTTIAGSSMGGLISMYALLKYPEVFGNAGVFSPAFWNAPQLFDLAKQVKISAKSRFYFVCGDAESDTMVPDMQKMADVVKSRGIKAENAPVTVIKGASHNEKQWNGDWPGFYKWLIGF
>NZ_CP043450.1|WP_112574039.1|1334747_1337762_-|TonB-dependent-receptor
MRKNYSKKYVLLCAFLMMSFMAFSQTGSIKGKVSDETNLPLPGATVTIDGTTIGSTTDPNGNYAINNVKAGTYTLSVKFIGYITIKKSVTVSGATIENFSLLPESKSLSEVVVIGYGTQRKKDLSGAITNVTAKDFQKGVITTPEQLIAGKVAGVSVISNSGAPGAGSTIRIRGGASLSASNDPLIVIDGVPISNASISGAANPLSLINPNDIESFSVLKDASAAAIYGNRASNGVILITTKKGKSGKPVIDFSSQVSASKIPKEASVLSADQIRDYVKANGTAAQIAQLGTASTDWQKQIYQTGITTDNNISVSGATKHLPYRVSAGYLDQDGVLKTSSMQRITGAINLSPSFFTDHLKVNLNAKGAQVKQRFANEGAIGSAVSFDPTKPVYSGNSRFGGYWQWLNNPAQPGGPLKDLATLNPLGLLEQQDNRSTVYRSIGNLQLDYKFHFLPELHANVNLGYDVSKGTGHNIIPDSAASNYKGFLDTKGVTHRGLNNQYKQTQSNTIFEGYLSYAKDLKSIASHIDAVAGYSYQDFSITNYNFGNFAHDGTEQPGTQPVYPYDKPENRLISVYGRLNYVFEDKYILTGTVRRDGSSKFNPNQRFGTFPSVAFAWKLKEESMFKGITALSDLKLRAGYGITGQQDGIGNYDVISFYNLSTNTAQYQFGDSFYNLYRPGGYYALRTWEQTAATNVAIDFGFLDNRITGTVDYYHRKTSKLLNKIPQPAGTNFSNYIVANIGDLTSNGLELNLSADVIRTSDITWNVNLNATYNTNKITKLTLAPDPSYPGAPTGGISGGTGNTIQINSVGYSRNSFYVYQQVYGTDGKPLDGVYVDRNKDGIVNENDLYRYKSSDPKGYFGLSSNLNYKKWSAGFVARASVGNYVYNNVFSSSGTQLSVFNGIGILNNASTNLLESGMTGSFDKSRLSDYYIQNASFIRMDNVNVGYNFGKVFHNTGNLRLSANVQNVFVITKYKGLDPEVNTGIDNNLYPRPRTYVLGLNLSL
>NZ_CP043450.1|WP_112574040.1|1333122_1334715_-|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKRHSLKYITITALIAGGLTSCTKKLDLLPTNDVTASQVYSTPEGYKQAFAKVYGAFALTGNKGPAGDDGTKDIQGIDEGTSDFFRLYWCAEELPTDEAVVGWGDVGLPDFHNMSWSSSNTFLTGLYYRCMYQITLANDFIRQSSDANLSSRGIKGTDADKVHQYVAEARFLRAYQYSILMDLFAAPPFVTENDPLGGPLPKQISRKDLFAYIESELKAIDAGLVDARGNEYGRADKAAAWALLARIYLNAEVYTGTAHYPDAVTYSKKVIDAGYSLVTDYTKLMRADNNLNKNEFILTINYDGLHTQSYGGATFMTHAPVGGSMPAADYGIAGGWAGLRTTKAFVNLFPGGASSADKRAQFYTDGQNIDINTISTFTDGYAISKFKDVKIDGGAPQSLDYADMDLPIFRLAEQYLIYAEATTRGGGGDAALALSYVNKLRARAYQSATTGQLTALTTDLLLDERGRELYWEGFRRTDLIRYKKFVEDTYLWPFKGGSKDGKGVESFRTVYPLPSADVTANPNLKQNTGY
>NZ_CP043450.1|WP_112574041.1|1332032_1333061_-|SusF/SusE-family-outer-membrane-protein
MKKIFTTLLAFGGIALLMLASCKKDETKVVANVGKVGALTSTTTSPALSKPNANNDAVTFSWAATPVTGYNAPVTYTLQLDVKGDNFKNTREVSTDKLTQTLKVGVLNDMLTALKLSYNDPSQVEVRIKSSAAPNLAATYSNVITLTVLPYQGTGYIYVPGAYQGWDPATADSLVSPNNDGVYDGYIGFPAGKLEFKITPKKVWDVAYGDAGSGKISTTGGNISVPAAGYYALHAVIDQSDKTKGTFTATPVFWSVIGDATPGGWNTDTDMLYDATTKTWSVTVALIAGKDMKFRFNHNWDVNLGGTPAALTAGGGNYTITTGGTYKIVLNTVVNTFTITKL
>NZ_CP043450.1|WP_112574042.1|1330460_1331747_+|citrate-synthase
MAETAQLKIGDKTFELPVIEGTEGEKAIDISKLRDQTGYVTLDIGYKNTGATKSAITFLDGEQGILKYRGYPIEELAEKSSFIEVAYLLIYGELPTAEQLKAFQYELSRHTLVHEDMKKFFDGFPSKSHPMGQLSSLVSALSAFYPESLKPSQTTEELNQSIIKMLAKMATVVSWIYKKSLGHPVIYPQNKYDYVTNFLYMTFGQRTEDVTIDPVVIDAMNKLLILHADHEQNCSASTVRIVGSSDSNIYASVSAGISALWGPLHGGANQAVIEMLEKIKEDGGDTDKWIAKAKDKNDPFRLMGFGHRVYKNFDPRAKIIKKACDDILEKLGINDEVLEIAKKLEEVALKDPYFVERKLYPNVDFYSGIIYRALGFPTDMFTVLFALGRLPGWIAQWKEMKENKEPIGRPRQIYVGATDREYADIASR
>NZ_CP043450.1|WP_146750081.1|1327041_1330329_-|PAS-domain-S-box-protein
MIKKLLQNMSLKGNSLVMIQNEATVYRLLLIGLFIASPSLHYLCFQNSYDPFWLRAINCFFCAVALFFSFINNAAFYKAAIVATVSSFLVINNCILLSKNEFAHVYLFSAITIFIALTLFCRKRREFIIISEANLAAIVIAYFMATKPVISSTVLVVLILVFTLIAYVSFLVVMAYQYQLKRAVDNVMELNNNLMQNDAELREHRKHLHALINSLNDIIFEFDETKICRNVWFNELTERAVDPRVAIGKTLDMVVGPQKAHKYDMALNYVMANRKPTSVEFPSDYDSGHWFIANFTPVFDSDGTYTGRISASVVDITEQKKYELALKENESLLLEAQNIAKIGNWWYDHESKETHWSANLNDLLEIEAIPGGMNRFHYYISLVHPDDRENTFQYLNAIRSTSQNKFEHKFITPAGKLKYIRIQRGEKELRSGTGSGTRTFGIIQDITEARLADKAVKLSQLELMEAQAIAKIGNWKYDVSTGNLSWSDELNNIYELGQDTSLYRKTFVNLLLKYVHPNDKNIIRKLLQSDANTMDSSHEYRIITPRGNLKYLSIIAGKRLYNEDGSVRKIIGTLQDITERKQAELDFRSAENKYKSVLEKINMIAITVDGDGTITFCNKYLAKLVGYKQQELIGMNWMDNFIPDDLKDFLKSWFANNAILPHFINPIICRNGEQRIISWQNTVFYDENGDIKETTSIGEDITDQQKAQQELIWAKEMAEKSSKFKSEFLSIMSHEIRTPMNAVIGSTNLLLDQDPRPEQMEYLNTLKFSGENLLAIINDILDYNKIEAGKLELNNSRFNIHQLIRKIKQSFESRAAEKALTLELIADDTIPADLMGDAMRLSQVLNNLISNAIKFTHNGKVTIRLDKDVTTENTVTIKFAVTDTGIGISPESFNIVFDPFMQDQQVINNDYGGTGLGLAITKRLIELHNSTIAVSSELGKGTTFCFSINFAVAPAIATPKPEVAPAPVTDNNLQGMNILVVDDNKMNLMIAGRFLKRWNAQVQEALNGKIAVDMVNHNTYDLIIMDLQMPVMNGFEATAIIRQSHPDIPVIALTADAMPETYQQALEAGMCDYLTKPFVPEILYSKLAKHIRQSA
>NZ_CP043450.1|WP_112574044.1|1326372_1326912_+|DUF3347-domain-containing-protein
MKTIKGFCFLAALAAATACNQPAKQQDSTKADSTATNAAKPAETQVAADTANTSDVLKAYIALKDEFIKSDVAGIKTAATDLEGKLSGIKGCTETATVAHQITTAADIKAQRDAFLVLSKDVIALVKGAKLKSAPIYVDFCPMADGGKGGYWLSSTKPIVNPYFPEHMKECGSVKEQIN
>NZ_CP043450.1|WP_112574045.1|1325117_1326365_+|FtsX-like-permease-family-protein
MLFLKLLRESFLFAGDALRQNKTRTLLSLLGVTIGIFTIIAVQSAVDTLRNNLQTSVNKLGNNSIYVQKWPWVGGSDFPWWKYLQRPESDLRDFNELSRRITTAEALSYEINIDNRTIKYKSNTVEGAQVDAASADHDKTWNFDFESGRYFTDMESKTGAPITNIGYDIAQNLFPDGDAVGKQIKVMGRYVTVVGVFSKQGKDMLGISTDKEVLLPLNFARNLIDIQSSKYGPSIIVRGKKGIPTDDVESEIKGLMRSIRRLRPGADDNFSLNRTTMITQQLDDLFKVVNIAGAIIGGFSILVGGFGIANIMFVSVKERTNIIGIQKSLGAKNYFILLQFLIESVLLCFVGGIIGLLFVYLGTFAVKAALDVQVILDAANISRGLSYSIIIGVIAGIIPAYSASRLDPVEAIRTN
>NZ_CP043450.1|WP_112574034.1|1344002_1344593_+|TetR/AcrR-family-transcriptional-regulator
MGKAERTRQFIIETAAPIFNEKGIAGTTIDDILAATKMAKGGLYGHFESKDEIASVMVNYLLDKLSDKVNTVMAKEKTAIKKILAFIDIYKDPIDSYIDGGCPILNFGVEADDNNPMLKQRLKTMIEEGQKVFVEIINKGVADGEISSEINAADYALKMFTLLEGGMLVSRVTGSGKYMNSLVRMLKNELKEYELK
>NZ_CP043450.1|WP_112574033.1|1344733_1345588_+|SDR-family-NAD(P)-dependent-oxidoreductase
MKIQKVILVTGASKGFGLEIAKTALAAGDKVIATVRSKADQLAATLSNNPNLLVVTMDVTNEAQVKAAVAEGLLRFGKIDVVINNAGYGIVTAIEEATDAEVKAQYETNVFGLLNVLRAVLPHLRAQKSGHIINVSSLFGFDAIPGWALYGSTKFAVEGISKGLAAELAPLNIKVTVVEPGLFSTEFLSAESYSAAKNIIADYTETVGPMRTGADQLHGNQPGDPKKLAKVVVDIAHNENPPLHLPIGKDAVGMYKANAEKTSKEIDQWIAVSTSTDHDHVATK
>NZ_CP043450.1|WP_112574032.1|1345626_1346370_+|SDR-family-oxidoreductase
MSTKKIALITGANRGIGFETAKQLGEKGVAVIVAARKLSAAEETAVQLTEQGIEAYGVQLDVTNADERKAIAAYIENKFGKLDILVNNAGVGPKDNDLFVKKTVATTADEFEYIFNTNLFSIVYLTNELLPLLKKSEAGRIVNLSSILGSITIHATEGSPIADFKRLSYSASKAALNVFTVLLADELKGTKIKVNSAHPGWVQTELGSVEHAPMSVPDGAKTSVELSLIGEDGPNGRFIHLGEELPW
>NZ_CP043450.1|WP_112574031.1|1346515_1346857_+|helix-turn-helix-transcriptional-regulator
MKARRDVYQAVADPTRRAIINMIATQPHNVNTIAANFDVTRQAISLHIQILADCGLINVKQQGRDRICEARLDQLSEISAWVDQYRQHWESKIDSLEKYVVQLKNERNGKQSK
>NZ_CP043450.1|WP_112574030.1|1346837_1347302_+|polyketide-cyclase
MENNQSNTANRELRLTRTLDAPIELVWEVWTQPEHIAQWWGPDGFTNTISKMEIKQEGEWDLVMHGPDGTDYKNKSVFKEIVPLKKIVYEHVSSPKFVATIEFEEQGEQTSLSWHMLFESHEQFVQVVKTFKADEGLKQNIEKLNQYLKEASKR
>NZ_CP043450.1|WP_112574029.1|1347791_1348400_+|hypothetical-protein
MKTTILTIATSLVLALGVTTAANAATKIDNGAAVVLNNVSKINKIEVRGNVEVYVSAGENENVKVYNKYYSESALVQNNNGTLRITSYKNEKLVVWVTANDLKAIDAYDNAEVKSFGKLAALDLNVNLYNNASAKLNVEAYAATVNVNDKAKAEFTGTADVYTLNHTKESFVNNNAFAAVSFTDKVTNAPAKYTVENEFAGL
>NZ_CP043450.1|WP_112574028.1|1348516_1349239_+|DUF2807-domain-containing-protein
MKNYLSTFTIAGAFISTAILSSCNYRCVHGSGNQTTEKRKAEDFKKVEISGAFKVHLKQDSSLTIDIKADDNLIKYISTSVESGTLHIKSKKNFCDPGDMVINIGVKNLEEIQAAGAVEVNSDGKLNAKDFKLDLSGATKITLDLNAANVSTEGSGATEVRLTGQAASHKIDLSGAGKIEAFDFVVGDYDIETSGIGHCKINVLKTLNVHTSGASEIQYKGSPSTVNNDKSGASSIKKVD
>NZ_CP043450.1|WP_112574027.1|1349329_1350313_+|c-type-cytochrome
MKKFLKWTAYAVIVLVLIAIAGVSYITLALPNVGQPEAIKIDATPQRIARGKYLANNVTLCMDCHSARNWSTFAAPADSAILGSGGEKFDASAGFPGTVYSPNITPLNLSNWTDGEIFRAMTTGVKKDGSAIFPIMPWPYYAKMDREDLYSIIAYLRTLKPNGKNYPGHQLDFPLNIIVHTMPQKAALGSIPNPADTIKYGAYLLNAAACKECHTQADKGKLNEAMAFAGGQGYIVPGGSKVFSANITPDKETGIGNWTKEQFVSSFTQYANGKVQPTPVKPGDFQTIMPWWKYAGMKTSDLEAIYAYLKTIKPISNHVVKFERNRN
>NZ_CP043450.1|WP_112574026.1|1350619_1351978_+|trigger-factor
MNITQEKINDLSAVVKININPEDYQPRVEKAIKENAKKAKLPGFRPGMVPAAHIKKMYGKSILVDEINNLLQDTLNNYIDEQKLAVLGQPLPALDDNKEYNWDFADNFEFSYELGLAPEFSIDFSSADKLTQYVIKIDDETLASRIKNIRRSYGKMTNPDVSADDDVLYSDLVQLSADGSVFEDGITNTASVRLDQIKDEAIKASLIGLKKGDVVTFDIRKAFDNDAAKIAGLLKIEEDDAADLRGDFQLTVKNVNRLEESDLNQEFFDKLFGEGTVTTEEEFRTKITEELESMMVQDSDRKLQDDMYKLAIAKVDFALPDEFLKRWLKATNEKLSDEELEGGYNDFAQNLKWTLIENKIITDNTIEIKYEDVFELAKIRLDQQFRMYSPTPIPEDQLGQYTVQYLQNKDNANKIFEEVKALKVFDYIKNVITLDKQDILYTDFSALVTAAQ
>NZ_CP043450.1|WP_112574025.1|1352402_1353131_+|ATP-dependent-Clp-protease-proteolytic-subunit
MSSNIDKNEFRKYAVKHHRINSLYVDKYIAGVERGNMPTGGITTVPTGMTPYILEERQLNVQAMDVFSRLMMDRIIFLGDAIYDNIANIIQAQLLFLQSADAKRDIQIYINSPGGSVYAGLGIYDTMQFISNDVATICTGMAASMAAVLLVAGTEGKRAALPHARVMIHQPSGGAQGQQSDIEITYQEITKLKKELYQIIADHSGAPYQKVWDASDRDYWMIAEEAKEFGMVDEILKGNKGK

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Crispr_ID: NZ_CP043450_4

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043450_4

1366353-1366444

Orphan

Consensus_repeat	Method
GATTGTTTTGGTTATTGTTGCGA	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043450_4

>merge|NZ_CP043450|4|1366353-1366444|CRISPRCasFinder
GATTGTTTTGGTTATTGTTGCGATTTTGGTTGTTGTTTTGCCTGCCGCCGCTGCCGCCACCACGATTTTGATTGTTTTGGTTGTTGTTGCGA

>NZ_CP043450|4|4|1366353-1366444|CRISPRCasFinder
GATTGTTTTGGTTATTGTTGCGA	TTTTGGTTGTTGTTTTGCCTGCCGCCGCTGCCGCCACCACGATTTT
GATTGTTTTGGTTGTTGTTGCGA

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043450.1\|WP_112574021.1\|1361552_1362914_+\|pyridoxal-phosphate-dependent-enzyme	unknown	unknown	gnl\|CDD\|273464
NZ_CP043450.1\|WP_112574024.1\|1353269_1354508_+\|ATP-dependent-Clp-protease-ATP-binding-subunit-ClpX	unknown	unknown	gnl\|CDD\|235422
NZ_CP043450.1\|WP_112574025.1\|1352402_1353131_+\|ATP-dependent-Clp-protease-proteolytic-subunit	unknown	unknown	gnl\|CDD\|184722
NZ_CP043450.1\|WP_112574176.1\|1367267_1368365_+\|dipeptide-epimerase	unknown	unknown	gnl\|CDD\|239435
NZ_CP043450.1\|WP_112574027.1\|1349329_1350313_+\|c-type-cytochrome	unknown	unknown	unknown
NZ_CP043450.1\|WP_112572251.1\|1375209_1375578_-\|helix-turn-helix-transcriptional-regulator	unknown	unknown	gnl\|CDD\|238045
NZ_CP043450.1\|WP_112574022.1\|1355531_1361387_-\|TonB-dependent-receptor-plug-domain-containing-protein	unknown	unknown	gnl\|CDD\|274948
NZ_CP043450.1\|WP_149301869.1\|1370839_1372075_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112572245.1\|1378896_1380054_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112574026.1\|1350619_1351978_+\|trigger-factor	unknown	unknown	gnl\|CDD\|272913
NZ_CP043450.1\|WP_112574017.1\|1369123_1370494_-\|dipeptidase	unknown	unknown	gnl\|CDD\|349929
NZ_CP043450.1\|WP_112572247.1\|1378184_1378544_-\|response-regulator	unknown	unknown	gnl\|CDD\|225114
NZ_CP043450.1\|WP_112574028.1\|1348516_1349239_+\|DUF2807-domain-containing-protein	unknown	unknown	gnl\|CDD\|371327
NZ_CP043450.1\|WP_112574020.1\|1363025_1364588_-\|glycosyltransferase-family-39-protein	unknown	unknown	gnl\|CDD\|379080
NZ_CP043450.1\|WP_112574023.1\|1354599_1355454_+\|AMP-nucleosidase	unknown	unknown	gnl\|CDD\|235940
NZ_CP043450.1\|WP_112574018.1\|1368368_1368824_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_CP043450.1\|WP_112574019.1\|1364735_1366043_-\|UDP-N-acetylglucosamine-1-carboxyvinyltransferase	unknown	unknown	gnl\|CDD\|236486
NZ_CP043450.1\|WP_146750050.1\|1374691_1374991_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112572255.1\|1373264_1374695_+\|tetratricopeptide-repeat-protein	unknown	unknown	gnl\|CDD\|276809
NZ_CP043450.1\|WP_112572249.1\|1375742_1378025_-\|AAA-family-ATPase	unknown	unknown	gnl\|CDD\|273429

Protein	Function_ID	Function_description	E-value
NZ_CP043450.1\|WP_112574021.1\|1361552_1362914_+\|pyridoxal-phosphate-dependent-enzyme	gnl\|CDD\|273464	TIGR01137, Cystathionine_beta-synthase, cystathionine beta-synthase. Members of this family closely resemble cysteine synthase but contain an additional C-terminal CBS domain. The function of any bacterial member included in this family is proposed but not proven. [Amino acid biosynthesis, Serine family].	6.45528e-169
NZ_CP043450.1\|WP_112574024.1\|1353269_1354508_+\|ATP-dependent-Clp-protease-ATP-binding-subunit-ClpX	gnl\|CDD\|235422	PRK05342, clpX, ATP-dependent Clp protease ATP-binding subunit ClpX.	0
NZ_CP043450.1\|WP_112574025.1\|1352402_1353131_+\|ATP-dependent-Clp-protease-proteolytic-subunit	gnl\|CDD\|184722	PRK14514, PRK14514, ATP-dependent Clp endopeptidase proteolytic subunit ClpP.	7.18393e-119
NZ_CP043450.1\|WP_112574176.1\|1367267_1368365_+\|dipeptide-epimerase	gnl\|CDD\|239435	cd03319, L-Ala-DL-Glu_epimerase, L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The genomic context and the substrate specificity of characterized members of this family from E.coli and B.subtilis indicates a possible role in the metabolism of the murein peptide of peptidoglycan, of which L-Ala-D-Glu is a component. L-Ala-D/L-Glu epimerase is a member of the enolase-superfamily, which is characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.	1.44244e-101
NZ_CP043450.1\|WP_112572251.1\|1375209_1375578_-\|helix-turn-helix-transcriptional-regulator	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.	4.73353e-13
NZ_CP043450.1\|WP_112574022.1\|1355531_1361387_-\|TonB-dependent-receptor-plug-domain-containing-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].	3.13662e-54
NZ_CP043450.1\|WP_112574026.1\|1350619_1351978_+\|trigger-factor	gnl\|CDD\|272913	TIGR00115, tig, trigger factor. Trigger factor is a ribosome-associated molecular chaperone and is the first chaperone to interact with nascent polypeptide. Trigger factor can bind at the same time as the signal recognition particle (SRP), but is excluded by the SRP receptor (FtsY). The central domain of trigger factor has peptidyl-prolyl cis/trans isomerase activity. This protein is found in a single copy in virtually every bacterial genome. [Protein fate, Protein folding and stabilization].	2.45584e-53
NZ_CP043450.1\|WP_112574017.1\|1369123_1370494_-\|dipeptidase	gnl\|CDD\|349929	cd05680, M20_dipept_like, uncharacterized M20 dipeptidase. Peptidase M20 family, unknown dipeptidase-like subfamily (inferred by homology to be dipeptidases). M20 dipeptidases include a large variety of bacterial enzymes including cytosolic nonspecific dipeptidase (CNDP), Xaa-methyl-His dipeptidase (anserinase),and canosinase. These dipeptidases have been shown to act on a wide range of dipeptides, but not larger peptides. For example, anserinase mainly catalyzes the hydrolysis of N-alpha-acetylhistidine while carnosinase degrades beta-alanyl-L-histidine.	0
NZ_CP043450.1\|WP_112572247.1\|1378184_1378544_-\|response-regulator	gnl\|CDD\|225114	COG2204, AtoC, Response regulator containing CheY-like receiver, AAA-type ATPase, and DNA-binding domains [Signal transduction mechanisms].	6.22626e-25
NZ_CP043450.1\|WP_112574028.1\|1348516_1349239_+\|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).	4.41187e-40
NZ_CP043450.1\|WP_112574020.1\|1363025_1364588_-\|glycosyltransferase-family-39-protein	gnl\|CDD\|379080	pfam13231, PMT_2, Dolichyl-phosphate-mannose-protein mannosyltransferase. This family contains members that are not captured by pfam02366.	1.90295e-23
NZ_CP043450.1\|WP_112574023.1\|1354599_1355454_+\|AMP-nucleosidase	gnl\|CDD\|235940	PRK07115, PRK07115, AMP nucleosidase; Provisional.	6.54756e-178
NZ_CP043450.1\|WP_112574018.1\|1368368_1368824_+\|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.	1.13375e-19
NZ_CP043450.1\|WP_112574019.1\|1364735_1366043_-\|UDP-N-acetylglucosamine-1-carboxyvinyltransferase	gnl\|CDD\|236486	PRK09369, PRK09369, UDP-N-acetylglucosamine 1-carboxyvinyltransferase; Validated.	0
NZ_CP043450.1\|WP_112572255.1\|1373264_1374695_+\|tetratricopeptide-repeat-protein	gnl\|CDD\|276809	sd00006, TPR, Tetratricopeptide repeat. The Tetratricopeptide repeat (TPR) typically contains 34 amino acids and is found in a variety of organisms including bacteria, cyanobacteria, yeast, fungi, plants, and humans. It is present in a variety of proteins including those involved in chaperone, cell-cycle, transcription, and protein transport complexes. The number of TPR motifs varies among proteins. Those containing 5-6 tandem repeats generate a right-handed helical structure with an amphipathic channel that is thought to accommodate an alpha-helix of a target protein. It has been proposed that TPR proteins preferentially interact with WD-40 repeat proteins, but in many instances several TPR-proteins seem to aggregate to multi-protein complexes.	2.33555e-08
NZ_CP043450.1\|WP_112572249.1\|1375742_1378025_-\|AAA-family-ATPase	gnl\|CDD\|273429	TIGR01073, ATP-dependent_DNA_helicase_PcrA, ATP-dependent DNA helicase PcrA. Designed to identify pcrA members of the uvrD/rep subfamily. [DNA metabolism, DNA replication, recombination, and repair].	0

>NZ_CP043450.1|WP_112574019.1|1364735_1366043_-|UDP-N-acetylglucosamine-1-carboxyvinyltransferase
MTNAFVINGGKPLKGEITPQGAKNEALQVISAVLLTEEKVTISNIPDIKDVNKLIELLGDMGVIVERVNEHTYTFEAKDINQDFFLSEAFKSKGGGLRGSIMIVGPLLARFGKASIPKPGGDKIGRRRLDTHFLGFEKLGAQFNYNPENGFFNVDASNLQGTYILLDEASVTGTANVVMAAVLAKGTTTIYNAACEPYLQQLCKMLSRMGAKISGIGSNLLTIEGVERLGGTEHRLLPDMIEIGSFIGLAAMTGSEITIKDVQYKELGMIPDVFKRLGIKLELRGDDIFIPAQEHYEIETFIDGSIMTIADAPWPGFTPDLLSIVLVVAIQAKGSVLIHQKMFESRLFFVDKLLDMGAQIILCDPHRATVIGLDNQVKLRGISMTSPDIRAGVSLLIAALSAQGQSTIYNIEQIERGYQHIDTRLKALGADITRI
>NZ_CP043450.1|WP_112574020.1|1363025_1364588_-|glycosyltransferase-family-39-protein
MPYKNRKSTYVYFVLIFVFIKVVLNLFAISHFGFHRDEFLHLVLADHLDWGYKEVPPFIAILAKISITCFGNSVFAARLFPTLFGGLIVLLTGLIVIEFGGKKFAITLACLSLIFAPAFAASEYLFQPVVFDQFWWVLTVWLLVKYLNTTDVRYLYWLGAAVGLGILTKYTMLFFAASLLIGILISKQRKLLFNKHILGAVMITVAIVLPNLIWQINHHMPVFTHMKNLREQQLDYITPTDFIKQQLLVNGVALFIWLNGLAFLIFSFRLRNFQFMALAYALIFFFLLMMDGKSYYIFGAYPMLFAAGAFGFERLLKTNGYVLRTALIVLFTLPNALLLPILLPILPMDQTLAFFRFADKHLPPVRFSMIWEDGKKHATTQDYADMLGWDDMAALVDKAYKSLSPDDQKQTLVYADNYGEAGAIHHYRKQYGYPNVISLNSSFTLWAPDSLKCKYLIYIDDGGGKNIKEFVAGNMIGSFTKVGEVSNPLAREKGTAVFIITPNYRLNQRYSPELAKKRLE
>NZ_CP043450.1|WP_112574021.1|1361552_1362914_+|pyridoxal-phosphate-dependent-enzyme
MWYSNILDTIGNTPLVKLNKVAKDIPATVLAKIETTNPGNSIKDRMALKMIEDAEKSGKLKPGGTIIEGTSGNTGMGLAIAAVIKGYKCIFTSTDKQSKEKFDALRAFGAEVIVCPTNVEPEDPRSYYSVSSRLEREVPNSWKPNQYDNLSNSQAHYESTGPEIWEQTEGKITHLIAGVGTGGTISGIARYLKEKNPAIQVLGIDTYGSVFKKYKETGVFDKNEIYPYITEGIGEDFLPQNVDFSLIDHFEKVTDKDAALMTREIARKEGIFSGNSTGSAVAGLLQMKDKFKEGDVVVIIFPDHGTRYLGKMYNDDWLRDRGFLKDEKLTARDIISKKDVQEIITIDCEKSVLEAINTIKSLNISQIPVTQKGMVIGKITESDILDSLIENPSIKSQPIKNITTAPFPFVDLNTSIDRISAMINKDNIAVLVEGEQGKIEIITQYDIINAISA
>NZ_CP043450.1|WP_112574022.1|1355531_1361387_-|TonB-dependent-receptor-plug-domain-containing-protein
MQATLKRSFLFFSFLSFCITTTFAQNVLTPSRQNSFYTYIYKVTADDVLKFYQHPDKKPDEQILRNPIDSFKTNTKWDNTLPPGNYMQVVAKKNLLSYSLIENHSANLKLLDNRYDLRFILLDNEGKIINNALVQTNNHTIAYDTKAGLYIADASKKGTILKVDYAGVTNYYNIKKQEKPSYYRYNPYRGMSFFKATWNRFKNLFKKGNKPHYRPLPGHDYEGFMVFNKAIYKPRDTVKFKAFILNKKSKKPINAAQLLIRLRYRNDEDGKIIGRVKSYRDGAYEYSFALTDSLDLSLDRDYTISLEDPSSEKYKLDDYKGDDDEGFLAKRKVYMTGEFKYEEYELKSITFSTRVDKEEHNPGNPATLYLKAVDENNLPVTDGRVNITLYTRNTGTHRQNYTFVPDQLWTHQLQLDAIGETKLIIPDSIFPKADVTYYINSEFLNSNNERQSANNNMSYRYNRFRVTAKLSGDTLVSEAFDNGEPIKTMATISTLNPRYDTISKIKVMLPSKTIINPYADNYNIQTDSTYADLYLKNNDSGISLSGYRTADSLFVKVENPRHLHFWYSVFGGNRLIDAGQADNLFYTRAYNDQNMVNFQVHCIWVGESRTEATDIVYRDKLMTINVRQPVSVYPGQQAKTDIVVTDAKGQPVANADLTAWSMTSKFTNYRTPYVPYLGKDFTYRKQKAAFEANGFNIIGTLQLNWKRWSKEMGLDSIAYYQFTHPDKIYQVEEDTKDSLTQVAPFVVKNGDVLPVHILYIDNRPVYFDQTRQLKRYSFAVSPGKHSFRFRTSHQNVWVDTIDVPKSKKLIFSINADSAKFTKVSDTLSTYECDLINRYLITIINNFGWKMALLTQSEKVFMINADPGQYNSVLVGPLAENFANLEVKGSGSRYFATEPGYSFQFEQGLIKQKSIATAYPFNPVLSSYQGTADDYTQEVLTRPDAENVWQQYLDLRSNTQALFNNPTISGEIGKLSMNITQPEDKKLLIKNIIIYKYNDPDFIMIYPGNTTYVSGLNAGRYRVLFLLKGDNYDIKENVVIKIQGTNFYNFTVLPAHAKDSVGTRISNIINNRTGAYTNGDREIENDALKIKEAFNDKYLDSGSFADTMSGIISGNDNQPAAGVSIRVRGAATGTFTDANGRFKIKVPKNGRLIISYIGYETQQVPIHPGETLRLALTSSSKLLQEVVVVGYGTVMRRELTGSVSTATYGLAGQVPGVSVNDGSPNLKVMIRGVSSLPSAPPLVVVDGEIVASLSDINKDDIAELSILKEAAATAIYGARAANGVIVIKTKAKPGLAGGQKTDTTQTGGTSTLRKNFSDYAYWQPKLTTDEHGKASFMVTYPDDITNWRTFIIGINGNKQTGFAESNIKSYKPLSANFIAPQFAVAGDEMNLIGKVMNYNTNTAKLTRVFKYNGQTLKQDELEIKNSKIDTLSITATSTDSLTFEYTIKRDNGYFDGEQRKIPVMPQGVKETKGIFEALDRDTTVSLKFDPALGPITFRAEASALPVLAEETRKLREYKYLCNEQLASKLKGLLMERRIKKFMGEDFKYEKNIREVIKKMQENRRGNGTWGWWKDSNEELWISLHAIEALVNAQKEGFVVELDKQKLTDYLVYQLESYKDRDKILCLQLLHKLEAKVDYQKYVAIIEKKQAKAREPFGGGLLVYDKLRLMLLRQESGLPIKMDSLLKPSKRTMFGNMYWGEDDYRFFDNSIQLSILAYHIIKNEGSHPELLSKIRGYFLEQRRHGDWRNTYESALILETILPDLLIENKQVKPSEITLNGSDTKTISKFPYSATLTDKQISVNKTGSLPVYITGYQQFWNSKPEKVSKDFTVDTWFERKEKTVTTLKGGEPVLLKAEVTVRGDADFVMVEIPIPAGCSYESKDQAWQNNEVHREYFKEKVSIFCRSLKQGKYTFSINLIPRYNGKYTLNPAKAEMMYFPVFYGREGMKQVVVD
>NZ_CP043450.1|WP_112574023.1|1354599_1355454_+|AMP-nucleosidase
MNEELDVKKDGDNVQKVKEVHTPIKSGLKTKEAIVANWLPRYTGRPLEAFGEYIILTNFSKYIQLFSQWNDNAPIMGLEKPMQSVTANGITIINFGMGSSVAATVMDLLTAIHPKAVIFLGKCGGLKKKNNVGDLILPIAAIRGEGTSNDYLPPEVPALPSFALQKAISTTIRDYSRDYWTGTCYTTNRRVWEHDKNFKKYLKDLRAMAVDMETATIFTTGFANKIPTGALLLVSDQPMIPEGVKTAESDSSVTEQFVETHLHIGIESLKQLINNGLTVKHLKF
>NZ_CP043450.1|WP_112574024.1|1353269_1354508_+|ATP-dependent-Clp-protease-ATP-binding-subunit-ClpX
MNKNSKEIRCSFCGAGKQDSLMLIAGLDAHICDKCVNQANEILAEELKVRKVKSSPLAPALLKPSEMKAHLDQYVIGQDDAKKILSVAVYNHYKRLNQRVDKDEVEIEKSNIIMVGETGTGKTLLAKTLAKVLNVPFCICDATVLTEAGYVGEDVESILTRLLQSADYDVTLAEKGIVYIDEVDKIARKSDNASITRDVSGEGVQQALLKILEGTMVNVPPQGGRKHPDQKMITVNTSNILFICGGAFDGIERKIANRLRTQTVGYKLKRDEGDIDTKNFYKYITPQDLKSFGLIPELIGRLPVLTYLNPLDREALHNILTEPKNSLLKQYKKLFEYEGVKLDFEDEVLDFIVDKAMEFKLGARGLRSICEAIMIDAMFEFPSKKDVKRLNVTLDYAHEKFEKSDLKKLKVA
>NZ_CP043450.1|WP_112574025.1|1352402_1353131_+|ATP-dependent-Clp-protease-proteolytic-subunit
MSSNIDKNEFRKYAVKHHRINSLYVDKYIAGVERGNMPTGGITTVPTGMTPYILEERQLNVQAMDVFSRLMMDRIIFLGDAIYDNIANIIQAQLLFLQSADAKRDIQIYINSPGGSVYAGLGIYDTMQFISNDVATICTGMAASMAAVLLVAGTEGKRAALPHARVMIHQPSGGAQGQQSDIEITYQEITKLKKELYQIIADHSGAPYQKVWDASDRDYWMIAEEAKEFGMVDEILKGNKGK
>NZ_CP043450.1|WP_112574026.1|1350619_1351978_+|trigger-factor
MNITQEKINDLSAVVKININPEDYQPRVEKAIKENAKKAKLPGFRPGMVPAAHIKKMYGKSILVDEINNLLQDTLNNYIDEQKLAVLGQPLPALDDNKEYNWDFADNFEFSYELGLAPEFSIDFSSADKLTQYVIKIDDETLASRIKNIRRSYGKMTNPDVSADDDVLYSDLVQLSADGSVFEDGITNTASVRLDQIKDEAIKASLIGLKKGDVVTFDIRKAFDNDAAKIAGLLKIEEDDAADLRGDFQLTVKNVNRLEESDLNQEFFDKLFGEGTVTTEEEFRTKITEELESMMVQDSDRKLQDDMYKLAIAKVDFALPDEFLKRWLKATNEKLSDEELEGGYNDFAQNLKWTLIENKIITDNTIEIKYEDVFELAKIRLDQQFRMYSPTPIPEDQLGQYTVQYLQNKDNANKIFEEVKALKVFDYIKNVITLDKQDILYTDFSALVTAAQ
>NZ_CP043450.1|WP_112574027.1|1349329_1350313_+|c-type-cytochrome
MKKFLKWTAYAVIVLVLIAIAGVSYITLALPNVGQPEAIKIDATPQRIARGKYLANNVTLCMDCHSARNWSTFAAPADSAILGSGGEKFDASAGFPGTVYSPNITPLNLSNWTDGEIFRAMTTGVKKDGSAIFPIMPWPYYAKMDREDLYSIIAYLRTLKPNGKNYPGHQLDFPLNIIVHTMPQKAALGSIPNPADTIKYGAYLLNAAACKECHTQADKGKLNEAMAFAGGQGYIVPGGSKVFSANITPDKETGIGNWTKEQFVSSFTQYANGKVQPTPVKPGDFQTIMPWWKYAGMKTSDLEAIYAYLKTIKPISNHVVKFERNRN
>NZ_CP043450.1|WP_112574028.1|1348516_1349239_+|DUF2807-domain-containing-protein
MKNYLSTFTIAGAFISTAILSSCNYRCVHGSGNQTTEKRKAEDFKKVEISGAFKVHLKQDSSLTIDIKADDNLIKYISTSVESGTLHIKSKKNFCDPGDMVINIGVKNLEEIQAAGAVEVNSDGKLNAKDFKLDLSGATKITLDLNAANVSTEGSGATEVRLTGQAASHKIDLSGAGKIEAFDFVVGDYDIETSGIGHCKINVLKTLNVHTSGASEIQYKGSPSTVNNDKSGASSIKKVD
>NZ_CP043450.1|WP_112574176.1|1367267_1368365_+|dipeptide-epimerase
MTITHIDIYRFSIPMEPFTIATGTLAHAQNVFIRIHTDAGFYGVGECSAFPMIVGETQDTCLVMAREFARLWKGKDALDIEARLQELHSFTAGNTTIKSAFDNALFDIAAKNADMPLYQFLGGEKRTVESDITIGIAGHHTMALKALDFKASGANILKVKLGKNVIEDVERVQQIREAVGPAMKIRIDANQGWSFNEAVFALQSIAQYDIEFCEQPIRTWYDDRLPELMQLSPVKIMADESVYNHHDARKQINAGACHYINIKMAKSGGIYEAKRIHDVAASYGIPCMMGGMLESRIALSAKLHFVYASPNIRFYDMDTCKLGHLVDPCVGGAMYDGYHLTIDDAPGIGADADEAFLADCERFTI
>NZ_CP043450.1|WP_112574018.1|1368368_1368824_+|GNAT-family-N-acetyltransferase
MLIRKATIEDLPVLLQFEQGIISTERPFDSTLKPDPISYYDLKAFISSSEVEVLVAEIDGEIAGSGYARIKKNPDSYYDFEKYAYLGFMYVLPPHRGKGINQAIIEELKKWVAEQGLAEIRLEVYNDNTGAIKAYEKVGFEKRMIEMRIRI
>NZ_CP043450.1|WP_112574017.1|1369123_1370494_-|dipeptidase
MQHIKQYVEQNKQRLLDELFDLLRLASVSADPKYKPEVLKTADYVAARLRDAGADNVEICQTAGYPIVYGEKIIDPSKPTVLVYGHYDVQPPDPLELWKTPPFEPTVRDGKIYARGACDDKGQFYMHVKAFELMMQTNTLPCNIKFMIEGEEEVGSSNLGIFVKANKEKLKADVVLISDTSMISMEHPSLETGLRGLSYLEVEVTGPNRDLHSGVYGGAVANPITILAQMIATLHDENNHITIPGFYNDVVPLTEAERAALNSAPYDEAEYKKDLDVTELWGEKGYSTFERTGTRPTLELNGIWGGYIGEGAKTVLPSKANAKISMRLVPNQTSEAITKLFTDHFLSIAPPYVKVKVTPHHGGEPAVTPTDSVAYRAAQKAIAESFGKEPIPTRGGGSIPIVALFEAELGLKTVLMGFGLDSDALHSPNEKYDIYNYYKGIETIPLFHKYFAELSE
>NZ_CP043450.1|WP_149301869.1|1370839_1372075_-|hypothetical-protein
MKNLTLIATLALSTILSTATIANAANGPQPKRDLGSADARGPQPKRDLGSADFARGPQPKRDLGSADFARGPQPKRDLGSADFAQSGPGPKRDLGSADFAQSGPGPKRDLGSADFAQSGPGPKRDLGSADFAQSGPGPKRDLGSADFAQSGPGPKRDLGSADFAQSGPGPKRDLGSADFAQSGPGPKRDLGSADFAFGPQPKRDLGSADFAQSGPGPKRDLGSADFAQSGPGPKRDLGSADFAQSGPGPKRDLGSADFAFGPQPKRDLGSADFAFGPQPKRDLGSADFAFGPQPKRDLGSADFAFGPQPKRDLGSADFAFGPQPKRDLGSADFAFGPQPKRDLGSADFAFGPQPKRDLGSADFAFGPQPKRDLGSADFAFGPQPKRDLGSADFAQSGPGPKRDLGSADFMA
>NZ_CP043450.1|WP_112572255.1|1373264_1374695_+|tetratricopeptide-repeat-protein
MKRIGTFILFILLSLTVYANDINDVAATDTNEVISINANAYKNRLTNPEQTVQDANKALKLSTKLNYINGIAEAYRVIGIGKYYLDQPEKAIENYLNSLSYFTRNNNLKGEASVYNNIGILFRDHDYERSLDYLNKGLEIAQKINDAKLLGSLYLNIGNVYTRKNNLYMALKFYDKSFPIFQKRKDSINMIQCLQNRGVIYFKLKDYDKALSLLLEANTGAKAGDLNESVASVDLTLAALYMAKGDFKNAEKMVQEGTAYTQLVKDPKLDYDYKYTTYELEYNKKNYARAVNLLREIYTQDSTTYKTNVSAQMNLVEAKRRQEEQLKENERIAERQAYDRSKFWAVTVVAGLLLVVIGLLISNVKRKAKTNAQLTLLNGEVSRQKDNLDRINHHLEEIIDERTKDLQLKNKKLSEHSSYLSHQIRGPIATLRGLINLEKEGLVDQAECLDMMDKCVSEIDEKIIEMSDMLHNPPRV
>NZ_CP043450.1|WP_146750050.1|1374691_1374991_-|hypothetical-protein
MSNYLISISKNENLSDGIIHDPKSKLKVKAFDLLKARFKPSKGEVRFFVTSASETLAFETQGYNQHRQLLVLQMISWYCIYLGLIEAQIHSNLPVHFAY
>NZ_CP043450.1|WP_112572251.1|1375209_1375578_-|helix-turn-helix-transcriptional-regulator
MSDTVKKKTNKSVGKNIRTLRHQHGWSQEDVANRLGISIPAFSKIETGVTDINLSRLEQIANIFDVNVVHLLALDSEEVDTKPSSLSVAQKKLIDRESEIANLQRKVILLYEELRNKAVVAM
>NZ_CP043450.1|WP_112572249.1|1375742_1378025_-|AAA-family-ATPase
MDYLQGLNPEQRAAVEQTEGPVMIIAGAGSGKTRVITYRVAHLIRKGVDSFNILVLTFTNKAAREMRERITHVVGTEAKNIWMGTFHSVFAKILRVEAEKIGYPSNFTIYDTDDSKSVLRAILKEMNLDDKLYNVNFVLNRISASKNNLISWQEYNKNEQIQADDFSSGRGQMGKIYEMYATRCYRAGAMDFDDLLYKTNELLKLHPDVLNKYQHKFKYLMVDEYQDTNFSQYLIVKKLAAVNENLCVVGDDAQSIYAFRGANIQNILNFEKDYPDLKVFKLEQNYRSTQNIVNVANSIIRNNKDQLKKNVFSEKESGDKIKVMRAFSDNEEGKIVAEAIMQDRSSNGLKWSAFAILYRTNAQSRSMEEALRKLGIPYKIYGGLSFYQRKEIKDLIAYFRLTFNPNDEEALKRVINYPKRGIGDTSVDKIIVAADQHGITPWEVIVEPGKYLEGKISGAVANFATMIQSFQVLAKTKSAYESALYVAQHSGLLKDLYEDKSVEGLNRYENIQELLNGIKEFSEREDIEEKGLDIFMQDVALLTNDDKDKNKDADTVSLMTIHSSKGLEFPQVYVVGLEENLFPSQMSLNSRSDLEEERRLFYVAVTRAESKLHISYATSRFKFGTLINCEPSRFLDEIDAKFLELDYTAKPSSASNPFDDERKAWSRDKQPDSFSRPKPAAAAPVKTTSILTKAHVPSANFKPSDTSNLQVGMEVEHERFGFGKVISLEGNKPDIKATIFFKEIGQKQLLLKFAKLYILQ
>NZ_CP043450.1|WP_112572247.1|1378184_1378544_-|response-regulator
MAKNILIIEDDAEILRVLETVLTFHDFEVTGLNRTDDIIAAVKNYNPDLVLTDYMLPGLNGGRICQLIKSNEDTRHIPVILISAYHEQAIALVNFGYDAFVPKPFDVNKLVKTINKFLN
>NZ_CP043450.1|WP_112572245.1|1378896_1380054_+|hypothetical-protein
MKTKFRPGRLMLLMFFIVVANRSIAQSADKSEGDNSVIMPRNDADTLGNNATAFMPPADPLKNAGIIYDEDNADNQIKNGALKIASKKYSKLYAAGKLDELMIENRFGEVKINTWNRSEFSVEVQVNIYADKQTDAQGFLNAINISDSRREALVSFKTIIGDNGINNGNVLWKGEDKPRIKKIEINYIVFMPVKNALSIINNYGTTILPDFEGKLMLNSLYSNLKAKRLINPLNYVKVNFGDVDIEGFSGTRLEVLHGSLDLNEGSNFSVSVSYGPARIGKIYSSATIDARFGKQFRIEDIDKNIKTLHVNAAYTSVQVGRITGVNANCDVSTYYGTLNNSDPQITLTSDKSPDNQEKSYKGRLGKGDANRNIVIKTNFGRVNFD

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Crispr_ID: NZ_CP043450_5

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043450_5

2510451-2510542

Orphan

Consensus_repeat	Method
GACAGGTTCGATATGGATAACCAGGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043450_5

>merge|NZ_CP043450|5|2510451-2510542|CRISPRCasFinder
GACAGGTTCGATATGGATAACCAGGGAAAGATAAAATCTATAGGACAAACCCGGTTTACGTATTACGACAGGTTTGATATGGATAACCAGGG

>NZ_CP043450|5|5|2510451-2510542|CRISPRCasFinder
GACAGGTTCGATATGGATAACCAGGG	AAAGATAAAATCTATAGGACAAACCCGGTTTACGTATTAC
GACAGGTTTGATATGGATAACCAGGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043450.1\|WP_112566821.1\|2514235_2515114_-\|DMT-family-transporter	unknown	unknown	gnl\|CDD\|284268
NZ_CP043450.1\|WP_112566828.1\|2512163_2513519_-\|magnesium-transporter	unknown	unknown	gnl\|CDD\|225148
NZ_CP043450.1\|WP_112566804.1\|2520174_2520969_+\|PASTA-domain-containing-protein	unknown	unknown	gnl\|CDD\|275384
NZ_CP043450.1\|WP_112566809.1\|2518179_2518815_-\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224054
NZ_CP043450.1\|WP_112566862.1\|2496692_2497991_+\|DEAD/DEAH-box-helicase	unknown	unknown	gnl\|CDD\|223587
NZ_CP043450.1\|WP_112566859.1\|2498063_2498276_-\|DUF2132-domain-containing-protein	unknown	unknown	gnl\|CDD\|378300
NZ_CP043450.1\|WP_112566837.1\|2509531_2510023_+\|YajQ-family-cyclic-di-GMP-binding-protein	unknown	unknown	gnl\|CDD\|377366
NZ_CP043450.1\|WP_112566812.1\|2517070_2518180_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112566831.1\|2511004_2512012_-\|biotin-synthase-BioB	unknown	unknown	gnl\|CDD\|215219
NZ_CP043450.1\|WP_112566847.1\|2505130_2505628_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112566818.1\|2515114_2516170_-\|bifunctional-diaminohydroxyphosphoribosylaminopyrimidine-deaminase/5-amino-6-(5-phosphoribosylamino)uracil-reductase-RibD	unknown	unknown	gnl\|CDD\|273015
NZ_CP043450.1\|WP_112566989.1\|2505674_2506241_-\|UbiX-family-flavin-prenyltransferase	unknown	unknown	gnl\|CDD\|223241
NZ_CP043450.1\|WP_112566853.1\|2502749_2503280_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112566843.1\|2506411_2507290_-\|exopolyphosphatase	unknown	unknown	gnl\|CDD\|274735
NZ_CP043450.1\|WP_112566840.1\|2507292_2509338_-\|polyphosphate-kinase-1	unknown	unknown	gnl\|CDD\|235469
NZ_CP043450.1\|WP_112566850.1\|2503583_2505083_+\|malate:quinone-oxidoreductase	unknown	unknown	gnl\|CDD\|377591
NZ_CP043450.1\|WP_112566815.1\|2516203_2517067_+\|peptide-chain-release-factor-N(5)-glutamine-methyltransferase	unknown	unknown	gnl\|CDD\|236467
NZ_CP043450.1\|WP_112566825.1\|2513611_2514226_-\|YigZ-family-protein	unknown	unknown	gnl\|CDD\|376491
NZ_CP043450.1\|WP_112566856.1\|2498450_2502746_+\|response-regulator	unknown	unknown	gnl\|CDD\|236848
NZ_CP043450.1\|WP_112566806.1\|2518929_2519919_-\|D-alanine--D-alanine-ligase	unknown	unknown	gnl\|CDD\|234993

Protein	Function_ID	Function_description	E-value
NZ_CP043450.1\|WP_112566821.1\|2514235_2515114_-\|DMT-family-transporter	gnl\|CDD\|284268	pfam06800, Sugar_transport, Sugar transport protein. This is a family of bacterial sugar transporters approximately 300 residues long. Members include glucose uptake proteins, ribose transport proteins, and several putative and hypothetical membrane proteins probably involved in sugar transport across bacterial membranes. These members are transmembrane proteins which are usually 5+5 duplications. This model recognizes a set of five TMs,.	0.00974409
NZ_CP043450.1\|WP_112566809.1\|2518179_2518815_-\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224054	COG1131, CcmA, ABC-type multidrug transport system, ATPase component [Defense mechanisms].	7.85368e-39
NZ_CP043450.1\|WP_112566862.1\|2496692_2497991_+\|DEAD/DEAH-box-helicase	gnl\|CDD\|223587	COG0513, SrmB, Superfamily II DNA and RNA helicases [DNA replication, recombination, and repair / Transcription / Translation, ribosomal structure and biogenesis].	1.2285e-47
NZ_CP043450.1\|WP_112566840.1\|2507292_2509338_-\|polyphosphate-kinase-1	gnl\|CDD\|235469	PRK05443, PRK05443, polyphosphate kinase; Provisional.	0
NZ_CP043450.1\|WP_112566828.1\|2512163_2513519_-\|magnesium-transporter	gnl\|CDD\|225148	COG2239, MgtE, Mg/Co/Ni transporter MgtE (contains CBS domain) [Inorganic ion transport and metabolism].	5.52706e-123
NZ_CP043450.1\|WP_112566804.1\|2520174_2520969_+\|PASTA-domain-containing-protein	gnl\|CDD\|275384	sd00037, PASTA, PASTA domain. PASTA domain is found at the C-termini of several penicillin-binding proteins (PBPs) and bacterial serine/threonine kinases. It is a small globular domain consisting of 3 beta-sheets and an alpha-helix. The name PASTA is derived from PBP and Serine/Threonine kinase Associated domain.	1.26655e-24
NZ_CP043450.1\|WP_112566831.1\|2511004_2512012_-\|biotin-synthase-BioB	gnl\|CDD\|215219	PLN02389, PLN02389, biotin synthase.	5.15995e-179
NZ_CP043450.1\|WP_112566815.1\|2516203_2517067_+\|peptide-chain-release-factor-N(5)-glutamine-methyltransferase	gnl\|CDD\|236467	PRK09328, PRK09328, N5-glutamine S-adenosyl-L-methionine-dependent methyltransferase; Provisional.	3.47009e-96
NZ_CP043450.1\|WP_112566818.1\|2515114_2516170_-\|bifunctional-diaminohydroxyphosphoribosylaminopyrimidine-deaminase/5-amino-6-(5-phosphoribosylamino)uracil-reductase-RibD	gnl\|CDD\|273015	TIGR00326, eubact_ribD, riboflavin biosynthesis protein RibD. This model describes the ribD protein as found in Escherichia coli. The N-terminal domain includes the conserved zinc-binding site region captured in the model dCMP_cyt_deam and shared by proteins such as cytosine deaminase, mammalian apolipoprotein B mRNA editing protein, blasticidin-S deaminase, and Bacillus subtilis competence protein comEB. The C-terminal domain is homologous to the full length of yeast HTP reductase, a protein required for riboflavin biosynthesis. A number of archaeal proteins believed related to riboflavin biosynthesis contain only this C-terminal domain and are not found as full-length matches to this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Riboflavin, FMN, and FAD].	1.92157e-95
NZ_CP043450.1\|WP_112566989.1\|2505674_2506241_-\|UbiX-family-flavin-prenyltransferase	gnl\|CDD\|223241	COG0163, UbiX family flavin prenyltransferase [Coenzyme transport and metabolism].	8.9011e-82
NZ_CP043450.1\|WP_112566843.1\|2506411_2507290_-\|exopolyphosphatase	gnl\|CDD\|274735	TIGR03706, exo_poly_only, exopolyphosphatase. It appears that a single enzyme may act as both exopolyphosphatase (Ppx) and guanosine pentaphosphate phosphohydrolase (GppA) in a number of species. Members of the seed alignment use to define this exception-level model are encoded adjacent to a polyphosphate kinase 1 gene, and the trusted cutoff is set high enough (425) that no genome has a second hit. Therefore all members may be presumed to at least share exopolyphospatase activity, and may lack GppA activity. GppA acts in the stringent response. [Central intermediary metabolism, Phosphorus compounds].	1.74948e-66
NZ_CP043450.1\|WP_112566837.1\|2509531_2510023_+\|YajQ-family-cyclic-di-GMP-binding-protein	gnl\|CDD\|377366	pfam04461, DUF520, Protein of unknown function (DUF520). Family of uncharacterized proteins.	3.25884e-81
NZ_CP043450.1\|WP_112566850.1\|2503583_2505083_+\|malate:quinone-oxidoreductase	gnl\|CDD\|377591	pfam06039, Mqo, Malate:quinone oxidoreductase (Mqo). This family consists of several bacterial Malate:quinone oxidoreductase (Mqo) proteins (EC:1.1.99.16). Mqo takes part in the citric acid cycle. It oxidizes L-malate to oxaloacetate and donates electrons to ubiquinone-1 and other artificial acceptors or, via the electron transfer chain, to oxygen. NAD is not an acceptor and the natural direct acceptor for the enzyme is most likely a quinone. The enzyme is therefore called malate:quinone oxidoreductase, abbreviated to Mqo. Mqo is a peripheral membrane protein and can be released from the membrane by addition of chelators.	0
NZ_CP043450.1\|WP_112566859.1\|2498063_2498276_-\|DUF2132-domain-containing-protein	gnl\|CDD\|378300	pfam09905, VF530, DNA-binding protein VF530. VF530 contains a unique four-helix motif that shows some similarity to the C-terminal double-stranded DNA (dsDNA) binding domain of RecA, as well as other nucleic acid binding domains.	9.79525e-45
NZ_CP043450.1\|WP_112566825.1\|2513611_2514226_-\|YigZ-family-protein	gnl\|CDD\|376491	pfam01205, UPF0029, Uncharacterized protein family UPF0029.	1.74321e-52
NZ_CP043450.1\|WP_112566856.1\|2498450_2502746_+\|response-regulator	gnl\|CDD\|236848	PRK11107, PRK11107, hybrid sensory histidine kinase BarA; Provisional.	8.70515e-131
NZ_CP043450.1\|WP_112566806.1\|2518929_2519919_-\|D-alanine--D-alanine-ligase	gnl\|CDD\|234993	PRK01966, ddl, D-alanine--D-alanine ligase.	5.95392e-122

>NZ_CP043450.1|WP_112566837.1|2509531_2510023_+|YajQ-family-cyclic-di-GMP-binding-protein
MPTFDIVSKIDGQTLDNAINTAKKEILNRYDFNDSKSTIDLDKKTNEVTIVTENDMRLKAIQDSIISRMVKQHLDPKALDFGKEQYASGNMIRKEIKIKEGIDKEAAKKIVKKIKDSGLKVQASIMDDQVRVQGKKIDDLQAVISLCRADDFGQPLQYINMRD
>NZ_CP043450.1|WP_112566840.1|2507292_2509338_-|polyphosphate-kinase-1
MDKQAPLINREISWLYFNDRVLQEAADPTVPLIDRIRFLAIFSSNLDEFYRVRVATLSRLAALNEKSKEILGYNPKKVLNQIKNIVVRQERKFNNLYENIIVKQLAEEKIFILNDKQLNVTRGTFVKNYFREKLLATLVPIMLNDTLPLPELRDRAVYFFVKLTTNKKTRFALIEFPDNLSRFVKLPDTNNLKFIILLDDIIRYSLEDIFFIFEHDSIEAYSIQLTRDAELDLDKEVSEKFVDSLAKSLQKRKKGKPMRLLYDSDMPMDMLKYLVNKMGLHGESLIPGNRYHNFKNFISFPNVGGPELEYSKYIPLPVSDLSFGKSLIDLIAKKDYLVSTPYQSYDYVIHFLREAAIDPKVKEINISVYRLAENSRVIHALINAAKNGKKVNCLVELRARFDEQNNIHWSNRLEEEGVTVLYGVPGYKVHSKICLVSRTEKGKLAYYACLSTGNFNEKTAQIYADHTLLTANKKITDDLVNVFKAINRGQLAKGLKSLIVSPIDSRPAIYRLIDNEIKNAKAGKQAYMILKMNSLADEDMINKLYQASNAGVKIKMIIRGMCCLIAGVKGYSENIEVISIVDKYLEHARVHIYCNGGKELIYLTSADFMSRNIDNRVEVGFPIYDEKLQKEIRDIIDIQLSDNTKAREINSQNTNKYHKTNSPESHRAQIEIYNYLKNKTK
>NZ_CP043450.1|WP_112566843.1|2506411_2507290_-|exopolyphosphatase
MRYAAIDIGSNAVRLLIADIIQNTGSVSFKKNTLIRVPLRLGDDAFIQQHISEKKTTELVKSMVAFRNLMDVYKVTDYLACATSAMREAKNGEEVVKLIKDEANIDIDIIHGSKEASIIYASHAEQNIDKSKNYLYIDVGGGSTELSLFSAGELIVSRSFNIGTIRILDNQDTEETWNEMKDFVRDNTRNFKQLSGIGTGGNINKLFRLSEEKEDMPLTFAKLRSLYTYLSSFSLKDRINVLGLNQDRADVIIPACEIYLTLMKNANIKNIYVPRVGLVDGIIQTLIEKNLQ
>NZ_CP043450.1|WP_112566989.1|2505674_2506241_-|UbiX-family-flavin-prenyltransferase
MMKKKIVVAVTGASGSIYASLLLKKLNELRHQIAEVGVVMSDNAKDVWKFELDNEDYTQLPFKFYAKNDFMAPFASGSAKFDTMVVVPCSMGTLGRIAGGISDDLITRAADVVLKERRKLILVARDTPLNLIHIRNMATVTEAGGIICPAIPSYYSKPQTIEELAMTVVNRVIDLIGLESKSYEWKGM
>NZ_CP043450.1|WP_112566847.1|2505130_2505628_-|hypothetical-protein
MNLKYIFPAIIGFILISGNGFAQVNKASVKQLAFMAGTWTQKHEWGDMEEFWGEPMGESMISSFRVVKDGKAVFYEFVVVEEQNGVPVFKMRHFNHGSIGWEDKNKPLLFYLTKIQKNKAEFELKDKSVHITYQLTAPDKLDVTVTEKDKKGKWQKDVFNYIRKK
>NZ_CP043450.1|WP_112566850.1|2503583_2505083_+|malate:quinone-oxidoreductase
MTNNGTGSNLTVDVVLIGAGIMSATLGVMLKELQPDLTIEIFERLDVIAAESSAPMNNAGTGHSAFCELNYTPQLPDGSVEIKKAIKIAEQFETSKEFWAHLIGKGLIKDPQNFIRKVPHMSFVWGAENVEYLKKRQQALVKHHFFKGMEYSEDKAQIKKWIPLVMEGRDVDEKVSATFMDIGTDVNFGSLTSALIDELKQKADVNVSLNHDVKDLKRNADGTWKVTVKDKATGNKRKLNAKFVFVGAGGGALHLLQKSGIAESKGFGGFPVSGQWLVCNKPEIVKQHEAKVYGKASVGSPPMSVPHLDTRMIDGKRALLFGPYAGFSTRFLKKGSLLDLFKSIKLNNILPLLAVGRDNWPLTKYLISQVMQSPADRLNALKDYMPTAKAEDWDLDIAGQRVQVIKKDAKHTGVLEFGTEVVTSADGSISALLGASPGASTSVPIMIQLIERCFKNHIKTDAWQQRLKEMIPSYGQSLANNEALSDETRARTSKVLGLV
>NZ_CP043450.1|WP_112566853.1|2502749_2503280_-|hypothetical-protein
MNLFKPCIYFCVLAMTISACKQSKPKPVSNDISKTTVTVAGKKDSVINNPRKKYGAATVAEPCVKCLLAVIQDSKSYKENTEGLSAQNINYTINWVKASAPALTPDTSNKTNGIRIDVKKDENGEDTRLCSYVYNNSSGTMYLLNNQNKYEHEISSITPAILKKIRNSCYWGVASR
>NZ_CP043450.1|WP_112566856.1|2498450_2502746_+|response-regulator
MNSYKCYLVLLLQAISLCVFSQSRPIHFQHIGSREGLSELNINCIIQDSRGFIWVGTRDGLNRYDGNKFKIFKNIIGDNNSISNSFVQDIVEDKNGNLWISTSGGGLNMYDRKLDRFVHYRHNPNNKNSIASDILVKIALDKSGNLWICNQKEGLDQFNIAQKKFTHYGYNEADNSSLSDNNVRVVYVDSQDKLWVGTTYGGLNLYNPQSHNFTRFVHDENKSSSLSANKVNAILEDSGHRLWVGVSDGGLNLFNPADKTFTHYKNDPNNKNSLSYNSVQCLAEDSNHDLWIGTENGGLNIFNYALNIFNNHQEDDVDNSSIANNSVDVILKDKSGNMWIGAFASGLNFYKKTSENFTHYQHGAQSISLSNNFVLSVYEDKKNNIWVGTDGGGLNLFNPEKGEFKYYKRSNSNICGDYVLTIQEDAKNNLWIGTWGDGVSMMNPQTRTFKSFKHNPDDSTSISGNNIYAIAKTLDGKLWFGTLGTGLDLFDPKTNKFIHYRHDTGNPKSISSDNINSLLGDSKGNLWVGTNDGGVNLYDATTNSFKPVQYEKLNSALGNNTALDLFEDHLGNIWICTYSGIYKLNPVTGKVTNFKAKDGLPNDYTYAIEEDAAGNLWISTNRGISRYNPNTNKFRNFTIADGLQAEEFKPHSAVKAHDGIMYFGGVNGFNMFDPAGIRNSIYDPPLVLTDFQIYNKSIHVAQNNDDPSPLKQDIAETKSITLTHDQSVISFEYVSMDYSLSNKESYAYQLEGFDKGWNYVGNKNTATYTNLPAGNYVFRVKSRSADGKWSLREVSLNVTVLPPFWLTWWFISLLVLVTIVVVYTWHRLRVKAIIEQKNLLEEQVTERTAEVMQQSEELKAQSENLQTLNVELQNQSEELQALNEELQAQSEELQLQKEQEREAREEADKANQAKSIFLATMSHEIRTPMNGVIGMASLLGETELNTEQREYTDTIISCGDSLVNVINDILDFSKIESGKMEMEQEDFDLRQCIEEVMDIFSQNAAKRELELVYQIDPALPQQIIGDSLRLKQVLTNLTGNALKFTEHGEVFIKVFLSKNIGDKEIEIGFSVMDTGIGIPEDKLITLFNAFSQVDSSTTRKYGGTGLGLVISERLVKLMGGEIWVESVFGEGSVFVFTIKSAISKKQSKQIPIVFNADELEGKKVLIVDDNKTNRFILQTQLEQWGIQTVAAASGRQALDILGANNGFNLVITDMEMPEMDGVGLAREIKDNYKNLPVIMLSSIGDGSKKKYPGLFSAILTKPVKQSQLGKSLQAEFQGKTQVQVVETKPDKLFDANFANEHPLSILVAEDNTVNQKLISRMLEKLGYDFELAHNGYDTLEKLKANPTFDVIFMDVQMPEMDGFEATRHIRQYAFKQPFIIAMTANAGPDDRDMCISEGMDDYIAKPMKTDALINVLKGAYKMMKNVKGKYV
>NZ_CP043450.1|WP_112566859.1|2498063_2498276_-|DUF2132-domain-containing-protein
MQQQPNNPLHGKTLEMILNELVAHFGWKELGIRIRINCFNDNPSVKSSLKFLRKTDWARKKVEDLYLEIV
>NZ_CP043450.1|WP_112566862.1|2496692_2497991_+|DEAD/DEAH-box-helicase
MAWSDKLKLNKQLLRSVNEVGFTNPKELQLKTINRIIGGQDIIAIGPEGSGKTTTYVLGVLNRFNYAPEGVPRVLILVPEKENVFAVIEQFDRLNKNKSIRIVGLYVTPGFESQMDDLADGADIVVATPDRARAIYLKLALNLNKVDLLVVDDADQIVKKGLQLPVVELANSIDKAQHLVFTEVIHAKLEKMLDPFMRDPAIIEVDELSDTVIETHEQLLYNVPNFGTKLNLLNLFMYDEELFTKTVVFVNTQTTAEKLFQSLKSRLRTGVAYLNPKFFDTKGFKNIEDFKADPATRILIVTNENEEELNLSDIPFLIQFDLPADNELFISRIVNHDPDSEEETLAMTFATDIELGQVKKIEQLIGHKIPVAELPEDLVIVTESKSKKADAKEDKKPAGVGEAFHEKKASNAKTYNLSASTKAKMNKKKKHG
>NZ_CP043450.1|WP_112566831.1|2511004_2512012_-|biotin-synthase-BioB
MTEVRHNWTKEEIAEIYHTPLLDLVYKAATIHRENKDYAEVQISSLISIKTGGCSEDCAYCPQAARYNTGVNVHAMMPKDEVIAAAEKAKAGGASRLCMGAAWREVRDNRDFDKVIDMVKAVNELDMEVCCTLGMLTEGQAQRLADAGLYAYNHNLDTSEEDYKRIITTRTYDERLKTLEHVRKAKITVCSGGIIGLGETVEDRVSMLKTLSNLPKHPESVPINALVPVAGTPLADQPRVSVWDMVRMVATTRIIMPKTVVRLSAGRTEMSTVEQAFCFMAGANSIFAGEKLLTTPNPSFDTDMAMFELLGLSPRKAFKNGRPNEVKKEEVEVAG
>NZ_CP043450.1|WP_112566828.1|2512163_2513519_-|magnesium-transporter
MQSFDLDKTDLLRIKTALEADDAELENVLKEYHASEIAILFEKLQQEEKERIINILPADVASEVLSEMDEEHGPAELLVNLDPEKRTEIVEELDYDDATDIISQLDEEDQQEILEDLDHEDASSIRALMTYAEDTAGGLMNSEIIKVNINMDKKDALDEIIRQSEEMEEFYTICVVDNNDILKGILSIKTVIKARADARISDLVTTDFVYVKAELDQEEVARLIKQYNLTSIPVVDDDMKLLGRVTVDDIIDVMEEENTEDILKISGVSEDEELSGNWVEAVKSRLPWLVINLGTAFLAASIIRTFDDTVAKLSIISAYMTIIAGMGGNAATQALAVTVRRISLSDLSDKQAYNTVLKEFLVGMINGAANGIIVFIVAFFYDANPMLGLVLFLAMTGNLIIAGLTGASIPLILKRVGIDPAVASSIIITTFTDCIGFLLPLYLATKLLLKN
>NZ_CP043450.1|WP_112566825.1|2513611_2514226_-|YigZ-family-protein
MLFDDTYKTIENPAEGIFRDRGSKFLAYAYPINSENDIKAIVTQLKSEHPKANHNCWAMRLTIDRSVFRVNDDGEPSGTAGRPILNTLLSKDLTNILVVVVRYFGGTLLGVPGLINAYKVATEEALNQAVIISKTVNDVYTVSFDYLQMNDVMRIIKEENLIILGQVFDNDCSIQLSIRKTQVEQALFKISKVSGTKVKYDHSI
>NZ_CP043450.1|WP_112566821.1|2514235_2515114_-|DMT-family-transporter
MLFVFLSICCSVIVSILLKLAKRYHVDVYQAITWNYSMAILLTWFFFKPQLSIIQNAPVYNYLALGILFPSIFVIMATSVRKAGIVRTDVAQRLSLFIPILAAFVLFGEATGTVKAIGIVLAFIAIICSVPWQKSAGNKVEKGSWIYLLIVFLGFGVIDVLLKQLTKVSNVPFTTAIFVIFIIAFVLTFIGLLYRVSIKKTKFSLPQIIIGWILGIANFGNILFYLKAHQALANSPSAVFSSVNIGVILVGTLIGIFVFKEKLSLLNKIGILVAVLAIVIIYFPQTLGFLHL
>NZ_CP043450.1|WP_112566818.1|2515114_2516170_-|bifunctional-diaminohydroxyphosphoribosylaminopyrimidine-deaminase/5-amino-6-(5-phosphoribosylamino)uracil-reductase-RibD
MLEHEKYMRRCLELAESGAGYVSPNPMVGAVVVHDGQIIGEGYHQKYGQAHAEVNAIAQVTQKFDNHAELLKNSTIYVSLEPCAHYGKTPPCADLIIKHQIPKVVVGCRDPFAQVDGKGIEKLQAVGIEVITGVLEQECQWLNRRFFTKVQKHRPYIILKWAQTQDGFFAPDDGSQFWITGPESKKLVHKWRSEEDAILIGKNTALSDNPQLNVRYWDGPSPKRVVIDRRLELNKGLNIFDQSAETLIFNEVKFDLDGKNRYIALEDFERFVPQYILYQLYLQDIQSVIIEGGARTLESFIEAGLWDEARIFTGDKVLGKGIKAPQITGILADEYPVGADRLQLLYNKPVI
>NZ_CP043450.1|WP_112566815.1|2516203_2517067_+|peptide-chain-release-factor-N(5)-glutamine-methyltransferase
MITIKDVFEVYRLQINGIYDINEIEALTLLVIAEVTGLSRASIKAFPERELTTEQADQIKNILTELKTGKPVQYILGITEFYGLPFRVNSFVLIPRPETEELVEWIISGERLKAKGEGFSILDIGTGSGCIAVSLKKNLSNVDVSAIDISEGALQTAKGNAQLNEVEVNFIHADILNIKPENVFPKFNIIVSNPPYVTLEDKKQMHTNVTDFEPHTALFVPEHDPLLFYRAIADFTLSNLMAEGLLYFEINENLGDETVALLADKGFKNIELRKDMSGRDRMVKAEL
>NZ_CP043450.1|WP_112566812.1|2517070_2518180_-|hypothetical-protein
MKPLTNILLKIFAGGFFRVHAGILLFVFLAMVGVVPPQYLIGYHKTLMLAMDSSSAVMAIVFVIWLIYAIKSWHYVSGQIFAAEQHFLFYSSNSLSKQKQLKSWFWAQAAILSPIIVYAFITIGVGFANHYYVLPVCIFLYLLILSYLSAVIYVKQINRLIDGNNQSLLLKLSSKWHKPYFSLYIYHLFDKRKVPYLITKGLSWLIITGVFYVFADVKTDVRVAGIAILAVVTAHIVLIFEERKFEENALSFSRNLPYSRKRRFLNFIGVYFVLLLPESIWLFSRFNPLMAIELLFLALSVAMLFHGLLYWFGLNMDKYLQWILGLFIVLFWIIMFKLLWILVPLNIAIAYWLFYHNYYRFEGVVSDKL
>NZ_CP043450.1|WP_112566809.1|2518179_2518815_-|ABC-transporter-ATP-binding-protein
MLQFQNFKKSYGNYPALKVEDLRLEAGIYWIKGVNGSGKSTLLKSIAGILAFDGDILLADHISIKKQPVPYRKLVNFAEAEPVFPDFLTGTEMIALFADAKDAPTGQQDHYIKSMGMQSFVDRPVGTYSSGMMKKISLLLAFLGKPKLILLDEPLITIDTASLAILNNWIREKHEQEGTSFLLSSHQILEDGSLPVSGELLVEDQTLKFIS
>NZ_CP043450.1|WP_112566806.1|2518929_2519919_-|D-alanine--D-alanine-ligase
MSVKNIALLAGGFTGEYEVSLNSAKNIAANLASNSNYKVYTILVTRDRWFFEANDTTVDVDKNDFTITLNQEKIKFDFAFITIHGTPGEDGKLQGYFDMLGIPYNTCDATTSAITMNKAYTKAIVNGIHGLHTAHSMRLFERDVHDVATIAANLKFPLFVKPNNGGSSVGMSKVQNIAGLPEALNRAFQEDAQVLVEEFIKGREFSIGIARLHGKIKVLPATEIITSKDFFDYEAKYTSGVTQEITPADLSPEKVQEIAGIVTEVYTRLNCRGMARIDFILLEGSNDFYFIEINTTPGQSAASLIPQQVRAAGMDVGEFYSALIEGAAL
>NZ_CP043450.1|WP_112566804.1|2520174_2520969_+|PASTA-domain-containing-protein
MSKFGAYLKSKSFRNNLLMAIVTVIAVVLIAFFSLGYYTRHGSGIPVPKLKGLTIDKAMDILKEQGFGYKIDSVYVQDVAPGTIVEQDPDPGTNVKENRVIYLTMVTLQAPNVALPDLEQSNYREAIATISNYGLKVGDTTYRSDIARDRILEVRFGGQVIKPGTKIPKGSRIDLVLGDGEGASEVEIPELVNLDLDAARFAIKGAGLTVGIITYQGTITDSTNVVVVSQYPMKTDSLSKTSIGTRINLTVSQGTKTDAAPPAN

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Crispr_ID: NZ_CP043450_6

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043450_6

4515133-4515238

Orphan

Consensus_repeat	Method
GATTGCTTCGTACCTCGCAATGACGTGGTGGAGAGG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043450_6

>merge|NZ_CP043450|6|4515133-4515238|CRISPRCasFinder
GATTGCTTCGTACCTCGCAATGACGTGGTGGAGAGGAAGCTGCCATGCCAATCCGCTCTGTACAGTTCGCGATTGCTTCGTACCTCGCAATGACGTGGTGGAGAGG

>NZ_CP043450|6|6|4515133-4515238|CRISPRCasFinder
GATTGCTTCGTACCTCGCAATGACGTGGTGGAGAGG	AAGCTGCCATGCCAATCCGCTCTGTACAGTTCGC
GATTGCTTCGTACCTCGCAATGACGTGGTGGAGAGG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043450.1\|WP_112567515.1\|4509953_4510730_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112567492.1\|4527481_4528012_+\|ferritin	unknown	unknown	gnl\|CDD\|153113
NZ_CP043450.1\|WP_112567521.1\|4504591_4505317_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|187585
NZ_CP043450.1\|WP_112567500.1\|4523790_4524441_-\|beta-phosphoglucomutase	unknown	unknown	gnl\|CDD\|213672
NZ_CP043450.1\|WP_112567494.1\|4526988_4527348_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112567498.1\|4524486_4526349_-\|glycoside-hydrolase-family-13-protein	unknown	unknown	gnl\|CDD\|200479
NZ_CP043450.1\|WP_112567525.1\|4503272_4503701_-\|MarR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197670
NZ_CP043450.1\|WP_112567490.1\|4528234_4528495_-\|(2Fe-2S)-ferredoxin-domain-containing-protein	unknown	unknown	gnl\|CDD\|239278
NZ_CP043450.1\|WP_112567506.1\|4515311_4517789_-\|glycoside-hydrolase-family-31-protein	unknown	unknown	gnl\|CDD\|376446
NZ_CP043450.1\|WP_112567519.1\|4505368_4506274_-\|helix-turn-helix-domain-containing-protein	unknown	unknown	gnl\|CDD\|131350
NZ_CP043450.1\|WP_112568123.1\|4519537_4521256_-\|alpha-amylase	unknown	unknown	gnl\|CDD\|200487
NZ_CP043450.1\|WP_112567517.1\|4506902_4509320_-\|FtsX-like-permease-family-protein	unknown	unknown	gnl\|CDD\|274576
NZ_CP043450.1\|WP_112568125.1\|4514773_4515073_-\|GIY-YIG-nuclease-family-protein	unknown	unknown	gnl\|CDD\|198395
NZ_CP043450.1\|WP_112567510.1\|4511751_4511943_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112567512.1\|4511191_4511749_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112567508.1\|4512049_4514332_-\|1,4-alpha-glucan-branching-protein-GlgB	unknown	unknown	gnl\|CDD\|235445
NZ_CP043450.1\|WP_112567504.1\|4517887_4519267_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340871
NZ_CP043450.1\|WP_112567502.1\|4521351_4523661_-\|glycoside-hydrolase-family-65-protein	unknown	unknown	gnl\|CDD\|237517
NZ_CP043450.1\|WP_112567523.1\|4503707_4504223_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_CP043450.1\|WP_112567488.1\|4528572_4529724_-\|DUF3095-domain-containing-protein	unknown	unknown	gnl\|CDD\|371453

Protein	Function_ID	Function_description	E-value
NZ_CP043450.1\|WP_112567521.1\|4504591_4505317_-\|SDR-family-oxidoreductase	gnl\|CDD\|187585	cd05324, carb_red_PTCR-like_SDR_c, Porcine testicular carbonyl reductase (PTCR)-like, classical (c) SDRs. PTCR is a classical SDR which catalyzes the NADPH-dependent reduction of ketones on steroids and prostaglandins. Unlike most SDRs, PTCR functions as a monomer. This subgroup also includes human carbonyl reductase 1 (CBR1) and CBR3. CBR1 is an NADPH-dependent SDR with broad substrate specificity and may be responsible for the in vivo reduction of quinones, prostaglandins, and other carbonyl-containing compounds. In addition it includes poppy NADPH-dependent salutaridine reductase which catalyzes the stereospecific reduction of salutaridine to 7(S)-salutaridinol in the biosynthesis of morphine, and Arabidopsis SDR1,a menthone reductase, which catalyzes the reduction of menthone to neomenthol, a compound with antimicrobial activity; SDR1 can also carry out neomenthol oxidation. 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, 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-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.	8.52971e-84
NZ_CP043450.1\|WP_112567500.1\|4523790_4524441_-\|beta-phosphoglucomutase	gnl\|CDD\|213672	TIGR01990, bPGM, beta-phosphoglucomutase. This model represents the beta-phosphoglucomutase enzyme which catalyzes the interconverison of beta-D-glucose-1-phosphate and beta-D-glucose-6-phosphate. The 6-phosphate is capable of non-enzymatic anomerization (alpha <-> beta) while the 1-phosphate is not. A separate enzyme is responsible for the isomerization of the alpha anomers. Beta-D-glucose-1-phosphate results from the phosphorylysis of maltose (2.4.1.8), trehalose (2.4.1.64) or trehalose-6-phosphate (2.4.1.216). Alternatively, these reactions can be run in the synthetic direction to create the disaccharides. All sequenced genomes which contain a member of this family also appear to contain at least one putative maltose or trehalose phosphorylase. Three species, Lactococcus, Enterococcus and Neisseria appear to contain a pair of paralogous beta-PGM's. Beta-phosphoglucomutase is a member of the haloacid dehalogenase superfamily of hydrolase enzymes. These enzymes are characterized by a series of three catalytic motifs positioned within an alpha-beta (Rossman) fold. beta-PGM contains an inserted alpha helical domain in between the first and second conserved motifs and thus is a member of subfamily IA of the superfamily. The third catalytic motif comes in three variants, the third of which, containing a conserved DD or ED, is the only one found here as well as in several other related enzymes (TIGR01509). The enzyme from L. lactis has been extensively characterized including a remarkable crystal structure which traps the pentacoordinate transition state. [Energy metabolism, Biosynthesis and degradation of polysaccharides].	5.01105e-84
NZ_CP043450.1\|WP_112567488.1\|4528572_4529724_-\|DUF3095-domain-containing-protein	gnl\|CDD\|371453	pfam11294, DUF3095, Protein of unknown function (DUF3095). Some members in this bacterial family of proteins are annotated as adenylyl cyclase however this cannot be confirmed. Currently no function is known.	6.84506e-138
NZ_CP043450.1\|WP_112567525.1\|4503272_4503701_-\|MarR-family-transcriptional-regulator	gnl\|CDD\|197670	smart00347, HTH_MARR, helix_turn_helix multiple antibiotic resistance protein.	1.80811e-13
NZ_CP043450.1\|WP_112567490.1\|4528234_4528495_-\|(2Fe-2S)-ferredoxin-domain-containing-protein	gnl\|CDD\|239278	cd02980, TRX_Fd_family, Thioredoxin (TRX)-like [2Fe-2S] Ferredoxin (Fd) family; composed of [2Fe-2S] Fds with a TRX fold (TRX-like Fds) and proteins containing domains similar to TRX-like Fd including formate dehydrogenases, NAD-reducing hydrogenases and the subunit E of NADH:ubiquinone oxidoreductase (NuoE). TRX-like Fds are soluble low-potential electron carriers containing a single [2Fe-2S] cluster. The exact role of TRX-like Fd is still unclear. It has been suggested that it may be involved in nitrogen fixation. Its homologous domains in large redox enzymes (such as Nuo and hydrogenases) function as electron carriers.	4.52241e-10
NZ_CP043450.1\|WP_112567506.1\|4515311_4517789_-\|glycoside-hydrolase-family-31-protein	gnl\|CDD\|376446	pfam01055, Glyco_hydro_31, Glycosyl hydrolases family 31. Glycosyl hydrolases are key enzymes of carbohydrate metabolism. Family 31 comprises of enzymes that are, or similar to, alpha- galactosidases.	0
NZ_CP043450.1\|WP_112567519.1\|4505368_4506274_-\|helix-turn-helix-domain-containing-protein	gnl\|CDD\|131350	TIGR02297, AraC-type_DNA-binding_domain-containing_protein, 4-hydroxyphenylacetate catabolism regulatory protein HpaA. This putative transcriptional regulator, which contains both the substrate-binding, dimerization domain (pfam02311) and the helix-turn-helix DNA-binding domain (pfam00165) of the AraC famil, is located proximal to genes of the 4-hydroxyphenylacetate catabolism pathway.	8.31958e-27
NZ_CP043450.1\|WP_112568123.1\|4519537_4521256_-\|alpha-amylase	gnl\|CDD\|200487	cd11349, AmyAc_3, Alpha amylase catalytic domain found in an uncharacterized protein family. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.	0
NZ_CP043450.1\|WP_112567517.1\|4506902_4509320_-\|FtsX-like-permease-family-protein	gnl\|CDD\|274576	TIGR03434, ADOP, Acidobacterial duplicated orphan permease. Members of this protein family are found, so far, only in three species of Acidobacteria, namely Acidobacteria bacterium Ellin345, Acidobacterium capsulatum ATCC 51196, and Solibacter usitatus Ellin6076, where they form large paralogous families. Each protein contains two copies of a domain called the efflux ABC transporter permease protein (pfam02687). However, unlike other members of that family (including LolC, FtsX, and MacB), genes for these proteins are essentially never found fused or adjacent to ABC transporter ATP-binding protein (pfam00005) genes. We name this family ADOP, for Acidobacterial Duplicated Orphan Permease, to reflect the restricted lineage, internal duplication, lack of associated ATP-binding cassette proteins, and permease homology. The function is unknown.	6.72198e-57
NZ_CP043450.1\|WP_112568125.1\|4514773_4515073_-\|GIY-YIG-nuclease-family-protein	gnl\|CDD\|198395	cd10448, GIY-YIG_unchar_3, GIY-YIG domain of uncharacterized hypothetical protein found in bacteria. The family includes a group of uncharacterized bacterial proteins with a GIY-YIG domain that shows statistically significant similarity to the N-terminal catalytic domains of GIY-YIG family of intron-encoded homing endonuclease I-TevI and catalytic GIY-YIG domain of nucleotide excision repair endonuclease UvrC.	8.69998e-40
NZ_CP043450.1\|WP_112567498.1\|4524486_4526349_-\|glycoside-hydrolase-family-13-protein	gnl\|CDD\|200479	cd11340, AmyAc_bac_CMD_like_3, Alpha amylase catalytic domain found in bacterial cyclomaltodextrinases and related proteins. Cyclomaltodextrinase (CDase; EC3.2.1.54), neopullulanase (NPase; EC 3.2.1.135), and maltogenic amylase (MA; EC 3.2.1.133) catalyze the hydrolysis of alpha-(1,4) glycosidic linkages on a number of substrates including cyclomaltodextrins (CDs), pullulan, and starch. These enzymes hydrolyze CDs and starch to maltose and pullulan to panose by cleavage of alpha-1,4 glycosidic bonds whereas alpha-amylases essentially lack activity on CDs and pullulan. They also catalyze transglycosylation of oligosaccharides to the C3-, C4- or C6-hydroxyl groups of various acceptor sugar molecules. Since these proteins are nearly indistinguishable from each other, they are referred to as cyclomaltodextrinases (CMDs). This group of CMDs is bacterial. The Alpha-amylase family comprises the largest family of glycoside hydrolases (GH), with the majority of enzymes acting on starch, glycogen, and related oligo- and polysaccharides. These proteins catalyze the transformation of alpha-1,4 and alpha-1,6 glucosidic linkages with retention of the anomeric center. The protein is described as having 3 domains: A, B, C. A is a (beta/alpha) 8-barrel; B is a loop between the beta 3 strand and alpha 3 helix of A; C is the C-terminal extension characterized by a Greek key. The majority of the enzymes have an active site cleft found between domains A and B where a triad of catalytic residues (Asp, Glu and Asp) performs catalysis. Other members of this family have lost the catalytic activity as in the case of the human 4F2hc, or only have 2 residues that serve as the catalytic nucleophile and the acid/base, such as Thermus A4 beta-galactosidase with 2 Glu residues (GH42) and human alpha-galactosidase with 2 Asp residues (GH31). The family members are quite extensive and include: alpha amylase, maltosyltransferase, cyclodextrin glycotransferase, maltogenic amylase, neopullulanase, isoamylase, 1,4-alpha-D-glucan maltotetrahydrolase, 4-alpha-glucotransferase, oligo-1,6-glucosidase, amylosucrase, sucrose phosphorylase, and amylomaltase.	0
NZ_CP043450.1\|WP_112567492.1\|4527481_4528012_+\|ferritin	gnl\|CDD\|153113	cd01055, Nonheme_Ferritin, nonheme-containing ferritins. Nonheme Ferritin domain, found in archaea and bacteria, is a member of a broad superfamily of ferritin-like diiron-carboxylate proteins. The ferritin protein shell is composed of 24 protein subunits arranged in 432 symmetry. Each protein subunit, a four-helix bundle with a fifth short terminal helix, contains a dinuclear ferroxidase center (H type). Unique to this group of proteins is a third metal site in the ferroxidase center. Iron storage involves the uptake of iron (II) at the protein shell, its oxidation by molecular oxygen at the ferroxidase centers, and the movement of iron (III) into the cavity for deposition as ferrihydrite.	3.20187e-60
NZ_CP043450.1\|WP_112567502.1\|4521351_4523661_-\|glycoside-hydrolase-family-65-protein	gnl\|CDD\|237517	PRK13807, PRK13807, maltose phosphorylase; Provisional.	0
NZ_CP043450.1\|WP_112567504.1\|4517887_4519267_-\|MFS-transporter	gnl\|CDD\|340871	cd17313, MFS_SLC45_SUC, Solute carrier family 45 and similar sugar transporters of the Major Facilitator Superfamily of transporters. This group includes the solute carrier 45 (SLC45) family as well as plant sucrose transporters (SUCs or SUTs) and similar proteins such as Schizosaccharomyces pombe general alpha-glucoside permease. the SLC45 family is composed of four (A1-A4) vertebrate proteins as well as related insect proteins such as Drosophila sucrose transporter SCRT or Slc45-1. Members of this group transport sucrose and other sugars like maltose into the cell, with the concomitant uptake of protons (symport system). Plant sucrose transporters are crucial to carbon partitioning, playing a key role in phloem loading/unloading. They play a key role in loading and unloading of sucrose into the phloem and as a result, they control sucrose distribution throughout the whole plant and drive the osmotic flow system in the phloem. They also play a role in the exchange of sucrose between beneficial symbionts (mycorrhiza and Rhizobium) as well as pathogens such as nematodes and parasitic fungi. There are nine sucrose transporter genes in Arabidopsis and five in rice. Vertebrate SLC45 family proteins have been implicated in the regulation of glucose homoeostasis in the brain (SLC45A1), with skin and hair pigmentation (SLC45A2), and with prostate cancer and myelination (SLC45A3). Mutations in SLC45A2, also called MATP (membrane-associated transporter protein) or melanoma antigen AIM1, cause oculocutaneous albinism type 4 (OCA4), an autosomal recessive disorder of melanin biosynthesis that results in congenital hypopigmentation of ocular and cutaneous tissues. The SLC45 family and related sugar transporters belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.7616e-80
NZ_CP043450.1\|WP_112567508.1\|4512049_4514332_-\|1,4-alpha-glucan-branching-protein-GlgB	gnl\|CDD\|235445	PRK05402, PRK05402, 1,4-alpha-glucan branching protein GlgB.	0
NZ_CP043450.1\|WP_112567523.1\|4503707_4504223_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|366181	pfam00583, Acetyltransf_1, Acetyltransferase (GNAT) family. This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.	6.92562e-14

>NZ_CP043450.1|WP_112568125.1|4514773_4515073_-|GIY-YIG-nuclease-family-protein
MHRGGCVYIVTNKTHSVLYTGVTSDIVGRIWDHKNKTYPQSFTAKYNCSKLVYYIFYSHIEEAIAAEKAIKGGSRQMKTDLVNQLNPEWKDLYDGLLNE
>NZ_CP043450.1|WP_112567508.1|4512049_4514332_-|1,4-alpha-glucan-branching-protein-GlgB
MAKKTTQTENPLPEAKPVKETKAVTKVKADKVTPETGSPEPKKAAKTKAVAAEKPAATAKAKTVATEKPAATAKAKTVAAEKPAAVKKAPTPAKAKAVKAEKPAETTPVQQPVKLKAVEAYSRFTDFDISLFKSGKHYKLYEKLGSHVVEYQGVVGTYFAVWAPNAQYVSVIGNFNGWNRGSHSLNARWDSSGIWEGFIPNIGVGETYKYFINSSSGEDLEKSDPFALRWELPPRTASIVADTYYEWKDQDWMKNRQEHNGLDKPYSVYEVHLGSWARNWESPDEFLTYTQLAEKMVPYVKEMGFTHVEFMPIMEHPYYPSWGYQVSGYFAAASRYGTPQELMYLIEEFHKAGIGVILDWVPSHFPGDIHALYRFDGTHLYEHADSRKGFHPDWKSYIFNYGRNEVRAFLISNALFWLDRYHADGLRVDAVASMLYLDYSRKHGEWEANMYGGNENLEAISFLKEFNEAVYSHFPSAQTIAEESTSFTGVSRPVYLGGLGFGMKWMMGWMHDTIGYFKEDPIHRKYHHNEITFSTIYAFTENFMLPFSHDEVVYGKGSMLRKMPGDEWRQFANLRLMYSYMFTHPGTKLLFMGAEFGQGDEWDFSRSLQWHVLQYPNHRGISETVKALNHLYRDEPALYEKAFAFDGFEWVDGGNANDSILVYRRKGHDSKNDLMIVLNMTPVIRRDYRIGVPAAGKWKEIFNSDQEKYWGSGIINYDALSTEPVKWHGKAQSIKITIPPLAAVVFKLSPDVPAKYELKK
>NZ_CP043450.1|WP_112567510.1|4511751_4511943_-|hypothetical-protein
MNPKFKYLYLIGGIVATILLIVQIVTTYPTPNTVGIILGALPALALFYLSYKAYHVKKDNELM
>NZ_CP043450.1|WP_112567512.1|4511191_4511749_+|hypothetical-protein
MTTNAPIEIPLSKSKIIKGLLGSTAFVAIGLWLLIRQPHIGNPVFDNALVKYGASIASIIFFGFAAFFFLKKLGDKKPGMIINNDGLYDNSSAAAIGLIPWDDIIGVSVSSVMNQQFLIICLKNPEQYIAAQTNLIKKKSFGFNYKNYGSPIAISANTLQCNLYELKAQIEDKIAKQKSGEVSAE
>NZ_CP043450.1|WP_112567515.1|4509953_4510730_+|hypothetical-protein
MGLFDLFKKKPTEPIQPTAQTQQEKPAMQQSEYNGYLTEALESRLLNMGYQIERHPQYLALIVDSEIEIAAAIVDIHGAHPFIMQVNVLTIHPVYFPKGIYECLVGFGETIDKRINSALDNYLDSTFSPIMAGFSDTHDPDVDLLITTNNREVLWHPKLGDLMVQGQWEEMPDGKCLFEILREKIKPLLTDNKFNWLKIYISKNADGAIIGECVFNNQLLNDALDDITQLAEAWIMKGEFKALKQFIMFRSCDAYDNI
>NZ_CP043450.1|WP_112567517.1|4506902_4509320_-|FtsX-like-permease-family-protein
MLKNYLLVAFRNLSKNKAFSAINIVGLAIGMAACLLILQYVSFELSYDNFHVKKDRVFRINQDRYNNGKLSTQWAGGAFAPGNAFKTELPEIEEYVKIVGAGQTIATHKEQKMVIQNVYYVSDAFFKTFSFPLLNGDPNTALKEPNTAVITQQIADKLFHGVNPVGQTLYINTDKPLKITGVMNNMPANTHMNFDIMQSYATLLKENPPNKDYNIDNAWLNDGCTTYLLLKPGVDPRKLEAKFIPIVKKAYDKYPGSGEGGVYTLQPVKDIHLYSNRMLEFQPNGDGKSVYLLLGIAIFVIVIAWINYINLATARGIGRAKEVGVRKTLGSAKAQLIAQFMLEAMMLNAMAIGLALLIIMACLPAFASISGMQMGFTLFAKPAFWLAVLGIFVLGSFFSGFYPALVLSAFRPVEIMKGKILASPGGVVLRKGMVVFQFAASIFLLIGSLTVFKQLKYMQSQKLGVRIDQTIVIKAPLTKVDSFYRSMSSFKHECLAQSAVKSVTVSTSIPGQPVGWNAGGIKLVGSDQSTSKQYRIIGADYDYLNAYNIKLIAGRKFSKAFGDEPHKVVFTKKGVEQLGFSKPADALGKRIDFWGQVYEIIGVADNFHQQSLHDAYDSMIFRCIPDVRGPVSVKVSTTNMPQTIADLKKTWAAFFPGDQFDYFFLDQFFNKQYQTDQRFGQVFGVFTGIAIFVACLGLFGLVSYTIVQRTKEIGIRKVLGASVNSILGLLYKDFALLVVVSFVISAPIGWYAIHQWLQTYAFRMDINPFLFVIPFFLVLLVAFATVSFLSVKAALMNPVKSLKTE
>NZ_CP043450.1|WP_112567519.1|4505368_4506274_-|helix-turn-helix-domain-containing-protein
MPVLTAPEKTVIPTFALQQKDGQGNTMIDVREAGGQCGEFKLDPAFLQPHRKDYYLFVLIKSGANRHWIDFVPYTVKPDTFYFTVPQQVHLKEHAGPTEGLMMSFTDEFLQLEDNRILKQLPIIQNPAAAHEIKLNPADLVFIEDTMRKMLVEFNADGTWRNQMLTSWLRVLVIYLSRLYSEQYNETCVTLNYCLLKSFQALIGEHYATQHDVAAYAEQLNLTPGHLTDVIKQQSGKTAITHIHDRLIVEAKRRLLHTGLSVKQIADELGFEDSAYFNRFFKRLTSTTPIAYRMQIREMYS
>NZ_CP043450.1|WP_112567521.1|4504591_4505317_-|SDR-family-oxidoreductase
MEKQTVLITGANKGIGLESARQLAKAGYYIYLGSRDQDRGQKAVEQLKAEGINDVELLLIDVTSEASVQKAHDELAAKINHLDVLINNAGIPGSFPQKADTVSDDTMKEVFEVNFFGVIRTVRIFIDLVKKSPNPRIVNVTSDLGSLTYHNDPEWEHYEIKSAAYGPSKTALNAYTVALAYDLKDQVKVNMVNPGYTNTEFNGNRGPKPVEDGAAPIVKYAMIGTDGPTGKFFSDYGESPW
>NZ_CP043450.1|WP_112567523.1|4503707_4504223_-|GNAT-family-N-acetyltransferase
MDTILKPDLASIKIRNKLLPGDLGYIAHVHGDLYAKECGYGLDFEAYVLQGLKDFALEYDTAKDKVWICEHENRIIGFLVAQHRGGDVLQFRYFIFLPQYRGIGLGKKLMQEFLDFMKQGGYTKAYLWTTEEQHSAIALYTRYGFKLSDEKPSNAFGKELIERRYDLTLNR
>NZ_CP043450.1|WP_112567525.1|4503272_4503701_-|MarR-family-transcriptional-regulator
MGTQKHIQEIRTFNRFYTDLIGLLDKHLLNSDYSLAEARILYEIFTAKELSASDIIYRLSIDKGYLSRILKKFEKEALIARQPSADDARVSLLSLTDAGLEVFNGLNEASEKQIMTLISTMSVKQLDALIGHMKAITGLLGK
>NZ_CP043450.1|WP_112567506.1|4515311_4517789_-|glycoside-hydrolase-family-31-protein
MESNTPPNPELITSKLVEVENLIEEEEEFHHLNNPADGIKPVVKKYLGIPTRASQSGNKFYFTDGDAKVEVIVVADEIIRVRLAPHGVFLDDFSYGVPKLPNKHVDYNLHEDDNEFRVSTYKVNCHIRKKDFFISFSDSSNHVTSMDAVPMHWEENVQDGGYYVFCTKTCATDESFFGLGDKPTEFNLRGKRLKNWNTDAYSFQWNQDPLYRSIPFYISVNEGIAHGIFFDNTFKAQFDFGAEDRTKTSFWADGGELQYYYIHGPHMMDVVKSYHTLTGTHPMPPLWALGYHQCRWSYYPEAKVRKIARGFRENQIPCDGIYLDIDYMDGYRCFTWNRKYFPDPKKMISELAADGFKTVVIIDPGIRVDDNYSVFKEGKEKKYFCRRSDDYFMEGHVWPGRCQFPDFTNPEVREWWGGLFDELVQMGVAGVWNDMNEPAVFGAGTFPDDVRHQYDGYRGSHRKAHNIYGMQMVRSTYEGLRKIMKNKRPFTITRAGYSGVQRFSSVWTGDNVASWEHLKLGNIQCQRLSISGIPFCGTDIGGFSGEPDGELFTRWIQMGTFSPFMRAHSAGDTKEREPWSFGEPFTAINRKFIELRYRLIPYLYSIFWEHHRYGFPILRPIVMHEQDTQLNHFRQDEFTYGDKILVCPVMEPGQLKRNVYLPKGKWYNFWTYEVVDGGKEVSVDTPLETMPLFVKAGSVIPEYPVMQYVGQKEIEEVKLNIYYTDYEVNSFLFEDYGETFAYEQDIYLEKKFVVNGSSRAVTIDQSMEGLYTPRYDGYHFNLIGLPFAPTKITVDGKDVKEFQVNEDKTVEFKYTKNFKHIEISK
>NZ_CP043450.1|WP_112567504.1|4517887_4519267_-|MFS-transporter
MSKPTIAQKPRLSFWQIFNMSFGFLGIQFGFALQTGNASRILQTFGADVEHLSWFWLAAPITGMIVQPIIGHYSDMTWNRLGRRRPYFLTGAILSGLALFFMPNSSMLAALIPPIVVGAGMLMIMDASFNVAMEPFRALVADNLPDSQHTTGFSMQTCLIGVGAVIGSWLPYVFAEWFGIGKTAEQGIVPNNVLYSFYIGAAVLIGAILWTVIRTKEYPPEVYATFHEKDESDSGHKGGLSEIFSDLANMPKTMKQLGLVQFFSWFALFSMWVFTTPAVADHVYHIPAGDTTSVAYNDAANWVNVLFGVYNAVSAVYALLLPRIVKKLSRKRAHAFSLVMGGVGLISVFFITDPKLLVLSMVGIGLAWGSILAMPYAILSSSIPASKIGVYMGIFNFFITFPQIVNGVIGGPIVKYAYSGHAVYALVMAGVFMFLAAIAVLFVKDGRKIQIIEPAVNKS
>NZ_CP043450.1|WP_112568123.1|4519537_4521256_-|alpha-amylase
MEQTTNHKLIIYQLLPRLFGNTKTLNKTNGSVEENGVGKLNDINDKALHEIKKMGFTYVWYTGVIEHATMTDYSQFGIKADDPDIVKGRAGSPYAIKDYYDIDPDLAVDVHNRIGEYEALIKRTHNNGLKVLMDLVPNHVARTYASDVKPAGVRDFGEDDDKGKGFSPKNDFYYMPGQPFVVPSGYNPGGDEFKSPLKDGKFDENPAKATGNDVFSAAPSINDWFETMKLNYGVDYMDHRRGYFDPIPPLWSKVYDILHYWSEKGVDGFRCDMVEMVPIEFWGWVIPKLKAEHPGLVFIGEAYDKGKYNDYIFKGKFDYLYDKVGLYDAIKRLTRDEPNSSTWEINAVWNHDSKGIDEHMLRFMENHDEQRIACNDFAGNPWLAVPGMIVTATLNTGPVMVYFGQEVGEPAVGTEGFSGNDGRTSIFDYWGVPQHQKWVNNHEYDGAQLSADQQKLRGFYHNLLTAVHNSEALKSGAFYELMMANERQPGFDTRLYIYARYTNNQRILVITNFNRSDRKLTVKLPDDLLTKLNQSGHKQFTDLLSGTKFNTDDIRNGVEVSLPAMSGLLLEF
>NZ_CP043450.1|WP_112567502.1|4521351_4523661_-|glycoside-hydrolase-family-65-protein
MKNYIKADEWKIIEEGFDAHYNKISESIFSLGNGRMGQRANFEEAYSGDTLQGNYVAGVYYPDKTRVGWWKNGYPEYFAKVLNAANWIGIDVVIDGEQLDLAKCEVFSFRRELNMKEGYLKRDFRAKTASGKEVKVEAIRFCSMADDETGAIKYTLTPLNFSGAITLTPSIDGDVVNKDSNYDEKFWDEVSKATQADGGYIVMRTKKTGFVVATGMKFNILQNGAAIEPATEAIEKEKYVAAKVSLEAKQGESITVIKYAANLSSQNYKQEELVGELNATLTRISTKGFDTMLAEQAAAWAEKWKHNDIIIEGDISAQQAIRFNIYQLNQTYTGEDDRLNIGPKGFTGEKYGGSTYWDTEAYCVPFYLSTAPQKVTRNLLLYRYKQLGKAIENAQLLGFKDGAALYPMVTMDGTECHNEWEITFEEIHRNGAIAFAIYNYVRYTGDEAYLGDYGFDVLLGIARFWSQRVTWSDDKQQYVMLGVTGPNEYENNVNNNWYTSTIATWCMQYTIDVADKIKDTEPEKYAALVSKLNLNEETEFGRFSDIVQKMYYPYDEKRQVFLQQDGYLDKEQILVKDLPASERPINQKWSWDRILRSCYIKQADVLQGIYFFEDQYDIDTIRRNFDFYEPRTVHESSLSPCVHAILAAKLGDEARAYEFYLRTARLDLDDYNNDTEDGCHITSMAGTWMAVVEGFGGMRVSDGKLSFQPFIPEKWSSFSFHIGFRGALLNIKVSKEGVQIKNASDVETTVLVYGKEQLVKANDELLVEA
>NZ_CP043450.1|WP_112567500.1|4523790_4524441_-|beta-phosphoglucomutase
MNTIKACIFDLDGVIVDTAVYHYKAWKRLANSLGFDFTEHQNEQLKGVSRVRSLQLILGWGGVTKTEAEQEQLATQKNTWYMEMVNQMKPEEILPGAKEFLKSCRAVGLKTALGSASKNSMTILEKIGITDMFDAVIDGNKVSKAKPDPEVFLAGAQALGALPEECVVFEDAIAGVEAAIAGDMKVVGIGLPDVLKGANLVIKGLDEMTLDKLYKL
>NZ_CP043450.1|WP_112567498.1|4524486_4526349_-|glycoside-hydrolase-family-13-protein
MRKTLLSTLYCLLAALGVKAQTPALERIEPMSWWVGMSNPNLQLVVHGNNIAQRSVSLSYPGVKLKAVHKVENSNYLFVDLQIFSSAIPGTFPIKFKKAGEKDLTYSYTLNKRDKSAGRAQGVTNKDLIYLIMPDRFSNGDAANDSFNNLREQGIHRDSMFSRHGGDLQGIMNHLDYLKNLGVTAIWLTPEIENDEPHASYHGYAVTDYYKIDPRYGTNDLYKKFVEKCHSMGLKVIKDLVHNHAGTEGYLIQDMPMKSWVHQWPQYTKSNFRDAAVMDPHASPMDRRLMQDGWFDHRMADMNQNNVYVQNYLTQNHIWWVEYAGIDGFRLDTYPYNEPVYMAKWARDVKAEFPKLSIFGETLVWSAANQAFFTQGNTVNRGFDTQLPGITDGVLKDAIYEAINGKDGWTDGVGRLYSVVAQDFLYQDATRNTIFMDNHDMSRLLSMVGEDIPKYKSAMAMLLTMRGVPQMYYGDEILMKNYSNPDGLVREDFPGGWAGDKQNKFTAEGRDKKENDAFNYVSKLANYRKVTTALQTGKMMQFVPENGIYVYFRYDAQKTVMVIFNSSEKDQETTTSRYFERVGDAKKAKNVLTDEMVGLDKVTIPAKTTLVLELIPGVTH
>NZ_CP043450.1|WP_112567494.1|4526988_4527348_+|hypothetical-protein
MIATTELTLWTDVFSTKTGAVYQCDAERCWYVDFAGKVARFDHRNFLKLRKAVYAIDIEEKLLNTTTDPDVEIIFICACDHCYVLSLAQIINLKELLEGTFVMLELNHIIHDRLFSNSL
>NZ_CP043450.1|WP_112567492.1|4527481_4528012_+|ferritin
MKDLLRIKSLISSDIEALLNQQVKKEAFSSSVYLAMASWCNRNGYDFSSEYFFKQAEEERHHQLKFYKYILDMGGNAVSPEITGIKQEYNSFREVFEEALDQEISVTNSIKNIYARCMKEQDFITMEFLNWFLKEQREEEYKARRALELFEVIGEEGTGRWQIDKHVGQIKYDSEA
>NZ_CP043450.1|WP_112567490.1|4528234_4528495_-|(2Fe-2S)-ferredoxin-domain-containing-protein
MSKFTIPDKVLYVCVGSKCGKRGGKDMYKLAKSYIKHYHGREELEVIETECTDRCKYAPICSIQPGNTWLKEYHPKEVLKLMDLID
>NZ_CP043450.1|WP_112567488.1|4528572_4529724_-|DUF3095-domain-containing-protein
MPATDQKFYSDLKVNTIPLGELFVKDELFYNVPADWHIIITDIKGSTLAVSSGQHENVNFVATGSIVSVLNIAFKNSITVPFFFGGDGATFIVPGVIVDAVMQALVLYKDNTLKNFDFELRTGIVPVKRVYDEGYKLCISKYCTSGNFTIPIVLGNGLSYAEKIIKGKEGESFDYMAQEGELDLTGMQCRWDKIPPPENTDEVVSLLVVARDESKQAAVFRKVIGYIDEIYGNPEKRQPISVPKLKLKSTFDRLEREMKVKLGKIKVMELFKDWVIMLYSYIWFNTKKGKHYLNRLVEMSDTLVIDGKINTVISGTSAQRKKLQDILVQLENEGELYFGFHVSRESVMSCYVRDLEDGHIHFVDGAEGGYTKAAGFIKRKLAG

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Crispr_ID: NZ_CP043450_7

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043450_7

5186513-5186600

Orphan

Consensus_repeat	Method
GGCAGGTTTTAGTGGCAGTTGCAGTTC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043450_7

>merge|NZ_CP043450|7|5186513-5186600|CRISPRCasFinder
GGCAGGTTTTAGTGGCAGTTGCAGTTCGCAGTAGCAGTGATTTAGCCTCCGCACAGGCAGTGGCAGGTTTTAGTGGCAGTTGCAGTTC

>NZ_CP043450|7|7|5186513-5186600|CRISPRCasFinder
GGCAGGTTTTAGTGGCAGTTGCAGTTC	GCAGTAGCAGTGATTTAGCCTCCGCACAGGCAGT
GGCAGGTTTTAGTGGCAGTTGCAGTTC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043450.1\|WP_112575677.1\|5189512_5191432_-\|glucosamine-6-phosphate-deaminase	unknown	unknown	gnl\|CDD\|235005
NZ_CP043450.1\|WP_112575679.1\|5195124_5196471_+\|TolC-family-protein	unknown	unknown	gnl\|CDD\|224455
NZ_CP043450.1\|WP_112575685.1\|5203897_5204686_-\|SDR-family-oxidoreductase	unknown	unknown	gnl\|CDD\|181508
NZ_CP043450.1\|WP_112575684.1\|5202886_5203666_+\|GLPGLI-family-protein	unknown	unknown	gnl\|CDD\|273495
NZ_CP043450.1\|WP_112575681.1\|5197808_5198558_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|213222
NZ_CP043450.1\|WP_112575683.1\|5200078_5202880_+\|outer-membrane-beta-barrel-protein	unknown	unknown	gnl\|CDD\|379720
NZ_CP043450.1\|WP_112575671.1\|5178200_5178494_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112575678.1\|5192176_5194741_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|226456
NZ_CP043450.1\|WP_112575675.1\|5183321_5186507_+\|peptidase-S41	unknown	unknown	gnl\|CDD\|143478
NZ_CP043450.1\|WP_112575666.1\|5173588_5174233_-\|uracil-phosphoribosyltransferase	unknown	unknown	gnl\|CDD\|234653
NZ_CP043450.1\|WP_112575682.1\|5198570_5199788_+\|FtsX-like-permease-family-protein	unknown	unknown	gnl\|CDD\|182528
NZ_CP043450.1\|WP_112575680.1\|5196483_5197809_+\|efflux-RND-transporter-periplasmic-adaptor-subunit	unknown	unknown	gnl\|CDD\|273776
NZ_CP043450.1\|WP_112575672.1\|5178579_5181057_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|226888
NZ_CP043450.1\|WP_112575674.1\|5182000_5183284_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|340851
NZ_CP043450.1\|WP_112575668.1\|5174873_5175353_+\|MarR-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|197670
NZ_CP043450.1\|WP_112575673.1\|5181255_5182008_-\|glycosyltransferase	unknown	unknown	gnl\|CDD\|133055
NZ_CP043450.1\|WP_112575676.1\|5186873_5189141_+\|aconitate-hydratase	unknown	unknown	gnl\|CDD\|273561
NZ_CP043450.1\|WP_112575667.1\|5174365_5174863_+\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|366181
NZ_CP043450.1\|WP_112575669.1\|5175638_5177663_+\|excinuclease-ABC-subunit-UvrB	unknown	unknown	gnl\|CDD\|235395
NZ_CP043450.1\|WP_112575670.1\|5177929_5178184_+\|DUF4834-domain-containing-protein	unknown	unknown	gnl\|CDD\|374375

Protein	Function_ID	Function_description	E-value
NZ_CP043450.1\|WP_112575677.1\|5189512_5191432_-\|glucosamine-6-phosphate-deaminase	gnl\|CDD\|235005	PRK02122, PRK02122, glucosamine-6-phosphate deaminase-like protein; Validated.	0
NZ_CP043450.1\|WP_112575679.1\|5195124_5196471_+\|TolC-family-protein	gnl\|CDD\|224455	COG1538, TolC, Outer membrane protein [Cell envelope biogenesis, outer membrane / Intracellular trafficking and secretion].	3.86982e-42
NZ_CP043450.1\|WP_112575685.1\|5203897_5204686_-\|SDR-family-oxidoreductase	gnl\|CDD\|181508	PRK08628, PRK08628, SDR family oxidoreductase.	1.87945e-171
NZ_CP043450.1\|WP_112575684.1\|5202886_5203666_+\|GLPGLI-family-protein	gnl\|CDD\|273495	TIGR01200, conserved_hypothetical_protein, GLPGLI family protein. This protein family was first noted as a paralogous set in Porphyromonas gingivalis, but it is more widely distributed among the Bacteroidetes. The protein family is now renamed GLPGLI after its best-conserved motif.	4.36265e-42
NZ_CP043450.1\|WP_112575681.1\|5197808_5198558_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|213222	cd03255, ABC_MJ0796_LolCDE_FtsE, ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and cell division protein. This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. An FtsE null mutants showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.	2.40315e-115
NZ_CP043450.1\|WP_112575683.1\|5200078_5202880_+\|outer-membrane-beta-barrel-protein	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.	2.41859e-33
NZ_CP043450.1\|WP_112575673.1\|5181255_5182008_-\|glycosyltransferase	gnl\|CDD\|133055	cd06433, GT_2_WfgS_like, WfgS and WfeV are involved in O-antigen biosynthesis. Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have 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.	1.78515e-79
NZ_CP043450.1\|WP_112575678.1\|5192176_5194741_-\|hypothetical-protein	gnl\|CDD\|226456	COG3947, COG3947, Response regulator containing CheY-like receiver and SARP domains [Signal transduction mechanisms].	2.94935e-06
NZ_CP043450.1\|WP_112575675.1\|5183321_5186507_+\|peptidase-S41	gnl\|CDD\|143478	cd07562, Peptidase_S41_TRI, Tricorn protease; serine protease family S41. The tricorn protease (TRI), a member of the S41 peptidase family and named for its tricorn-like shape, exists only in some archaea and eubacteria. It has been shown to act as a carboxypeptidase, involved in the degradation of proteasomal products to preferentially yield di- and tripeptides, with subsequent and final degradations to free amino acid residues by tricorn interacting factors, F1, F2 and F3. Tricorn is a hexameric D3-symmetric protease of 720kD, and can self-associate further into a giant icosahedral capsid structure containing twenty copies of the complex. Each tricorn peptidase monomer consists of five structural domains: a six-bladed beta-propeller and a seven-bladed beta-propeller that limit access to the active site, the two domains (C1 and C2) that carry the active site residues, and a PDZ-like domain (proposed to be important for substrate recognition) between the C1 and C2 domains. The active site tetrad residues are distributed between the C1 and C2 domains, with serine and histidine on C1 and serine and glutamate on C2.	4.84392e-70
NZ_CP043450.1\|WP_112575666.1\|5173588_5174233_-\|uracil-phosphoribosyltransferase	gnl\|CDD\|234653	PRK00129, upp, uracil phosphoribosyltransferase; Reviewed.	9.64432e-70
NZ_CP043450.1\|WP_112575682.1\|5198570_5199788_+\|FtsX-like-permease-family-protein	gnl\|CDD\|182528	PRK10535, PRK10535, macrolide ABC transporter ATP-binding protein/permease MacB.	5.13649e-83
NZ_CP043450.1\|WP_112575680.1\|5196483_5197809_+\|efflux-RND-transporter-periplasmic-adaptor-subunit	gnl\|CDD\|273776	TIGR01730, COG0845:_Membrane-fusion_protein, RND family efflux transporter, MFP subunit. This model represents the MFP (membrane fusion protein) component of the RND family of transporters. RND refers to Resistance, Nodulation, and cell Division. It is, in part, a subfamily of pfam00529 (Pfam release 7.5) but hits substantial numbers of proteins missed by that model. The related HlyD secretion protein, for which pfam00529 is named, is outside the scope of this model. Attributed functions imply outward transport. These functions include nodulation, acriflavin resistance, heavy metal efflux, and multidrug resistance proteins. Most members of this family are found in Gram-negative bacteria. The proposed function of MFP proteins is to bring the inner and outer membranes together and enable transport to the outside of the outer membrane. Note, however, that a few members of this family are found in Gram-positive bacteria, where there is no outer membrane. [Transport and binding proteins, Unknown substrate].	1.33645e-54
NZ_CP043450.1\|WP_112575672.1\|5178579_5181057_+\|hypothetical-protein	gnl\|CDD\|226888	COG4485, COG4485, Predicted membrane protein [Function unknown].	4.64668e-05
NZ_CP043450.1\|WP_112575674.1\|5182000_5183284_-\|glycosyltransferase	gnl\|CDD\|340851	cd03825, GT4_WcaC-like, putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.	6.23019e-118
NZ_CP043450.1\|WP_112575668.1\|5174873_5175353_+\|MarR-family-transcriptional-regulator	gnl\|CDD\|197670	smart00347, HTH_MARR, helix_turn_helix multiple antibiotic resistance protein.	1.12677e-10
NZ_CP043450.1\|WP_112575676.1\|5186873_5189141_+\|aconitate-hydratase	gnl\|CDD\|273561	TIGR01340, Homocitrate_dehydratase_mitochondrial, aconitate hydratase, mitochondrial. This model represents mitochondrial forms of the TCA cycle enzyme aconitate hydratase, also known as aconitase and citrate hydro-lyase. [Energy metabolism, TCA cycle].	0
NZ_CP043450.1\|WP_112575667.1\|5174365_5174863_+\|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.	1.51188e-17
NZ_CP043450.1\|WP_112575669.1\|5175638_5177663_+\|excinuclease-ABC-subunit-UvrB	gnl\|CDD\|235395	PRK05298, PRK05298, excinuclease ABC subunit UvrB.	0
NZ_CP043450.1\|WP_112575670.1\|5177929_5178184_+\|DUF4834-domain-containing-protein	gnl\|CDD\|374375	pfam16118, DUF4834, Domain of unknown function (DUF4834). This family consists of uncharacterized proteins around 90 residues in length and is mainly found in various Parabacteroides and Bacteroides species. Protein in this family are characterized by a strongly conserved KDEGEYVD motif on the C-terminal and a very divergent N-terminal. The function of this family is unknown.	1.31039e-05

>NZ_CP043450.1|WP_112575675.1|5183321_5186507_+|peptidase-S41
MKKLYIVLFSAVLCQTNLKAQTAGNYFTSNPTLTPDGKTVIFTYEGDLWKADINSPAATRLTAMQGDESNPRVSPDGQWLAFSSNQFGNNDVYVMPLAGGDIKQITFNDGADNVDSWTWDSKSIYFNSTRYNGFSEYKVAATGGTPVRLFGHYFNTIHGVVEHPQTGELFFSNTWESIYFPTRKHYKGAYNPDIQSYNPKTKAYKKYTDWQGKDFWTTIDQKGNIYFVSDEGNEEYNLYTFIDGKKTPLTQFPTSIKRPQVSADGSKVVFEKDYQIFVYDVASKQTQKLSLNLFRNNVLPKDQSFETGGKIGAADLSPDGKKLAFVSRGELFVSDAEGKFIKKLERNTSERVTEVEWLNDNKTLIFGQTLGGFPNWYTIAADGTGEEKQLTTDKGSNRMLSMNKDRSKAIYLSGRNELKLLDSKTLTSKTIVTDEFWGFENLAPRFSPNGEYVVYNAYRNFEMDVFVYEIKTGKIINLTNSGVTEAAPFWSPDGKYIYFTSSRTQPEYPYGSKDSHIYRMPLQKYDDPFKMDKFTALFKEEKKDDDKDKKDKDKKASNKKKPLSEQPTPKAPDDITIDTEEPMKRLERISPEFGQAQGSYVIQKGDKTLVYYASNHSEGKAALYRTTLENFEQPKTEKVGSGDFGSFDIFGNSDKYFLLAGGNIYTLNIDANKVDKVEINYSFTRNMAGEFAQMFDETWAGLDENYYDGNFHGADWKKVHDTYKAFVPYINNRSDLRLLLNDMLGELNSSHQGFYSNGSEEKKTLSYRTMETGIIFDNDSPYKVSGIATRSNADKAGVDVKSGDILKAVNGVTVDEKQDRNYYFSKPSLDKEIELTFNRGGKEIKVKLHPESTGDLSGNLYDDWIKTNAKTVAEKSKNRIAYSYMKNMGDGALEDFLEDMVDDAYNKDALILDLRYNTGGNVHDNVLKFLSQKPYLQWAYRDGKKAQQSNFAPAAKPIILLMNEQTLSDGEMTSQGFKQLGLGRIIGTETYRWIIFTSGKGLVDGSFYRIPAWGCYTLDGKDIEKTGVTPDIYVKTDFADRLENKDPQLDRAIEEILKQLK
>NZ_CP043450.1|WP_112575674.1|5182000_5183284_-|glycosyltransferase
MLKVVHLNTYDGNGGAGRACMRLNRALLSQNINSKIIVHYKFGNNPDIKTFNRSIIQKSYAAATIILERILAKRFLKPDSRTPFSFTWFGRSVIKHPDLKNADVIHLHWINHGFLDPKHLAEIKKLGKPVVWTFHDSNAFTGGCHVRYTCDHYQQQCGNCPLLINAGDNDISHRIWQQKNKAYQQLGFNIIAPSLWMQASVNKSSLMQGRAVSNIPNTLETDIFKPIDKKLAKQQAGLPTDKFIFLSGFMPSRKDLHKGTQYLLESMELLRQRLGADTDQIELVVFGNRGTENLPDFPFKTSFLGTINNDEKLALHYAAADAFLIPSLEDNLPYTVMESLSCGTPVIAFTTGGIPDMVQHQYSGYLATYRSSESFTDGMEWIIKHPEKDKLNQQARQAIMDNFSEDVIAKKHVEVYQQLLNNGGNNV
>NZ_CP043450.1|WP_112575673.1|5181255_5182008_-|glycosyltransferase
MSNPRLSVITIVYNNVRDIERTIRSVVNQTYPNIEYVIVDGLSNDGTLQVIDRYKSQITKFISEKDEGIYDAMNKGLALATGDYVIFMNSGDEFYDRETVAAVFASADDADIYYGETEMIDDDGHSLGQRRHKAPAKFTWRGFKYGMSISHQAIYIRRSLAEPYDRRYQLSSDIDWIIRAAKKAKNIVNVNRYVAKYLVGGMSKKKHRQSLMERFDIMKRNYGLIPTVFNHVVIAFNLAWYWLKNRRTND
>NZ_CP043450.1|WP_112575672.1|5178579_5181057_+|hypothetical-protein
MNNWFKRNGIHFAIAAIFLVICFIFLTPAFQGKTLGGNDVTRAQSTQKEINDYKAKDTTILWTNQIYGGMPTYQVWAPYKANLTTWVVSAINYTFPTPVGTVLLFLLGTYFLFIVLKVNPWLAAAGAVAFTFSSYNIILLVAGHANQAFAIAFFGPILAGIILTLRGKHLLGFSVTALFLALEIRANHIQMTYYLMLALLIMVGIELYHAIKNKTLNDFLKSLGYVAAAVLLAVAVNASILWSTADYGNETIRGKSNLTRQAAEPNNGLARDYAYEWSQGVGECITFLIPNAYGGGEQGSTDPDSHVIKTLGASGADPNQVAGISANYLPLYWGNKPFTAGPFYFGAVICLLFVWGLMIVKNRIKWWLLGAVVLTMLLSFGRNWPYLSDLFFNYFPLYNKFRAVESILAVAGFCFPILAVLAVNEAIVNEDKANLFKKLKIAFYITGGIVLIVAAVPSLLLSFSVSEQQAGVIAQIGQALKTDSSAITRALIADRESMAQADAIRSLIFLAVAFGIAWAFLKKKINPTVASLAFLALILVDLWGIDKRYLNHDSFAPKQDNETPQPREVDQFIMKDKDPDFRVFDVTQSIKGDGLTPFFYKSLGGYSAARLKRWEELVDNQLSKSINQDVLDMMNVKYIINSDPKTQNVGMQVNQTACGHAWFVKSIKYADNADQEMVAISSFTPKDEAIVDKQYKSIIDEKTLGAGAGEGKIELTSYSPDHMVYQSGSTASQIAVFSEVYYNKGWKMYIDGVEKPYFRADYLLRAAQIPVGNHKIEFIFHPASYYTGENISLAGSILLVLALGGAAYTENKKKTPAAKPADKKA
>NZ_CP043450.1|WP_112575671.1|5178200_5178494_+|hypothetical-protein
MDTNPVFNRRHNHNNTPASVTLIITNFIVFGLSTQMFTSCAGINTFFWVVLAALAVYNYFTIRKYREDYDKPQVIAYVVSLVVMIGLYFVLRYAQHC
>NZ_CP043450.1|WP_112575670.1|5177929_5178184_+|DUF4834-domain-containing-protein
MILIRFLIISICILYIVRSLARYLLPFLFESVVNKAQQQYQQQQRNYNEGPKPDGKVRIDHIPQPKKGSVPDSEGEFVDYEEVK
>NZ_CP043450.1|WP_112575669.1|5175638_5177663_+|excinuclease-ABC-subunit-UvrB
MDFQLTSQYKPTGDQPEAIRQLVEGINNGDQYQTLLGVTGSGKTFTVANIIAQTQKPTLILSHNKTLAAQLYGEFKQFFPENAVNYFVSYYDYYQPEAFIPTTNTYIEKDLQINEEIEKLRLRTTSALMSGRRDVIVVSSISCIYGMGNPDDFADSVFKFAVGTRISRNAFLHRLVEILYARTTADFKRGTFRVKGDTVDIFPAYLDYAYRISFFGDDIEELSTFDIGTGKTLEKMTHMVVYPANLYVAPRERFLQSIWAIQEELETRKKQFIDDGRFLEAKRLEERVNYDLEMIRELGYCSGIENYSRFFDGRKPGARPFCLLDYFPEDYLMVIDESHVTVPQIRAMYGGDRSRKISLVDYGFRLPAALDNRPLNFQEFENLAPQTVYVSATPGDFELEKSGGVVVEQVIRPTGLLDPVIDVRPVINQVDDLLDEVDKTIKKGDRVLVTTLTKRMAEELAKYMDRLGIKCRYIHSEVKTLQRVEILRGLRLGEFDVLIGINLLREGLDLPEVSLVAILDADKEGFLRSERSLIQTIGRAARNDRGRVIMYADTITDSMQITMDETNRRREIQIAYNTLHGITPLTVGKTREEIMEQTSVVDFKGGVQQAYVETDTVTLAADPIVQYMTKADLKKSIDNTKKDMLAAAKNMDFLLAAKLRDEMFALEKMMEEKF
>NZ_CP043450.1|WP_112575668.1|5174873_5175353_+|MarR-family-transcriptional-regulator
MNVIDESGILAISTRLQRLAEQLRKEGVLIYKANNIEFEPKWFPVIYTLHFKPMLSVVEIAAEIGYTHPSTISLLKELEKEKLIRSKKDKADERKRLITLTTKGQELIERMKPVWEIIKAAAAEIADTQNNLMKAITEAEEKLKQQSFLDRALRLKAKM
>NZ_CP043450.1|WP_112575667.1|5174365_5174863_+|GNAT-family-N-acetyltransferase
MNTTPVISSLNNTYCQQIIDIILPIQQIEFNVPITLEAQPDLLDIESNYHQTGGNFWGATYNEQLVGTIALIAFGDNAAAIRKMFVLKEYRGKELGIAQLLLDNLIAYCRQNNITSIYLGTVEVLKAAHRFYERNGFTRLAKHDLPESFPLMAADTIFYELHLNN
>NZ_CP043450.1|WP_112575666.1|5173588_5174233_-|uracil-phosphoribosyltransferase
MIFVLNKTDTIANQFLAELRDAVIQQDKERFRRNQERLGAILAYELSKSLHYETKEIQTPLGTASVNMLADEPVLGIILRAGLPFHHGFMQFFDQASSAFITAYRKVKRNGSFLIQVDHIATPNLDDKIFILCDTMLATGQSVVAVCKELMAQYSIKELHIAAVIASTEGVAHVKANLPKAKIWVCAVDDEMTSKAYIVPGLGDAGDLAFGEKA
>NZ_CP043450.1|WP_112575676.1|5186873_5189141_+|aconitate-hydratase
MAFDLDMIKKVYDRYSTRVDAARKATGKPLTLTEKILYAHLSEGDAQKAFGRGVDYVDFAPDRVAMQDATAQMALLQFMQAGRPQVAVPSTVHCDHLIQAKIGAVEDLSTAVDVNREVYDFLASVSDKYGIGFWKAGAGIIHQVVLENYAFPGGMMIGTDSHTPNAGGLGMIAIGVGGADACDVMAGLPWELKFPKLIGVKLTGKLSGWTSAKDVILRVAGILTVKGGTGAIVEYFGEGARSMSATGKGTICNMGAEIGATTSIFGYDEKAAAYLKGTKRADIAELADAIAEHLTGDDEVYANPEQYFDQVIEINLSELEPHVNGPFTPDLAWPISKFATAVKENGWPTKLEVGLIGSCTNSSYEDITRSASIAKQAIDKKLKTQAEFTITPGSEQVRYTVDRDGYLDTFAQMGGVVLANACGPCIGQWARHTDDPTRKNSIITSFNRNFAKRQDGNPNTHAFVASPEIVTAFAIAGDLTFNPLTDTLTNEAGEQVKFDEPQGIELPVKGFAVEDAGYQAPAEDGSKVEVIVSPTSSRLQLLEPFKAWEGTDITGLKLLIKAKGKCTTDHISMAGPWLKFRGHLDNISNNMLIGAINYFNLTADSVKNELTGEYGPVPATQRAYKAAGIGSIVVGDENYGEGSSREHAAMEPRHLGVRAILVKSFARIHETNLKKQGMLGITFADNNDYDKIQEDDTIDITGLTTFAPGKQLTVVLHHKDGSTESFPVNHTYNAQQIEWFKAGGALNIIRKQMAS
>NZ_CP043450.1|WP_112575677.1|5189512_5191432_-|glucosamine-6-phosphate-deaminase
MARLNLLEETRYEKLPVSVYNNQQEASVAVANRIADLIRSKQAKGEKAVLGLATGVTPIGVYAELVRQHKEAGLSFKNVITFNLDEYYPMKPTAAQSYVTFMYENLFSHIDIEKENVHIPDGTLDKDEVVAFCLAYEKQIEELGGLDLQILGIGRTGHIGFNEPGSAPNSGTRMVTLDDLTRRDAARDFGGKADVPTKAITMGIGTIFKAREIILMAWNKKKAPIIKKAVEGEISGEVPATYLQLSQHVEFVLDADAASELTRFDTPWLVKDCVWENTLKKKAVIWLANEVNKPVLKLTEEDYNNHGMAQLAVEQGPVYNINIDIFNQIQHTITGWPGGKPDADDSQRPERALPAKKRSIIFSPHPDDDVISMGGTFIRLVDQGHDVHVAYQTSGNTAVWDDDVLRYMEFAIDFTNSIGEDTTHLQKSYEDMRAFFPTKQPNEIDTQEIRNVKGFIRKTEAISGARYAGLQDDHIHFMALPFYETGKTKKNSVGEEDIQLTIELLQKIKPQQIFAAGDFADPNGTHLVCFKIILAALDRLKGKEAWVEDCWLWMYRGAWHEFETYEIEMAVPLSPQEVIRKRNAIFKHQSQKDTPVFPGDDAREFWVRAEDRTRDTAQRYDRLGLAEYEAMEAFVRYKF
>NZ_CP043450.1|WP_112575678.1|5192176_5194741_-|hypothetical-protein
MIKKSKVLMLSKRAYKLVLLFVLLLPAMKGMGQGLQFGSNDSLMSKRTSYQVFKEDLPTFHDRLVIGFDLSLWDNQHLGYILNLTDDKGNSYSLSAIYDQGSFLNFNIDSRSNKLNIPLANALLKRRKWFKVIVDLDLKDDKVGISVNGKWYRANELGFTGKIKAKITFGKNEHYSDVPNMAIKNLVVSNDDKTYTFPLNEWAGNDVFNSDGDNLGYVDNPAWLINESYYWKQKFVHTFNEVAGINFNEKNEQFFIFKSDSLMFYDAERDAVWSKPFKSKLEVPLHLGKSIVNLKENKCYLYEVLRASQPAPSIASFNLDSLNWDYYGKSTIMEQRHHHNIFYDKDFNNFYLFGGYGSFKYYNNFFKYDKATDNWQKQSFTGDVINPRFFSAASTADQNNDVYIFGGYGNQSGNQVVGGMHYYDLYRVNLGNHTIKKLWEIKPDEEAFVPANNLIVSKDKQFLYVLCYPHERPKTSLRLYKFSIKDGSYQVVSGTIPVVSERIETDHNLFYNAKQDVFYCTTQEFETPSRSTIKIFALSAPPVSQAEFTAAHQPKSKSFTLYRVLGGASALILLGGVVAFFLRRKKADDESAPAAPEEIIVEEVTEAVVDNKANAVYLLGEFTVFDKNKRDITYLFSPKIKQLFILILLNSREKNGVVSKKISTTLWPDKDVVKTKNIRGVTINHLRNILSDIEGLELAFLNDTYSFIITEGFYCDYFVVRDSLKQAGNVEPAVFNSFDLVSRGGLLQHIPEIWLDDFKQDYEEALMPVILPVIKKVYDAQDYKKALEISRVVLNIDPFNDIGIKFKLKALRRTKGIEHARKIYEEFSAEYEKSLGEEYPVPFEKICSNKSDQR
>NZ_CP043450.1|WP_112575679.1|5195124_5196471_+|TolC-family-protein
MPIKVKHIITFFFLLAVGSQLRAQDSTLVGQSLKWDLAKCIDYAKKNNIQINSLRLSQQTSQQEYLLAKAARLPDLSATGSQTFAHGNNFSNGDNGRHSGYNVSGSYGLSSNVTLYNGSYINNNISQKNLQVQSANLSILQQENDIVLQITQAYLTVLLDKESVIYNTDLLSTTQAQVKLQQQRYNVGSVARKDLIQLQAQQATDQYTLVNSQNAVRNDLLTLKQLLVLPTDLSFDIMKPDTVMAPIDSVSSFPEAEQTALQNRPEVKNGELGVKIAQFDVDKAKAGYKPTLTAGASLNTGYANGQGVSFGNQINNNFYQQLGVNLSIPIFTKRVVKTQVEEAKINVKQSQLDLKNTKITLSQTVERAYINVQNARSQFSAAAEEYKFSKESYRIASEQLKVGVANTVDFLLQKNLFVQAQQSFVQAKYNALLTLKIYDFYRGVPITL
>NZ_CP043450.1|WP_112575680.1|5196483_5197809_+|efflux-RND-transporter-periplasmic-adaptor-subunit
MKSSYKKILIIAGIVVALVLIWFLFIRKKEEPVVLQTQKPAKGYIAQSVTATGRIEPVDTVTVGTQVSGIIKYVYADFNSKVKKGQLIAELDKSLLQATLDQARGTLLNAQSQLVFAQNNFGRQNLLFKTDAISKADYDTALNTLNAAKAQVKSAEAQVRSAEKNLSYADIYSPIDGVVLNRNVSVGQTVAASFSTPTLFVLAKDITKMEVEANVDEADIGDVKSGDRASFTVDAFINDQFAGTVEDIRLHPSVSSNVVTYTTIINAPNDDMKLKPGMTASIIIYTKEVNNALLIPAKALSFTPDSALMKDYEIVGKVGHKGNKKRSGGQGGNAPAGSAGNGGANDNSQALHTAKSRKDSSGVNKQTAIVWVLQGKKIVRKKIQTGLNDNTQVEVLSGLTVDDAVITGVTGGSSSSSTAAAKPGASPFMPQRPRGGGGGRR
>NZ_CP043450.1|WP_112575681.1|5197808_5198558_+|ABC-transporter-ATP-binding-protein
MSKKILDIRELKREFQMGSETVRALKGISFEVEAGEFVTIMGSSGSGKTTLLNILGCLDKPSIGDYFLDGVDVKKLSRDELAQLRNRKIGFVFQAYNLLPRTSALENVELPLLYNKEISVSERRDRAIHALEAVKLAERLDHTPSQLSGGQQQRVAIARALVNEPVMILADEATGNLDSRTSYEIMSLMQELNSQQGKTIVFVTHEPDIASFSSRTIQLRDGRIQKDTQNANKRSAKEVLAGLPITDDY
>NZ_CP043450.1|WP_112575682.1|5198570_5199788_+|FtsX-like-permease-family-protein
MNFFNLIRIAYKALQRNKLRAFLTMLGIIIGVASVIAMVAIGQGSKQSIHDQLSSMGSNMITVLPSSNLNGGVRIAGSSFQTLTQKDIVALKKAQYITELSPSITSKGQAINGALNWPTSIQGVSPDYLDIRKLSLKDGIAFTEEDILTSAKVCLIGQTVIDNLFPNGENPIGKVIRFNKIPFQIIGILNPKGQNAFGQDQDDILIAPYTTIQKRILATIYYQNIYASAASEQVTDAAVSEMTQILRDSHRLRDSEDNDFTVRTQAELINTLSSTSGLLTVLLTVIAGISLVIGGIGIMNIMYVSVTERTREIGLRMSIGARGKDIMLQFLMEAILISITGGIIGVVLGIVSSNLVTLTLSWPTIVSESSVLLSFVVCAITGIFFGYYPAQKAARLDPIEALRYE
>NZ_CP043450.1|WP_112575683.1|5200078_5202880_+|outer-membrane-beta-barrel-protein
MKITFIGILLLCLSWTTSFAQTGYSIKGKVADTVANTNLINASVSVITAKDSILQKFTRIKDDGTFTINNLNKGKFILVATYPGYADFVEHFALDSAHTTHNFGRISMLLKERLLQEVIVKGKAAAIKIKGDTTEFNPAAYNIQPNSKVEDLLKQLPGIEVDKDGKITAQGQTVKKVLVDGEEFFGDDPTLVTKNLRADMVDKVQLYDKKSDQAAFTGIDDGVKDKTINIKLKEDKKNGYFGKLDGGIGTDGYYQGQALFNRFKGKQKFSVYGTLGNTGKTGLGWEDNNKYGGGGGMEFGDDGGFYIFGGGDDLDSFDGRYNGEGKPVARTGGAHYDTKWNNDKESINTNYKIGSLTVDGTKNTQQQNNFPGNISNVNSDQSNHNYMFRQKLDVNYQVKIDSMQNLKITADGTLKNSNTRSNFATQTRRLDGSLINSNDRENSANVDGKVFNANAFYTKKFKKKSRTLSVNFRTAYNESDSKGFLKSNTQFYDSVGTYVNKDTIDQYKVNKTKSTNINTNITYTEPLAKDFTLALSYALAVNNATADRRTFNKPVSSAAIYTALDSVYSSDYKLNQLSNQGGAVFNMQKQKYSFNFGTKVASVKFKQVDEFGRISDLVRNFTNWYPQASFQYKFSKQSSIRVSYNGNTTQPNIDQIQPVRINTDPLNIQEGNADLKPSFTNRYNISYNSYKVISNQYIWISGSYSTTSNPIVSNVMRDTTTGISTYKSSNLKNKSTNNFWVNTYFERKIPGIGINAGLEVYANGNTYYNMSNDVLNETKSYSYSGSVRLSKYKEKKYDAWVSAGPTYTINSSSLNTVLNNNGRGFNANGGFNIYLPGKFQIGSDGNYTYNAPTKSFPQDFKRFLWNANISRTFFKDALKASVTGNDLLNQNTGYNRTGSANVLTQERYTTIRRYFMFSLTWDFNKVGGGAPKK
>NZ_CP043450.1|WP_112575684.1|5202886_5203666_+|GLPGLI-family-protein
MKKILTLTTILFLSANLLLAQGNKHFTFHGTIEYDKSSNMWAMLQKLINKDNESWYQPMFDQYKKNKPQFKVLKSTLKFADNQTLFTPIEPEYTPNNFGDELPMAVQNNTIFTDYNTGISTSQKKVFEETFLVKDTTRHIKWKLTGESREIAGYNCRRANGLILDSIYVVAFYTDEIPVSGGPESFNGLPGMILGVALPHENITWFATKVTEQPVDEKSFMAPKKGKAGNNKSFLTVLQNAMKDWGETYAKQYLKGFSL
>NZ_CP043450.1|WP_112575685.1|5203897_5204686_-|SDR-family-oxidoreductase
MNLQLTDKVIIVTGGAKGIGEGIVKVLAAEGAIPVVLGRNEADNLKTVEAVEAAGHKAHQVVAELTEPSACEKAVKEVVAKFGRIDGLVNNAGVNDGVGLESGDYEGFMASLHKNVVHYYLMAHHALPELKKSKGAILNITSKTADTGQGNTSGYAASNGGRNALTREWAVELLKYGIRVNALVVAECWTPLYANWIKTLPDPEAKLREIESKIPLGNRMTTAEEIANTVAFLLSPASSHTTGQLIYVDGGYVHLDRALANA

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Crispr_ID: NZ_CP043450_8

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043450_8

5627389-5627503

Orphan

Consensus_repeat	Method
GAAGTCCGCAGTCAGAAAGTCCGAAAGAAAT	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043450_8

>merge|NZ_CP043450|8|5627389-5627503|CRISPRCasFinder
GAAGTCCGCAGTCAGAAAGTCCGAAAGAAATAAGCATTGCTTAGTCTTTCGGATTTTACTTTTTAAATGAAATAGCTTCAAACAGAAGTCCGCAGTCGGAAAGTCCGAAAGAAAT

>NZ_CP043450|8|8|5627389-5627503|CRISPRCasFinder
GAAGTCCGCAGTCAGAAAGTCCGAAAGAAAT	AAGCATTGCTTAGTCTTTCGGATTTTACTTTTTAAATGAAATAGCTTCAAACA
GAAGTCCGCAGTCGGAAAGTCCGAAAGAAAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043450.1\|WP_112568828.1\|5640852_5641953_-\|phytase	unknown	unknown	gnl\|CDD\|226698
NZ_CP043450.1\|WP_112568830.1\|5642012_5643266_-\|right-handed-parallel-beta-helix-repeat-containing-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112568822.1\|5635208_5637665_+\|TonB-dependent-receptor-plug-domain-containing-protein	unknown	unknown	gnl\|CDD\|274948
NZ_CP043450.1\|WP_112568805.1\|5619507_5620263_-\|lipoyl(octanoyl)-transferase-LipB	unknown	unknown	gnl\|CDD\|319743
NZ_CP043450.1\|WP_112568799.1\|5616430_5617858_+\|L-serine-ammonia-lyase	unknown	unknown	gnl\|CDD\|273233
NZ_CP043450.1\|WP_146749986.1\|5624577_5627379_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|376626
NZ_CP043450.1\|WP_112568824.1\|5637651_5638968_+\|carboxypeptidase-like-regulatory-domain-containing-protein	unknown	unknown	gnl\|CDD\|372685
NZ_CP043450.1\|WP_112568808.1\|5620262_5620904_-\|4'-phosphopantetheinyl-transferase-superfamily-protein	unknown	unknown	gnl\|CDD\|225002
NZ_CP043450.1\|WP_112568820.1\|5633090_5634920_+\|ABC-transporter-ATP-binding-protein	unknown	unknown	gnl\|CDD\|224055
NZ_CP043450.1\|WP_112569045.1\|5618788_5619445_-\|SGNH/GDSL-hydrolase-family-protein	unknown	unknown	gnl\|CDD\|238870
NZ_CP043450.1\|WP_112568801.1\|5617863_5618325_-\|RES-family-NAD+-phosphorylase	unknown	unknown	gnl\|CDD\|378053
NZ_CP043450.1\|WP_112569047.1\|5628892_5629366_+\|histidine-phosphatase-family-protein	unknown	unknown	gnl\|CDD\|132716
NZ_CP043450.1\|WP_112569049.1\|5640164_5640725_+\|thioredoxin-family-protein	unknown	unknown	gnl\|CDD\|379658
NZ_CP043450.1\|WP_112568810.1\|5621115_5621652_+\|dCTP-deaminase	unknown	unknown	gnl\|CDD\|234753
NZ_CP043450.1\|WP_112568812.1\|5621780_5624498_+\|TonB-dependent-receptor-plug-domain-containing-protein	unknown	unknown	gnl\|CDD\|274948
NZ_CP043450.1\|WP_112568797.1\|5615609_5616353_+\|RDD-family-protein	unknown	unknown	gnl\|CDD\|377640
NZ_CP043450.1\|WP_112568816.1\|5628516_5628798_+\|ATP-dependent-Clp-protease-adaptor-ClpS	unknown	unknown	gnl\|CDD\|376861
NZ_CP043450.1\|WP_112568818.1\|5629418_5630948_-\|acetylxylan-esterase	unknown	unknown	unknown
NZ_CP043450.1\|WP_112568803.1\|5618321_5618729_-\|DUF2384-domain-containing-protein	unknown	unknown	gnl\|CDD\|131346
NZ_CP043450.1\|WP_112568826.1\|5638974_5640003_-\|hypothetical-protein	unknown	unknown	gnl\|CDD\|311610

Protein	Function_ID	Function_description	E-value
NZ_CP043450.1\|WP_112568828.1\|5640852_5641953_-\|phytase	gnl\|CDD\|226698	COG4247, Phy, 3-phytase (myo-inositol-hexaphosphate 3-phosphohydrolase) [Lipid metabolism].	4.4184e-45
NZ_CP043450.1\|WP_112568822.1\|5635208_5637665_+\|TonB-dependent-receptor-plug-domain-containing-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].	1.23243e-08
NZ_CP043450.1\|WP_112568805.1\|5619507_5620263_-\|lipoyl(octanoyl)-transferase-LipB	gnl\|CDD\|319743	cd16444, LipB, lipoyl/octanoyl transferase. Lipoate-protein ligase B is a octanoyl-[acyl carrier protein]-protein acyltransferase the catalyzes the first step of lipoic acid synthesis. It transfers endogenous octanoic acid attached via a thioester bond to acyl carrier protein (ACP) onto lipoyl domains, which is later converted by lipoate synthase LipA into lipoylated derivatives.	1.0914e-93
NZ_CP043450.1\|WP_112568799.1\|5616430_5617858_+\|L-serine-ammonia-lyase	gnl\|CDD\|273233	TIGR00720, hypothetical_protein_NEICINOT_00681, L-serine dehydratase, iron-sulfur-dependent, single chain form. This enzyme is also called serine deaminase and L-serine dehydratase 1. L-serine ammonia-lyase converts serine into pyruvate in the gluconeogenesis pathway from serine. This enzyme is comprised of a single chain in Escherichia coli, Mycobacterium tuberculosis, and several other species, but has separate alpha and beta chains in Bacillus subtilis and related species. The beta and alpha chains are homologous to the N-terminal and C-terminal regions, respectively, but are rather deeply branched in a UPGMA tree. This enzyme requires iron and dithiothreitol for activation in vitro, and is a predicted 4Fe-4S protein. Escherichia coli Pseudomonas aeruginosa have two copies of this protein. [Energy metabolism, Amino acids and amines, Energy metabolism, Glycolysis/gluconeogenesis].	0
NZ_CP043450.1\|WP_146749986.1\|5624577_5627379_+\|hypothetical-protein	gnl\|CDD\|376626	pfam01835, A2M_N, MG2 domain. This is the MG2 (macroglobulin) domain of alpha-2-macroglobulin.	0.000284513
NZ_CP043450.1\|WP_112568824.1\|5637651_5638968_+\|carboxypeptidase-like-regulatory-domain-containing-protein	gnl\|CDD\|372685	pfam13715, CarbopepD_reg_2, CarboxypepD_reg-like domain. This domain family is found in bacteria, archaea and eukaryotes, and is approximately 90 amino acids in length. The family is found in association with pfam07715 and pfam00593.	4.42965e-18
NZ_CP043450.1\|WP_112568808.1\|5620262_5620904_-\|4'-phosphopantetheinyl-transferase-superfamily-protein	gnl\|CDD\|225002	COG2091, Sfp, Phosphopantetheinyl transferase [Coenzyme metabolism].	4.19134e-18
NZ_CP043450.1\|WP_112568820.1\|5633090_5634920_+\|ABC-transporter-ATP-binding-protein	gnl\|CDD\|224055	COG1132, MdlB, ABC-type multidrug transport system, ATPase and permease components [Defense mechanisms].	2.69783e-94
NZ_CP043450.1\|WP_112569045.1\|5618788_5619445_-\|SGNH/GDSL-hydrolase-family-protein	gnl\|CDD\|238870	cd01832, SGNH_hydrolase_like_1, Members of the SGNH-hydrolase superfamily, 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 from other serine hydrolases, but may lack the carboxlic acid. Myxobacterial members of this subfamily have been reported to be involved in adventurous gliding motility.	1.02173e-34
NZ_CP043450.1\|WP_112568801.1\|5617863_5618325_-\|RES-family-NAD+-phosphorylase	gnl\|CDD\|378053	pfam08808, RES, RES domain. This presumed domain contains 3 highly conserved polar groups that could form an active site. These are an arginine, glutamate and serine, hence the RES domain. The domain is found widely distributed in bacteria. The domain is about 150 residues in length.	4.88936e-26
NZ_CP043450.1\|WP_112569047.1\|5628892_5629366_+\|histidine-phosphatase-family-protein	gnl\|CDD\|132716	cd07040, HP, Histidine phosphatase domain found in a functionally diverse set of proteins, mostly phosphatases; contains a His residue which is phosphorylated during the reaction. Catalytic domain of a functionally diverse set of proteins, most of which are phosphatases. The conserved catalytic core of this domain contains a His residue which is phosphorylated in the reaction. This set of proteins includes cofactor-dependent and cofactor-independent phosphoglycerate mutases (dPGM, and BPGM respectively), fructose-2,6-bisphosphatase (F26BP)ase, Sts-1, SixA, histidine acid phosphatases, phytases, and related proteins. Functions include roles in metabolism, signaling, or regulation, for example F26BPase affects glycolysis and gluconeogenesis through controlling the concentration of F26BP; BPGM controls the concentration of 2,3-BPG (the main allosteric effector of hemoglobin in human blood cells); human Sts-1 is a T-cell regulator; Escherichia coli Six A participates in the ArcB-dependent His-to-Asp phosphorelay signaling system; phytases scavenge phosphate from extracellular sources. Deficiency and mutation in many of the human members result in disease, for example erythrocyte BPGM deficiency is a disease associated with a decrease in the concentration of 2,3-BPG. Clinical applications include the use of prostatic acid phosphatase (PAP) as a serum marker for prostate cancer. Agricultural applications include the addition of phytases to animal feed.	0.000174986
NZ_CP043450.1\|WP_112569049.1\|5640164_5640725_+\|thioredoxin-family-protein	gnl\|CDD\|379658	pfam14595, Thioredoxin_9, Thioredoxin.	8.43987e-50
NZ_CP043450.1\|WP_112568810.1\|5621115_5621652_+\|dCTP-deaminase	gnl\|CDD\|234753	PRK00416, dcd, deoxycytidine triphosphate deaminase; Reviewed.	3.53889e-65
NZ_CP043450.1\|WP_112568812.1\|5621780_5624498_+\|TonB-dependent-receptor-plug-domain-containing-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].	5.85426e-08
NZ_CP043450.1\|WP_112568797.1\|5615609_5616353_+\|RDD-family-protein	gnl\|CDD\|377640	pfam06271, RDD, RDD family. This family of proteins contain three highly conserved amino acids: one arginine and two aspartates, hence the name of RDD family. This region contains two predicted transmembrane regions. The arginine occurs at the N-terminus of the first helix and the first aspartate occurs in the middle of this helix. The molecular function of this region is unknown. However this region may be involved in transport of an as yet unknown set of ligands (Bateman A pers. obs.).	3.10244e-16
NZ_CP043450.1\|WP_112568816.1\|5628516_5628798_+\|ATP-dependent-Clp-protease-adaptor-ClpS	gnl\|CDD\|376861	pfam02617, ClpS, ATP-dependent Clp protease adaptor protein ClpS. In the bacterial cytosol, ATP-dependent protein degradation is performed by several different chaperone-protease pairs, including ClpAP. ClpS directly influences the ClpAP machine by binding to the N-terminal domain of the chaperone ClpA. The degradation of ClpAP substrates, both SsrA-tagged proteins and ClpA itself, is specifically inhibited by ClpS. ClpS modifies ClpA substrate specificity, potentially redirecting degradation by ClpAP toward aggregated proteins.	5.65729e-21
NZ_CP043450.1\|WP_112568803.1\|5618321_5618729_-\|DUF2384-domain-containing-protein	gnl\|CDD\|131346	TIGR02293, conserved_protein_of_unknown_function, putative toxin-antitoxin system antitoxin component, TIGR02293 family. Proteins in this family are found almost exclusively in the Proteobacteria, but also in Gloeobacter violaceus PCC 7421, a cyanobacterium. This family was proposed by Makarova, et al. (2009) to be the antitoxin component of a new class of type 2 toxin-antitoxin system, or addiction module. [Cellular processes, Other].	1.32102e-14
NZ_CP043450.1\|WP_112568826.1\|5638974_5640003_-\|hypothetical-protein	gnl\|CDD\|311610	pfam07745, Glyco_hydro_53, Glycosyl hydrolase family 53. This domain belongs to family 53 of the glycosyl hydrolase classification. These enzymes are enzymes are endo-1,4- beta-galactanases (EC:3.2.1.89). The structure of this domain is known and has a TIM barrel fold.	4.44018e-98

>NZ_CP043450.1|WP_146749986.1|5624577_5627379_+|hypothetical-protein
MKYLRAVPLLVLLLLNLKSFAQTDSSFLKKAVALSNKQLTDKPTEKVYLHLDKPFYNITDTIWFKVYTVTGAEHQLSDISGVVHVELINAKDSVARRINLKLTNGVAWGDFVLPGNYKAGSYRLRAYTNWMRNQGTVAMFDQRIQVNGRPVFGANQPQNQPATENKTDVQFFAESGSLVNGLRSKIAVKVIGQNGLGRDAKGSITDNDGNEVAEFETTHLGMGIFALLPQAGKTYKAKITTDGIPPFTVDLPKAGDEGFTMTVNNRLTDSINIKLTASSKTLGTKQHAYYYLVGQSGGKVYYTTSFKLEDPGYSFKIEKKRFPSGIAQFTLFGADAEPLNERIAFIRANDTLKLKLNIAAQKLATRNAVSVVMEAANNASKPVIGAFSVSVINESRIPFNQNAESTILNNLLLTSDLKGYIEQPNYYFNNITDKTESDLDMLMLTQGYHGFEWRKTLSEKQEQPDFKAEKSLSLAGALQTPGGKPIPNGKVTLLGNRENFYADTVTNLNGDFKFEDVDVSDTSHLLVQARKQNDGKNVTIFVKQTDYPKVEKTTTSVSNQIALFSNPQQIFAQYLEQQKADSLKNGVALKEVVIKGKKATAPNEFNRNGTNQVVNVNMAKLRAVKDVSLKTALYTAEPRAHIELGGTYKNDILNGFASSMLVDGTIVDEQQLAFYSVDEIESVQLVFGAGGIKPKFVITTKRYAGTDTTVLKEVNIRSTKTSKANYRGYSAGKLGPAPDQVIMGEKLVGCTKLSDCLRNQIFGVIFDVNGNPINSRDNKKMAILLNGAVLDGSVLNSISAADVYSIEVLRGASYAVAIGSEFPGGALAITTKQGGDNYVTGSSSSSGVITYPFKGFYKARTFYSPKYTAANVNTNIPDYRTTIFWEPNIVTNETGEASFSYFNADTRGIYRVTVEGIDANGNLGRQVYRYKVE
>NZ_CP043450.1|WP_112568812.1|5621780_5624498_+|TonB-dependent-receptor-plug-domain-containing-protein
MNFKRLSVGTLIILLVGTTLAFIKPDDELVTKIVAQLDKWRAEYPQEKVYLHFDKPSYAIGEDIWFKAYVTIGSEHKLSAYSETLNVDLIDDNDSVKRSLKLPLTAGLAAGDFALADSMSEGNYRIRAYTNWMRNQGEAYFFDKTIAVVNGISNKVFTKTAYNYSTLNGKQKVTAVITYTDLNGIPYVNKPVSYEAEINGKSIAKGKGVTDDKGNLTASFTNNSPVAITTGHINTEVKLDDKRTVTKAVPIKTLSNKVDVQFFPESGNLINGIFEKVAFKAVGADGLGVDIKGYIADDQNNQISALGESHFGMGTANFEPESGKTYKAHITYADGSEGIFDLPKAVDNGYVLSVNSMRDDKVFVSIIPGKNAANGTASLSGLTLIAQSGGELCYAGKSKDGATSFSAAIPKDKFPSGIVQFTLFSATGEPLNERLVFIQNPDQLKLAVTSEKQSYKPREKVTINLNAKISQDKPVIGSFSASVIDESKVNTDEANESSIFSTLLLTSDLRGYIEKPNYYFTNVSNETKANLDALMLTQGYHRFEWKQLLAGKFTPIVFKPEKSLEVTGHLKTFGGKPVPNGKVTLFSTAGGTFIIDTVADAEGKFTFKDLVFRDSIKFVIQARTAKDRKNLDITLDKITPQAVGPNKNAPDIQININDGASAYLLNSKKLYDEQVKYGIGNHTIVLKEVVIKEKRENPFKNSANLNGAGNADQTLTSKDLIYGGMLSQVLQGRLNFVTFRNGIPYSTRSPNTPMQIILDGAYVESDFLDNLTPSDVATVEVLRTIGTTAIYGARGSGGVLVITTKRGGGDAVYNKYAPGIATYAPKGYYRAREFYSPKYDDPKTNAQMQDLRSTIYWSPGLITDKDGNTSMSFFNADAKGTYRVIIEGIDADGNLGRQVYRYKVE
>NZ_CP043450.1|WP_112568810.1|5621115_5621652_+|dCTP-deaminase
MILSDKRILEEIEQGHIIIEPFNREYLGTNSYDVHLGKYLATYRNRVLDAKVHNEIDGFEIPKDGFVLQPNTLYLGVTMEYTETHRHVPFLEGKSSTGRLGIDIHATAGKGDVGFCNTWTLEISCAQPVRIYPGMPIGQLIYFVVEGEIETLYNSKANAKYNNPTTRPVESMMWKNKW
>NZ_CP043450.1|WP_112568808.1|5620262_5620904_-|4'-phosphopantetheinyl-transferase-superfamily-protein
MAIAYRQRIDDDTEFALWRIEEEATDLYSQLQLNQQEKDFVESLSNGKRHLHWLGTRVLLRKMLRTDEYIDCKVDEHGKPYLVNLPYHISLSHSFDYAAVMISKTHKVGIDIEQIKQKVERIANKFMRKQELAFIGGRQKIEQLYVCWCAKEAVYKCNGQKEVSFADNILLEPFQFEHHGVVNAQLHKKNNVIDYTVGYMQYEDYMIGYVKGE
>NZ_CP043450.1|WP_112568805.1|5619507_5620263_-|lipoyl(octanoyl)-transferase-LipB
MKNKKVFFQDWGLIDYQQAWDKQESIFSETVKTKIENRNRETAYEAAAKDGGAGVAYDTIEADETFNYLVFCEHPHVYTLGKSGKPEHLLLDEEGLKEKHAVYYPINRGGDITYHGPGQIVSYPILDLDNFFTDIHLYLRTLEEAVILTLADFGLNAGRYEGYTGVWFDADNEKARKICAMGVRCSRWVTMHGLALNVNTDLSYFKNIVPCGIDDKAVTSMQQELGQDVDINEVKKNLKHHISVLFGMEIL
>NZ_CP043450.1|WP_112569045.1|5618788_5619445_-|SGNH/GDSL-hydrolase-family-protein
MPAPVSYNPPSKPVTVIQDTLTYLALGDSYTIGQSVPIDQAFPNQLANQLQGFKVNAPTIIARTGWTTDQLIEAIDKSDVKSNTYDVVTLLIGVNDQYGGLSQENYRVKFEQVLNTAIKFAGGIREHVFVLSIPDYGVTPFAHGNDAVIGPEIDQFNDINREISSNAKVNYVEITGISKLAAHDLSLLADDGLHPSGKMYGMWVDKLKVDVGAVFAKK
>NZ_CP043450.1|WP_112568803.1|5618321_5618729_-|DUF2384-domain-containing-protein
MSTPKPYKFLDDDEVNLTSMVREGISFPYLTKLSNYIHFNIDDWASYLHLSERTIQRYKKENKTFDPIYSEKIVMIELLYKKGIEVFGDENKFYAWMDYQSIPLGGVKPKELLDTAFGINMIRDELGRIEHGILA
>NZ_CP043450.1|WP_112568801.1|5617863_5618325_-|RES-family-NAD+-phosphorylase
MIVYRLSKQAYINDLSGRGAELNGGRWNSKGTAVVYTSSSRALAVLEVAVHTPLGLMPADYFMVTIELPDNSEVFKPAADQLPEKWNSNPLIKATQQLGDSFVKANKYLVMQVPSATVAGDFNYLLNPLHIDFKSVKITATGFFQFDSRLFKK
>NZ_CP043450.1|WP_112568799.1|5616430_5617858_+|L-serine-ammonia-lyase
MQREQISVFDMFKIGIGPSSSHTLGPWRAAQQFVQSLEQQGVLPLVQQVKILLYGSLAKTGVGHGTDIAILLGLSGDDPVTFEVDQVTPKIAHIKSSHQLILGGVLPISFYAEDDLLFLFNESLPYHPNAVTFQAFLSNGKAVSETYYSIGGGFVVKDGASGPAKAEVDLPFPIDTASDLLHWCIKTGLRISEVVAENELAWRSEQETRTGALNIFRALKECIYRGCHTTGQLPGGLNVARRAAKLNARLIGNNKYSNYDEWVAAIRNTGDSFKNTLDWVSCFALAVNEENASFGRVVTAPTNGAAGVIPAVLQYYIAFCEGNTEQKIINFLFTASEIGSIFKKGATISAAMGGCQAEIGVSSAMAAAALTECMGGTQRQVLMAAEIAMEHHLGLTCDPIGGLVQVPCIERNTMGAIKAITASQLALQSNPEKAKVSLDAVVKTMWQTALDMNSKYKETSDGGLAINIPISLPEC
>NZ_CP043450.1|WP_112568797.1|5615609_5616353_+|RDD-family-protein
MQTIAIKTAQNIDIDYEVAGLGERILARLIDYALYLAVYLIYIWTNGSSYHPSVFYSFTLPQILFLIFYGFYDIITELLFNGQSLGKYIMKIKVISLDGGRPRLGQYLLRYIFRLIDFGLTLQIGAIISVAVTENKQRIGDIVANTTLVRTKTRTSIDTLNFVHIEEDYQPVIPEAVMLADSDISLIHEVLNHFNKTADVIFVDRMAERICKQLDITIPPDLTSYKFLVAVLKDHNYYVLNVSPQLI
>NZ_CP043450.1|WP_112568816.1|5628516_5628798_+|ATP-dependent-Clp-protease-adaptor-ClpS
MPTEVQEETFTLEELLAGLKETHRLILWNDDFNTFDHVIHCMMKYLDYSEPQAEKIAWKVHNEGKCAVLEGSFTEMEIYRKILQQEGLTVSVE
>NZ_CP043450.1|WP_112569047.1|5628892_5629366_+|histidine-phosphatase-family-protein
MKLVFIRHAEKPDVGDNLSCAGFNRSLKLPEVLKAKFGLPDHIYVPAMHQGKSTPRSRMFQTISPFAVKYNLTINSNFEEEDDNGMAKELTSKKGTILIVWEHNELKPLLKALGLKVKDLQWPDNDFDSIWIVTFKKGQPSLTQDKEGITPAAGCSF
>NZ_CP043450.1|WP_112568818.1|5629418_5630948_-|acetylxylan-esterase
MKSTTLFFLLTYAIMAKAQNTPPVNFTADQDHQNMMKQLGIKKLRNGPSGDESAPNHANYDESLANPYPDLPEVLTLKNGKKVTTPQMWWKQRRPEIVEDMEREVYGRIPADVPKVTWTVKVTDKERVGFFPVIAKQLIGHVDNAAYPLINVNIEMTLVLPANAKGPVPVLMMFGRSVLPAPAQPPAADLEKINNALKELLVKDHPELKTIFEQYPAYNPIAEQSPFGPAGFPTMKGDPPTASQLIANGWGYVLIDPASIQADNAEGLTKGIIGLVNKGQPRKPEDWGALRAWSWGAARALDYLETEPAIDAKHVGIEGVSRYGKAALVTLAFEQRFAMGLIGSSGEGGAKLHRRNFGEAVESLTGGEYYWMAGNFMKYGAAEATFGVKTVKDIPVDAHELIALCAPRFTFISYGIPEQGDAKWLDQQGSYMATVAAGPVFKLLGAKDLGVSSDYKTEKMPPVNTGLLNGELAWRQHDGGHTDAPNVKYFIAWANKLMGYGKEGADKSK
>NZ_CP043450.1|WP_112568820.1|5633090_5634920_+|ABC-transporter-ATP-binding-protein
MAKTRNIKPEQKISFKERLSALSNLPEFFSLVWQSSPGKTTMSFLLRIIRSAMPVALLYVGKLIIDQVVLLNRHGGSQHELWKLVIIEFLLAILTDGLNRMISLIDSLLGDLFSNYTSMRIMRHAATLDLEQFEDSVFYDKLERARQQTVGRTVLLSQVMSQIQDFISIAFLLTGLLTLNPWLILLLLISIIPSFMGESYFNSQNYALTRSQTPERRELDYVRYLGASDETAKEVKIFGLADFIINRFKTLSDKFYTDNSKLAVRRSAWGTFFSVLGSIGYYVAYGFIIYQTVTGKSSVGTLTFLAGSFRQLSSLMENSLNRFTSVSQGAIYLNDFHEFFEIKPKITVAASPLPFPKPIKQGFTFEDVGFKYNNAESWANRHLNFTLQPGEKIALVGENGAGKTTLVKLLARLYDPTEGRILLDGTDLRNYDIADLRLNLGIIFQDYIRYQMSFSQNIAVGNIDEQANIELIRKAAHESLADTLAARLPLGYDQWLGRRFNEGVELSGGEWQKVALARAYMKDAQVLILDEPTAALDARAEYEVFQRFSSLTQGKSAVLISHRFSTARLADRIIVLERGCILEAGTHEQLMANNGRYAELFNLQAAGYQ
>NZ_CP043450.1|WP_112568822.1|5635208_5637665_+|TonB-dependent-receptor-plug-domain-containing-protein
MIIKKGLLFLLPAIFFRMTVFGQTASPESKIPPLLQQFGEKFPQEKVHLHLDRNNHSSGDTLRFRAYVVNAQNNQFTDLSKVLYVDLLNSQDSRVIELRFPVNDGGVSGWVALPDSMERGTYTLRAYTAWMRNFKPELFYHTSLKIGNPANSKQSIPRETKKTRNDELHNIQFFPEGGDLVNGITSVIAFKAINNTGLGEDVSGTITDESGKILSNLQSSFAGMGRFNLTPTQGHSYEAHVRFKDGVTKKVTLPVALTSGYALAVNNQDKANVIIQVMAGGLKATEPVWLAAQANNKLISLTKLDLSNNQGSISIPKRTLPTGIVQFTLFNNLSEPKAERLIFIDRHDQLRLNAGTPKILSTNSVIQIPIEATDQLANPVSANFSVAVVNRKTPVDSTTLTPSILSDLLLTSDLNGYIEYPNHYFKSREPQISLQLDNLMLTQGWRRFIWKDLLAGKFPDVIYPAQTQQTLSGKIQTGKGSTLPKQNVMLVSKGDSAFTIRTVTDSKGRFTFNLPDLQEQHQFSIIASTDSKDINIILDQFAPADSTGYVVKEELSNYPAQSPTNQAHTIKNGTRQLSEVVVKSKKLSATEKAVAPSANFNGAGNANQIITYKDLNHCDNLEICLEGRLVGVYFRIKKDPFSHGYTKVPYSTGGLNKPMLFVLDGVPIQPGQISLNSIPAGNVQSIEVLRSGSLIAAYGLAGSGGVLVITTKKGGINYNEMDEPEDITVTSTPGVINFTYNGYQKYREFYVPKYPVADRTKRNSPETLFWNPVVKTDDRGQSVLEFPIGADVKNIALTIEGISGDGKIGYHYQEYAIK
>NZ_CP043450.1|WP_112568824.1|5637651_5638968_+|carboxypeptidase-like-regulatory-domain-containing-protein
MLLNKRNRIMKKILTIIFCLFVTHAFGQQQISGKVTDEKGSPLVNASVFIAESKNGTMTDTSGHFKLTLQAKGNFKIVVSYIGYKTTARALNTSSISSNIDFVLTPVSHQLKDVIVTSKASNNWKRWGAMFTEQFIGTSAFAAHCTITNPEVIGFDYDDAKQELHAYASEPLIIRNEDLGYLVSLTLVDFTFYTSKNEVDYQGYYLFKEIDGNERRKATWEQNRLKAYSLSFMHFTRALYNDKLKEEGFEVRQFSAGNIREKERIEKLYAQKLNTYLDSAKIEKNKLLDTNQIASKIFNKDSLRYYKKILTNKSEIKMSEPLKAKDISAKSENNITLNFKDQLQVVYKKIKEPEEYYNYRNHAALTTESTTVQSTGISTSQLIMPTKQYPFTELLLEKGIPVEITENGYYNNTNLYLNGFWGWWEKMATKLPYDYEPN
>NZ_CP043450.1|WP_112568826.1|5638974_5640003_-|hypothetical-protein
MEHRFSVNKILLIALSIIGIGALSAYKPSPAKNVPVKLKLIMGADISFIPQLEAEGHKFYDNGVSKDPFIILKDHGFNYVRLRVFNNPKADSGYSAKAYCGLEDTKKMALRIKDAGMGFLLDFHYSDTWADPGHQHKPAAWKNLNNQQLQDSIKAFTRLTLLTLKQQGTLPDMVQVGNEINHGILWPDGRAKNLDTLAGFLKAGTNTVREVSGKIKVMLHIACGGQNAESRYFVDNMLKRGVKFDIIGESYYPEWHGTPDSLRNNLTDLNTLYKQDVIVVEYSQLKREVNDVAFSLPGNKVKGTFIWEPFSWGETFVDKQGNTNAHMATYDSVKTQYHIADK
>NZ_CP043450.1|WP_112569049.1|5640164_5640725_+|thioredoxin-family-protein
MNFTAYQELFFDILNSPNPPAPYDNPDYLNYTKLNWSRQQRWLKVGVLNPDLTAAIEKISKPQTWTVITEAWCGDASHTIPFLHRLSELNPLIKVDYQLRDSPPFLIESYLTNGTRSIPKIIISDENNQDLGTWGPRPAECQRLYLQMVKDHVEMSEKKIVLQKWYNEDKGVSFQLEFLDIINHTL
>NZ_CP043450.1|WP_112568828.1|5640852_5641953_-|phytase
MNKLSKLAFVALAVAIGNTACGQSQVRNSKGLTIPGSTAPEIKPVVITEPVLYDTDDPAIWVNPADPSKSLIIGTDKNSEGALFVFDLQGKIIKDKVVHGLKRPNNVDLAYGLMLGGKPTDIVITTERMTHKLRIYSLPDMKPVDNGGIDAFVGETGLEYRDLMGISIYTAKNGKMYAIVGRKNGPQNGGYIWQYLLEDDGSGNVKATLARKFGKYSGKKEIESIAVDNELGYIYYSDEQVGVRQYYADPEKGDQELAIFGTSGFKADHEGISIYKLTDTTGYILVSDQGANRFQIFSREGTKANPFEHQLLKIANVAARESDGSDVIATPLNDTFKHGIFVVMSTDKTFHYYRWEDIAGKELKVK
>NZ_CP043450.1|WP_112568830.1|5642012_5643266_-|right-handed-parallel-beta-helix-repeat-containing-protein
MKLKQIFAAVLLSAIAFSSCRKANLDVDTSSADGSASGEVSGVWAKGSTQIIKGDIIIPEGKSLTIEEGVTVLMDTIAKPEFIVKGNLYSLGTAENPVRITVNPAYRTDAKKFGKMWGGILAAKTCAELVLDHTILEYGGNTTSDGSSSVKMGLYKAVAGENLPALWFSNVNGKLIVVNSTVRNFQEDCTYIEGGKIIFANNTFYTTGVTGGEAMNFKSGCLADVGFNLVYSANTNALKLSNSGDRDPQAYIICYNNTMVNTGWRRPSAKGGSVWVENNVRADIRNNLFANTRFGIKRDTKSTEDKRTVISNNLYYGYDQTTVNQFQPSKDIIGGVNEVIGTKAGDNDPKFVNYPESTPVLNAVFDTNWDFHLQSGSPALNHGVTNFTRHHAAGITVNGITYVSPDPATYIGAFGTK

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Crispr_ID: NZ_CP043450_9

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043450_9

6143679-6143757

Orphan

Consensus_repeat	Method
CTTGAAACCAGCGGTGGCGGCATC	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043450_9

>merge|NZ_CP043450|9|6143679-6143757|CRISPRCasFinder
CTGGAAACCAGTGGCGGCGGTATTGGTCTGGATAATTTAAAAGGTAACGAGAAATTTAGCACCAGCGGCGGCGGCTTAC

>NZ_CP043450|9|9|6143679-6143757|CRISPRCasFinder
CTGGAAACCAGTGGCGGCGGTATT	GGTCTGGATAATTTAAAAGGTAACGAGAAA
TTTAGCACCAGCGGCGGCGGCTTAC

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043450.1\|WP_112568462.1\|6147582_6150576_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|274948
NZ_CP043450.1\|WP_112568484.1\|6139875_6140610_-\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|235975
NZ_CP043450.1\|WP_112568454.1\|6153462_6153744_-\|DUF4242-domain-containing-protein	unknown	unknown	gnl\|CDD\|379428
NZ_CP043450.1\|WP_112568482.1\|6140614_6140833_-\|4-oxalocrotonate-tautomerase-family-protein	unknown	unknown	gnl\|CDD\|224853
NZ_CP043450.1\|WP_112568472.1\|6142764_6143148_+\|VOC-family-protein	unknown	unknown	gnl\|CDD\|319924
NZ_CP043450.1\|WP_112568460.1\|6150597_6152226_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|369630
NZ_CP043450.1\|WP_112568464.1\|6146614_6147232_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112568452.1\|6154044_6156318_+\|CRTAC1-family-protein	unknown	unknown	gnl\|CDD\|379232
NZ_CP043450.1\|WP_112568480.1\|6140862_6141396_-\|YceI-family-protein	unknown	unknown	gnl\|CDD\|377274
NZ_CP043450.1\|WP_121808191.1\|6144395_6145115_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112568492.1\|6136588_6137431_-\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|180446
NZ_CP043450.1\|WP_112568490.1\|6137504_6138254_-\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293841
NZ_CP043450.1\|WP_112568478.1\|6141505_6142078_-\|Crp/Fnr-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|223736
NZ_CP043450.1\|WP_112568450.1\|6156379_6156961_-\|HPP-family-protein	unknown	unknown	gnl\|CDD\|377434
NZ_CP043450.1\|WP_112568474.1\|6142270_6142756_+\|peptide-deformylase	unknown	unknown	gnl\|CDD\|366575
NZ_CP043450.1\|WP_112568486.1\|6139426_6139804_-\|nuclear-transport-factor-2-family-protein	unknown	unknown	gnl\|CDD\|378987
NZ_CP043450.1\|WP_112568488.1\|6138250_6139327_-\|nitronate-monooxygenase	unknown	unknown	gnl\|CDD\|240081
NZ_CP043450.1\|WP_112568466.1\|6145211_6146372_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340882
NZ_CP043450.1\|WP_112568448.1\|6156974_6158228_-\|cation:proton-antiporter	unknown	unknown	gnl\|CDD\|223551
NZ_CP043450.1\|WP_112568458.1\|6152304_6153399_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379871

Protein	Function_ID	Function_description	E-value
NZ_CP043450.1\|WP_112568462.1\|6147582_6150576_+\|TonB-dependent-receptor	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_CP043450.1\|WP_112568484.1\|6139875_6140610_-\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|235975	PRK07231, FabG-like, SDR family oxidoreductase.	1.95511e-68
NZ_CP043450.1\|WP_112568454.1\|6153462_6153744_-\|DUF4242-domain-containing-protein	gnl\|CDD\|379428	pfam14026, DUF4242, Protein of unknown function (DUF4242). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 90 and 170 amino acids in length. There is a single completely conserved residue C that may be functionally important.	6.27709e-23
NZ_CP043450.1\|WP_112568482.1\|6140614_6140833_-\|4-oxalocrotonate-tautomerase-family-protein	gnl\|CDD\|224853	COG1942, COG1942, Uncharacterized protein, 4-oxalocrotonate tautomerase homolog [General function prediction only].	2.99769e-19
NZ_CP043450.1\|WP_112568472.1\|6142764_6143148_+\|VOC-family-protein	gnl\|CDD\|319924	cd07263, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.	3.94689e-41
NZ_CP043450.1\|WP_112568460.1\|6150597_6152226_+\|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.	5.81438e-30
NZ_CP043450.1\|WP_112568452.1\|6154044_6156318_+\|CRTAC1-family-protein	gnl\|CDD\|379232	pfam13517, VCBS, Repeat domain in Vibrio, Colwellia, Bradyrhizobium and Shewanella. This domain of about 100 residues is found in multiple (up to 35) copies in long proteins from several species of Vibrio, Colwellia, Bradyrhizobium, and Shewanella (hence the name VCBS) and in smaller copy numbers in proteins from several other bacteria. The large protein size and repeat copy numbers, species distribution, and suggested activities of several member proteins suggests a role for this domain in adhesion (TIGR).	2.72733e-11
NZ_CP043450.1\|WP_112568480.1\|6140862_6141396_-\|YceI-family-protein	gnl\|CDD\|377274	pfam04264, YceI, YceI-like domain. E. coli YceI is a base-induced periplasmic protein. The recent structure of a member of this family shows that it binds to poly-isoprenoid. The structure consists of an extended, eight-stranded, antiparallel beta-barrel that resembles the lipocalin fold.	5.17851e-30
NZ_CP043450.1\|WP_112568492.1\|6136588_6137431_-\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|180446	PRK06180, PRK06180, short chain dehydrogenase; Provisional.	2.09778e-94
NZ_CP043450.1\|WP_112568490.1\|6137504_6138254_-\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293841	cd16283, RomA-like_MBL-fold, Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain. Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.	6.44038e-17
NZ_CP043450.1\|WP_112568478.1\|6141505_6142078_-\|Crp/Fnr-family-transcriptional-regulator	gnl\|CDD\|223736	COG0664, Crp, cAMP-binding proteins - catabolite gene activator and regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms].	9.48883e-22
NZ_CP043450.1\|WP_112568450.1\|6156379_6156961_-\|HPP-family-protein	gnl\|CDD\|377434	pfam04982, HPP, HPP family. These proteins are integral membrane proteins with four transmembrane spanning helices. The most conserved region of the alignment is a motif HPP. The function of these proteins is uncertain but they may be transporters.	1.09905e-55
NZ_CP043450.1\|WP_112568474.1\|6142270_6142756_+\|peptide-deformylase	gnl\|CDD\|366575	pfam01327, Pep_deformylase, Polypeptide deformylase.	4.7995e-47
NZ_CP043450.1\|WP_112568486.1\|6139426_6139804_-\|nuclear-transport-factor-2-family-protein	gnl\|CDD\|378987	pfam12893, Lumazine_bd_2, Putative lumazine-binding. This is a family of uncharacterized proteins. However, the family belongs to the NTF2-like superfamily of various enzymes, and some of the members of the family are putative dehydrogenases.	1.17581e-36
NZ_CP043450.1\|WP_112568488.1\|6138250_6139327_-\|nitronate-monooxygenase	gnl\|CDD\|240081	cd04730, NPD_like, 2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.	4.54446e-76
NZ_CP043450.1\|WP_112568466.1\|6145211_6146372_-\|MFS-transporter	gnl\|CDD\|340882	cd17324, MFS_NepI_like, Purine ribonucleoside efflux pump NepI and similar transporters of the Major Facilitator Superfamily. This family is composed of purine efflux pumps such as Escherichia coli NepI and Bacillus subtilis PbuE, sugar efflux transporters such as Corynebacterium glutamicum arabinose efflux permease, multidrug resistance (MDR) transporters such as Streptomyces lividans chloramphenicol resistance protein (CmlR), and similar proteins. NepI and PbuE are involved in the efflux of purine ribonucleosides such as guanosine, adenosine and inosine, as well as purine bases like guanine, adenine, and hypoxanthine, and purine base analogs. They play a role in the maintenance of cellular purine base pools, as well as in protecting the cells and conferring resistance against toxic purine base analogs such as 6-mercaptopurine. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. The NepI-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.35162e-16
NZ_CP043450.1\|WP_112568448.1\|6156974_6158228_-\|cation:proton-antiporter	gnl\|CDD\|223551	COG0475, KefB, Kef-type K+ transport systems, membrane components [Inorganic ion transport and metabolism].	6.19637e-55
NZ_CP043450.1\|WP_112568458.1\|6152304_6153399_+\|hypothetical-protein	gnl\|CDD\|379871	pfam16670, PI-PLC-C1, Phosphoinositide phospholipase C, Ca2+-dependent. PI-PLC-C1 is a family of calcium 2+-dependent phosphatidylinositol-specific phospholipase C1 enzymes from bacteria and fungi. The enzyme classification number is EC:3.1.4.11. This enzyme is involved in part of the myo-inositol phosphate metabolic pathway.	0

>NZ_CP043450.1|WP_112568472.1|6142764_6143148_+|VOC-family-protein
MKQFIAHITVVVSNYDEAIQFYTEKLNFDLIEDTLINENKRWVLVRPKGSSECSLLLAKAVGEEQQQRIGRQTGGRVFLFLRTDDFWRDYHAMRNRNIEFVREPKAESYGTVAVFKDPFGNLWDLLG
>NZ_CP043450.1|WP_112568474.1|6142270_6142756_+|peptide-deformylase
MKKLNDILLLGDERLYQVCDPVMQNELPLLNGWIADMHNVMKEIRQKYNFGRAIAAPQLGIMKRLVYMNIDNPVIFINPEIQDVSDELFELWDDCMSFPNLLVKVKRHKTITVNYLDENWQQQQWAMTDALSELMQHENDHLNGILCTMRAIDSMSFKWRP
>NZ_CP043450.1|WP_112568478.1|6141505_6142078_-|Crp/Fnr-family-transcriptional-regulator
MQPKEILKEHVSKTITLTDEQFDYFFSHFTYKTFKKGQTIIGEGDKVDCEYFVLSGYLKSFFINDDMKMFILQFAMPTWWASDYNALYSGERATVNVDCITDAEVLCLTSQDREKLCREIHEGEHFFRWRTNKGYVATQKRLLSFMNNDAKHRYEELLAQYPTLYNIVPKQLIASYLGVSRETLSRLYHS
>NZ_CP043450.1|WP_112568480.1|6140862_6141396_-|YceI-family-protein
METQKFEIISAKSNIDWVGRKVTGAHNGTIAIKEGSLNFADGQLADGKFTIDTTSIKILDVTDPATNAQFAGHLASDDFFNSDNYPEAQFVITAISKESNDTYRIIGNLTIKGITHPVSFDAQVTTTADIVSATGKVVVDRTKYGMRFRSGNFFKDLGDTLIYNDFDLNVNITAKAV
>NZ_CP043450.1|WP_112568482.1|6140614_6140833_-|4-oxalocrotonate-tautomerase-family-protein
MPYVKIELTREGVTREQKQTLIKGVTDLITNTLNKDPHLTHVVINEVELDDWGYAGEQVSVLREKGITADKK
>NZ_CP043450.1|WP_112568484.1|6139875_6140610_-|SDR-family-NAD(P)-dependent-oxidoreductase
MKKQTIIVTGASSGIGKEIARYFLEKGDNVVINSTTADKLEAVYQELGAGDNLAAVAGNVSDKATGEKLAQIAIDKFGSVDVLVNNAGIFETRPFLEVDEAYLDRFLDTNLKGTYFTTQAVIPQMIKQHDGVVINIGTPLVNHALSGVPITAQMASKGAVHALTIQLAGEFGKDNIRVNTIAPGTIRTPMHGDNADQTAGLHLLNRVGEVEDIAQMAYSVAKSNFITGAIINVDGGTAAGRNLN
>NZ_CP043450.1|WP_112568486.1|6139426_6139804_-|nuclear-transport-factor-2-family-protein
METNNQAKAAIEQALENYYFKGIYEGNLDLLNQVMNAGTLLFGDVKGEPYAKTLDVYLDGVKNRVSPKDSGKPFEGKIISVKAVNSIAVAEVQVKMYDFNYHEFLSFHKLNGKWLIVNKMISDTN
>NZ_CP043450.1|WP_112568488.1|6138250_6139327_-|nitronate-monooxygenase
MWYNTKATEILGIDYPIMQGPFGGNLSSVELVSTVSNAGGLGGYGAYTLSGSEIVEIDRRIRAATNKPYNINIWVSETDAPNGEATDEQFEHAAQLFKPYFDEAGIPLPPKPAPFKLRFENQLQVILDLRPKVFSFMFGTLPADVMEQCRRLGIVTVGAATTLDEAIALEASGVDMIIASGFEAGGHRPSFLAQAEASTTGTFVLLQLIKEKVKTPVIAAGGIANGRGVAGALILGADAVQIGTAFLACDESGALPVHRQMLFSDAAKYTTLSRAFTGRLGRGITSRVAKDLIGKEAGFLPFPLQTTFMSPLRKAALEQQKLDMVLFWGGQIAPVLKHTKAAELMQSIIADTTKIMNP
>NZ_CP043450.1|WP_112568490.1|6137504_6138254_-|MBL-fold-metallo-hydrolase
MKNEVNVTYIGGPTVILEIGGLRFMTDPTLDPVGEQFMINDKPAYHKTEGPATTDIGKIDVVLLSHDQHGDNLDNAGRELLKQVSKTLTTKIGAERLGGNTIGLAPWESISLNDNVVITGTPARHGPAGSEKLTGDVTGFIVTVAGFQIYFTGDTVFYDGIKEVAEKFKPQYVFIFAGAAKPRGPFNVTMGTNDAIDTAFAFPDATIIPVHFEGWSHYTETGEMLQQSFNALGIGGQLKILAPGIKTSL
>NZ_CP043450.1|WP_112568492.1|6136588_6137431_-|SDR-family-NAD(P)-dependent-oxidoreductase
MNSTKVWYVTGASQGLGLTLVKKLLDNGHRVAATSRNAQTLKQAVGLIDTDRFLPLAVDLSNPDCIEESIRETLKAFGQIDVLVNNAGYGMAGTVEEIEGQKIRDIFNVNVLAAIDVTKAVLPVMRGQGSGYVINIGSVAGFVGAPGWSVYSATKAAIAAFSEVLALDVKEFGIKVTVVEPSGFRTGFLTTGSLAFTESNIEGYQAVKNAQQRYLAADGKQPGDPEKASEIIMSLIDMDEPPLHLYLGEDAYKRASEKLRIMTAELEKWKEFTISADFKS
>NZ_CP043450.1|WP_121808191.1|6144395_6145115_-|hypothetical-protein
MKKSYTLLVFILFIGISICKAQDYQPGYVIMNDGTRVGGVIALNEAEPWYNQRYIRVKDSVAFAKDPNVKPKRIKADDMKFYVVGTRLFDKVHYVDLQNLQLKSMGTNDHMMERLAVGRITAHRFYEYPADVAVYVASEEEIERREKEKKDALIRGYFILAQKDNDKLRNAFDYDLQKYFEDTPEVLEKYKSGSYGNQPVKKGLAARMVAMAKKTAFKQEEADGIVAAFNDYNSKNATK
>NZ_CP043450.1|WP_112568466.1|6145211_6146372_-|MFS-transporter
MTRILPVIVLSQFFCTSLWFAGNAVMGDIAKQLQLEPSYLAYLTSAVQLGFITGTLVFAILSIADRFSPVRVFFICALIAAAVNALACLPGTDATIILVLRYTTGFFLAGIYPVGMKIASDHYPQGLGKALGFLVGALVLGTSFPHLLKSLMAALPWRYVILSTSILAAIGGCAMVLLVPDGPARKPGAALNPATFLKNFGNRQFRSAAFGYFGHMWELYAFWAFVPVMLSAYNSRYSDANLNVPLLSFLIIGVGAFACVGSGIISGYIGVKKVATMALTISGVCCLVSPLFLFAGSAWILIVFLLVWSMAVIADSPLFSTLIAQNADQQLKGTALTIVNCIGFAITIVSIQLITALRTVENARYIYMLLAIGPLLGLLALLKRSQ
>NZ_CP043450.1|WP_112568464.1|6146614_6147232_+|hypothetical-protein
MEKQQIIDQIKWMIADGNADHEIEALLVGEGVARAEAKYTLSVVKNELFPDEYPLIIEPKSNRAYLWAGLLIVAALVSLLAFHSWRKSSGTAEREINPADMIRLMKDGPGVYTTELNKINAGWTFNQDKDRWENNKRKTALAIRLEQLLYMCPVLHDHSFQDYLENHEFRDIIYTKPGSKIFQNDEFMFTIQTNADYTMISLAYR
>NZ_CP043450.1|WP_112568462.1|6147582_6150576_+|TonB-dependent-receptor
MEKHYRSILRLCHRSSKTICLFMLMFMATSMAFAQQRTIRGTVTDETNLPLPGVVVTVKSTGKATSTTANGIYQVTVSGPEDVIKFTFLGSLPKEVTVGDKKVVNVTMVTDTKQLKDVVVIGYGTASRKDVTGAITSVKAEDFNAGVLTTPAELLQGKVAGLNITKSGDPNKQPATILRGPSTLREGAAQQPFYVIDGVPGASIDLLAPADIESIDVLKDASSTAIYGSRAANGVIIVTTRRAKAGQTRLTYSAYAAVENVSKNIDVLTGDELRKYLTDNGVPKLSAADDDGSNTNWQKLAERTGYSQNHNLSYGGAGTNSEYGASVNYMKNNGILNNTSLERTIYKGYINQRFFNDRLKLGITLTNSATKNNDIFQSQVLSGILFYLPTVGPYNADGTYKENYSRTGSGPLNPLSLINNNFTRTENNKTLINGFASLDILKGLKFTVSGSTQKEQNNVNTYSTSQSGIYVNAGGVAVRSAYTNTSNVVEAYFNYDRVFGKHSLKLLGGYSYQQDRNNDGFGVQTQGFSNDALTYNYLALSNPTQLSQIVFNPAYISTLRFVSFYARAQYEFSDKYLLQASLREDGSSAFGINQRHGYFPAASAGWKIINEDFMKSIPVISDLKLRAGYGVSGNSLGFDAFTARLIYGVPPGGGKFLSNGNIVNPIGPVRNDNPDLKWESTATTNIGLDFGLFNNRLTGSVDYYIKKTSDLIYTYPVSTTLYFYPFYTANVGKIKNSGIEVVLNAVPVKSQAFTWRTSFNVSHNKNVVESLSNSQFGLNFIQTAQLGGKGQSGNYSQIIQPGYAIGTFDLWHYLGKNGNGVSTYEKADGSTTATQPLTTDQFIKYDAQPKLIYGWSNSFFYKGFDLNFLVRGVYGNKVLNATLASLNNPADSKLQNIPRFTLGESFKDINAYLISDRFLESGSYLRLDNATLGYTIKPHIQAIKSLRFYASGNNIFIITKYRGVDPEVNIGGLTPGIDNRDYYPKTRTFSLGITAQF
>NZ_CP043450.1|WP_112568460.1|6150597_6152226_+|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKKIFLACAAFATMIGTYSCTKLDVPVESQYVTSNFPVTDADYTALLGTIYSNLSSSYAVPYWRMQDMSTDEAILPARDGNFDDGGQYRQLHYHSWTFDHPNVISVWQWGFGGINTCNRIISVINASSSSAAKKASSVAEVKAMRALYLYFMMDLYGNVPIITDFPVTTQPANQPRAKVYEFIESELKTVLPLLPAKSSNAATNVGQYGRPTKGMVFALLAKMYLNSGVYIGTNRYQETVAMCDSVQTNTNYFLDAKFRDIFLPTNGPQINETIFAVPYDQQIPGNQFTRFGFFYYLAQAYGFNVGLSIAMSTTPEFYNRFNIPGDDRTKTWLAGPQYYPDGNGGFTSQPVYYPTGTAGVPANTQINIKPDLILTGLKPMDLGNDVLNAQSEGVRSIKYYPDVNIIQATRLNSNDVPVFRLADIYLMKAEAILRGAAPTTINGDAQTPLTLVNKLRTRAHAQAATSIDLDGLLDERARELSWEAWRRNDLIRYGLFEKEYSLPVMGGKTDDLKMNTDPTRRLYPIPSTELKTNPNLKQNPGY
>NZ_CP043450.1|WP_112568458.1|6152304_6153399_+|hypothetical-protein
MKFTGGLIAGIVLSASALLNNPDDQKMNHFQVIGSHNSYKQAINPKLFRFLQQRDSVGMSKIDYEHISLSDQLNLGLNALEIDVYADPKGGKYAHPKGLDWVPGQPAFDTQGVMKEPGFKVFHIEDIDFRSNCATFKLCLQELKKWSDEHPDHNPIYITMNAKDEPMDKPGFTVPEKFTAQTFADLDKEILTYLGKQYLITPDDVRGSYKTLEAAVLHNNWPTLKAAKGKFIFILDEKGEKRATYIVGHPSLKGRVLFADALPGTPEAAIHIMNDAKKDLAAIQKLVKKGYIIRTRADSDTQEARANDMSSFEAAQKSGAQIISTDYYKKSTHFNSDYVISFNGGTYFKPDPLFQTGSQDSVGN
>NZ_CP043450.1|WP_112568454.1|6153462_6153744_-|DUF4242-domain-containing-protein
MKKFVIERELPGAGNLSPEELQAISQTSCSVVNDLGKPYHWIQSFVTADKIYCIHIAESEDVIREHAMKGGFPVTSIAEVKAVIDPTTSTVTV
>NZ_CP043450.1|WP_112568452.1|6154044_6156318_+|CRTAC1-family-protein
MRLQHIYISVIKGYLFFLTITFLACLIASCGGSSHQDMIDILHNESKRTFSRLNANCPEAQLLHCDSDLHTVTDQGNINFLNYAKASLLVRVGQEEKAVSIYQNLLDRMDPEVSKQMLPEVAIAYMRVGERNNCMLNHTGSSCVFPIRDEGVHVIKTGSTKAIEIYEQILKQNPGDLESRWLLNIAFMTLGKYPQEVPHNLLIPNLNADTGFKVKPFVDAGPSLNLSVNNKAGGVIADDFNGDGYIDLITSGMGFDDAMHYFRNNKDGTFTDIAETAGLKGITGGLNIQQTDYNNDGKPDIFVLRGAWLDKGFGNQPSSLLRNNGDGTFTDVTIPSGLLFYHSTQTATWADFNNDGWLDVFIGYESKTPDDIEKCALYINNHGEGFVNVAEQAHCDVVGFVKGVTSGDYDNDGKPDIFVSCIDGKKFLLHNTTQPGKNVNFENVTDKAGFANNTNPTFGTWFFDYNNDGYLDLVACNFNFKSYTTTLGYFAASEALGKPVKGAGNIFLFRNNKNGTFTDITDLAGLTRVVFAMGCNFGDIDNDGYPDMYFGTGNPDFRSLVPNKLFRNMSGKRFADVTTSARVGNLQKGHGIAFADFRNIGKQDIYAEMGGTYNGDSYANPLYVNPGQNDNNWIGLKLEGTKANKSAIGSRIKLTFMENGVKRSVYKDVNSGGSFGSSPLRQEIGIGQAKSIAEIEIKWAGTTEKQYFRNIAPNQFLQITEGNNTPRPIKLKSLEFKIKAGTTVCLPVSLTTQVKTN
>NZ_CP043450.1|WP_112568450.1|6156379_6156961_-|HPP-family-protein
MRRRIHRHIRTAKYIVYKETLVDFREHFWTFISSFSGIALIGLLNSRYFTASDNLFLIGSFGASSVLIYGVINSPLAQPRNLIGGHVLCALVGVTIHKLVPNELWLAAALSVSIAIVLMQVTKTLHPPGGATALIANIGSEKIKALGYMYVFSPVFSGALILLLVALLFNNMTKHRHYPNNKKWLQVWRRYQR
>NZ_CP043450.1|WP_112568448.1|6156974_6158228_-|cation:proton-antiporter
MHNADILGRLTQQFELPFSNPVLVFSLILLIILLAPIVMGKFRFPGIVGFILAGIAIGPHGLNLLKKNSAIDLFSTIGLLYIMFIAGVELDLNEFKQKKHRSLVFGFFTFCIPILIGFPICYYLLGYPLITSALTASMFATHTLVAYPIVSKYGMAKNEAVAISVGGTILTDTAVLILLPVIMGAKNGGLGFSFWLQLMISLSIFAFIMFVLIPPLARWFFNRYRDSKTLPYVFVLFIVFLSAFLSQLAGVEPIIGAFVAGLALNKAVQQSQQLMHRIDFVGNAIFIPFFLISVGMLVDLRVLTRGPQATIVALSLTLGALLGKWLAALSTQKIFKYSATQRTLIFGLSSAHAAATLAIILVGFKAQIIDDNILNGTIILILVTCVVASFATEHAGKKLVKRLEEPPVLTEEEQTIG

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Crispr_ID: NZ_CP043450_10

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043450_10

6143841-6143972

Orphan

Consensus_repeat	Method
CTTGAAACCAGCGGTGGCGGCATC	CRISPRCasFinder

2 spacers

The CRISPR arrays of NZ_CP043450_10

>merge|NZ_CP043450|10|6143841-6143972|CRISPRCasFinder
CTTGAAACCAGCGGTGGCGGCATCGAGGCGAAAAACTGCAACGGAAAAATCAGACTTGAAACCAGCGGCGGCGGCATCACTTTAGAAAACCTTAAAGGCACCATCAATGCCGAAACCAGCGGTGGCGGCGTT

>NZ_CP043450|10|10|6143841-6143972|CRISPRCasFinder
CTTGAAACCAGCGGTGGCGGCATC	GAGGCGAAAAACTGCAACGGAAAAATCAGA
CTTGAAACCAGCGGCGGCGGCATC	ACTTTAGAAAACCTTAAAGGCACCATCAAT
GCCGAAACCAGCGGTGGCGGCGTT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043450.1\|WP_112568462.1\|6147582_6150576_+\|TonB-dependent-receptor	unknown	unknown	gnl\|CDD\|274948
NZ_CP043450.1\|WP_112568484.1\|6139875_6140610_-\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|235975
NZ_CP043450.1\|WP_112568454.1\|6153462_6153744_-\|DUF4242-domain-containing-protein	unknown	unknown	gnl\|CDD\|379428
NZ_CP043450.1\|WP_112568482.1\|6140614_6140833_-\|4-oxalocrotonate-tautomerase-family-protein	unknown	unknown	gnl\|CDD\|224853
NZ_CP043450.1\|WP_112568472.1\|6142764_6143148_+\|VOC-family-protein	unknown	unknown	gnl\|CDD\|319924
NZ_CP043450.1\|WP_112568460.1\|6150597_6152226_+\|RagB/SusD-family-nutrient-uptake-outer-membrane-protein	unknown	unknown	gnl\|CDD\|369630
NZ_CP043450.1\|WP_112568464.1\|6146614_6147232_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112568452.1\|6154044_6156318_+\|CRTAC1-family-protein	unknown	unknown	gnl\|CDD\|379232
NZ_CP043450.1\|WP_112568480.1\|6140862_6141396_-\|YceI-family-protein	unknown	unknown	gnl\|CDD\|377274
NZ_CP043450.1\|WP_121808191.1\|6144395_6145115_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112568492.1\|6136588_6137431_-\|SDR-family-NAD(P)-dependent-oxidoreductase	unknown	unknown	gnl\|CDD\|180446
NZ_CP043450.1\|WP_112568490.1\|6137504_6138254_-\|MBL-fold-metallo-hydrolase	unknown	unknown	gnl\|CDD\|293841
NZ_CP043450.1\|WP_112568478.1\|6141505_6142078_-\|Crp/Fnr-family-transcriptional-regulator	unknown	unknown	gnl\|CDD\|223736
NZ_CP043450.1\|WP_112568450.1\|6156379_6156961_-\|HPP-family-protein	unknown	unknown	gnl\|CDD\|377434
NZ_CP043450.1\|WP_112568474.1\|6142270_6142756_+\|peptide-deformylase	unknown	unknown	gnl\|CDD\|366575
NZ_CP043450.1\|WP_112568486.1\|6139426_6139804_-\|nuclear-transport-factor-2-family-protein	unknown	unknown	gnl\|CDD\|378987
NZ_CP043450.1\|WP_112568488.1\|6138250_6139327_-\|nitronate-monooxygenase	unknown	unknown	gnl\|CDD\|240081
NZ_CP043450.1\|WP_112568466.1\|6145211_6146372_-\|MFS-transporter	unknown	unknown	gnl\|CDD\|340882
NZ_CP043450.1\|WP_112568448.1\|6156974_6158228_-\|cation:proton-antiporter	unknown	unknown	gnl\|CDD\|223551
NZ_CP043450.1\|WP_112568458.1\|6152304_6153399_+\|hypothetical-protein	unknown	unknown	gnl\|CDD\|379871

Protein	Function_ID	Function_description	E-value
NZ_CP043450.1\|WP_112568462.1\|6147582_6150576_+\|TonB-dependent-receptor	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_CP043450.1\|WP_112568484.1\|6139875_6140610_-\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|235975	PRK07231, FabG-like, SDR family oxidoreductase.	1.95511e-68
NZ_CP043450.1\|WP_112568454.1\|6153462_6153744_-\|DUF4242-domain-containing-protein	gnl\|CDD\|379428	pfam14026, DUF4242, Protein of unknown function (DUF4242). This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria and archaea. Proteins in this family are typically between 90 and 170 amino acids in length. There is a single completely conserved residue C that may be functionally important.	6.27709e-23
NZ_CP043450.1\|WP_112568482.1\|6140614_6140833_-\|4-oxalocrotonate-tautomerase-family-protein	gnl\|CDD\|224853	COG1942, COG1942, Uncharacterized protein, 4-oxalocrotonate tautomerase homolog [General function prediction only].	2.99769e-19
NZ_CP043450.1\|WP_112568472.1\|6142764_6143148_+\|VOC-family-protein	gnl\|CDD\|319924	cd07263, VOC_like, uncharacterized subfamily of vicinal oxygen chelate (VOC) family. The vicinal oxygen chelate (VOC) superfamily is composed of structurally related proteins with paired beta.alpha.beta.beta.beta motifs that provide a metal coordination environment with two or three open or readily accessible coordination sites to promote direct electrophilic participation of the metal ion in catalysis. VOC domain is found in a variety of structurally related metalloproteins, including the bleomycin resistance protein, glyoxalase I, and type I ring-cleaving dioxygenases. A bound metal ion is required for protein activities for the members of this superfamily. A variety of metal ions have been found in the catalytic centers of these proteins including Fe(II), Mn(II), Zn(II), Ni(II) and Mg(II). The protein superfamily contains members with or without domain swapping. The proteins of this family share three conserved metal binding amino acids with the type I extradiol dioxygenases, which shows no domain swapping.	3.94689e-41
NZ_CP043450.1\|WP_112568460.1\|6150597_6152226_+\|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.	5.81438e-30
NZ_CP043450.1\|WP_112568452.1\|6154044_6156318_+\|CRTAC1-family-protein	gnl\|CDD\|379232	pfam13517, VCBS, Repeat domain in Vibrio, Colwellia, Bradyrhizobium and Shewanella. This domain of about 100 residues is found in multiple (up to 35) copies in long proteins from several species of Vibrio, Colwellia, Bradyrhizobium, and Shewanella (hence the name VCBS) and in smaller copy numbers in proteins from several other bacteria. The large protein size and repeat copy numbers, species distribution, and suggested activities of several member proteins suggests a role for this domain in adhesion (TIGR).	2.72733e-11
NZ_CP043450.1\|WP_112568480.1\|6140862_6141396_-\|YceI-family-protein	gnl\|CDD\|377274	pfam04264, YceI, YceI-like domain. E. coli YceI is a base-induced periplasmic protein. The recent structure of a member of this family shows that it binds to poly-isoprenoid. The structure consists of an extended, eight-stranded, antiparallel beta-barrel that resembles the lipocalin fold.	5.17851e-30
NZ_CP043450.1\|WP_112568492.1\|6136588_6137431_-\|SDR-family-NAD(P)-dependent-oxidoreductase	gnl\|CDD\|180446	PRK06180, PRK06180, short chain dehydrogenase; Provisional.	2.09778e-94
NZ_CP043450.1\|WP_112568490.1\|6137504_6138254_-\|MBL-fold-metallo-hydrolase	gnl\|CDD\|293841	cd16283, RomA-like_MBL-fold, Enterobacter cloacae RomA and related proteins; MBL-fold metallo hydrolase domain. Derepression of the romA-ramA locus results in a multidrug-resistance phenotype. Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry.	6.44038e-17
NZ_CP043450.1\|WP_112568478.1\|6141505_6142078_-\|Crp/Fnr-family-transcriptional-regulator	gnl\|CDD\|223736	COG0664, Crp, cAMP-binding proteins - catabolite gene activator and regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms].	9.48883e-22
NZ_CP043450.1\|WP_112568450.1\|6156379_6156961_-\|HPP-family-protein	gnl\|CDD\|377434	pfam04982, HPP, HPP family. These proteins are integral membrane proteins with four transmembrane spanning helices. The most conserved region of the alignment is a motif HPP. The function of these proteins is uncertain but they may be transporters.	1.09905e-55
NZ_CP043450.1\|WP_112568474.1\|6142270_6142756_+\|peptide-deformylase	gnl\|CDD\|366575	pfam01327, Pep_deformylase, Polypeptide deformylase.	4.7995e-47
NZ_CP043450.1\|WP_112568486.1\|6139426_6139804_-\|nuclear-transport-factor-2-family-protein	gnl\|CDD\|378987	pfam12893, Lumazine_bd_2, Putative lumazine-binding. This is a family of uncharacterized proteins. However, the family belongs to the NTF2-like superfamily of various enzymes, and some of the members of the family are putative dehydrogenases.	1.17581e-36
NZ_CP043450.1\|WP_112568488.1\|6138250_6139327_-\|nitronate-monooxygenase	gnl\|CDD\|240081	cd04730, NPD_like, 2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.	4.54446e-76
NZ_CP043450.1\|WP_112568466.1\|6145211_6146372_-\|MFS-transporter	gnl\|CDD\|340882	cd17324, MFS_NepI_like, Purine ribonucleoside efflux pump NepI and similar transporters of the Major Facilitator Superfamily. This family is composed of purine efflux pumps such as Escherichia coli NepI and Bacillus subtilis PbuE, sugar efflux transporters such as Corynebacterium glutamicum arabinose efflux permease, multidrug resistance (MDR) transporters such as Streptomyces lividans chloramphenicol resistance protein (CmlR), and similar proteins. NepI and PbuE are involved in the efflux of purine ribonucleosides such as guanosine, adenosine and inosine, as well as purine bases like guanine, adenine, and hypoxanthine, and purine base analogs. They play a role in the maintenance of cellular purine base pools, as well as in protecting the cells and conferring resistance against toxic purine base analogs such as 6-mercaptopurine. MDR transporters are drug/H+ antiporters (DHA) that mediate the efflux of a variety of drugs and toxic compounds, and confer resistance to these compounds. The NepI-like family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.	1.35162e-16
NZ_CP043450.1\|WP_112568448.1\|6156974_6158228_-\|cation:proton-antiporter	gnl\|CDD\|223551	COG0475, KefB, Kef-type K+ transport systems, membrane components [Inorganic ion transport and metabolism].	6.19637e-55
NZ_CP043450.1\|WP_112568458.1\|6152304_6153399_+\|hypothetical-protein	gnl\|CDD\|379871	pfam16670, PI-PLC-C1, Phosphoinositide phospholipase C, Ca2+-dependent. PI-PLC-C1 is a family of calcium 2+-dependent phosphatidylinositol-specific phospholipase C1 enzymes from bacteria and fungi. The enzyme classification number is EC:3.1.4.11. This enzyme is involved in part of the myo-inositol phosphate metabolic pathway.	0

>NZ_CP043450.1|WP_112568472.1|6142764_6143148_+|VOC-family-protein
MKQFIAHITVVVSNYDEAIQFYTEKLNFDLIEDTLINENKRWVLVRPKGSSECSLLLAKAVGEEQQQRIGRQTGGRVFLFLRTDDFWRDYHAMRNRNIEFVREPKAESYGTVAVFKDPFGNLWDLLG
>NZ_CP043450.1|WP_112568474.1|6142270_6142756_+|peptide-deformylase
MKKLNDILLLGDERLYQVCDPVMQNELPLLNGWIADMHNVMKEIRQKYNFGRAIAAPQLGIMKRLVYMNIDNPVIFINPEIQDVSDELFELWDDCMSFPNLLVKVKRHKTITVNYLDENWQQQQWAMTDALSELMQHENDHLNGILCTMRAIDSMSFKWRP
>NZ_CP043450.1|WP_112568478.1|6141505_6142078_-|Crp/Fnr-family-transcriptional-regulator
MQPKEILKEHVSKTITLTDEQFDYFFSHFTYKTFKKGQTIIGEGDKVDCEYFVLSGYLKSFFINDDMKMFILQFAMPTWWASDYNALYSGERATVNVDCITDAEVLCLTSQDREKLCREIHEGEHFFRWRTNKGYVATQKRLLSFMNNDAKHRYEELLAQYPTLYNIVPKQLIASYLGVSRETLSRLYHS
>NZ_CP043450.1|WP_112568480.1|6140862_6141396_-|YceI-family-protein
METQKFEIISAKSNIDWVGRKVTGAHNGTIAIKEGSLNFADGQLADGKFTIDTTSIKILDVTDPATNAQFAGHLASDDFFNSDNYPEAQFVITAISKESNDTYRIIGNLTIKGITHPVSFDAQVTTTADIVSATGKVVVDRTKYGMRFRSGNFFKDLGDTLIYNDFDLNVNITAKAV
>NZ_CP043450.1|WP_112568482.1|6140614_6140833_-|4-oxalocrotonate-tautomerase-family-protein
MPYVKIELTREGVTREQKQTLIKGVTDLITNTLNKDPHLTHVVINEVELDDWGYAGEQVSVLREKGITADKK
>NZ_CP043450.1|WP_112568484.1|6139875_6140610_-|SDR-family-NAD(P)-dependent-oxidoreductase
MKKQTIIVTGASSGIGKEIARYFLEKGDNVVINSTTADKLEAVYQELGAGDNLAAVAGNVSDKATGEKLAQIAIDKFGSVDVLVNNAGIFETRPFLEVDEAYLDRFLDTNLKGTYFTTQAVIPQMIKQHDGVVINIGTPLVNHALSGVPITAQMASKGAVHALTIQLAGEFGKDNIRVNTIAPGTIRTPMHGDNADQTAGLHLLNRVGEVEDIAQMAYSVAKSNFITGAIINVDGGTAAGRNLN
>NZ_CP043450.1|WP_112568486.1|6139426_6139804_-|nuclear-transport-factor-2-family-protein
METNNQAKAAIEQALENYYFKGIYEGNLDLLNQVMNAGTLLFGDVKGEPYAKTLDVYLDGVKNRVSPKDSGKPFEGKIISVKAVNSIAVAEVQVKMYDFNYHEFLSFHKLNGKWLIVNKMISDTN
>NZ_CP043450.1|WP_112568488.1|6138250_6139327_-|nitronate-monooxygenase
MWYNTKATEILGIDYPIMQGPFGGNLSSVELVSTVSNAGGLGGYGAYTLSGSEIVEIDRRIRAATNKPYNINIWVSETDAPNGEATDEQFEHAAQLFKPYFDEAGIPLPPKPAPFKLRFENQLQVILDLRPKVFSFMFGTLPADVMEQCRRLGIVTVGAATTLDEAIALEASGVDMIIASGFEAGGHRPSFLAQAEASTTGTFVLLQLIKEKVKTPVIAAGGIANGRGVAGALILGADAVQIGTAFLACDESGALPVHRQMLFSDAAKYTTLSRAFTGRLGRGITSRVAKDLIGKEAGFLPFPLQTTFMSPLRKAALEQQKLDMVLFWGGQIAPVLKHTKAAELMQSIIADTTKIMNP
>NZ_CP043450.1|WP_112568490.1|6137504_6138254_-|MBL-fold-metallo-hydrolase
MKNEVNVTYIGGPTVILEIGGLRFMTDPTLDPVGEQFMINDKPAYHKTEGPATTDIGKIDVVLLSHDQHGDNLDNAGRELLKQVSKTLTTKIGAERLGGNTIGLAPWESISLNDNVVITGTPARHGPAGSEKLTGDVTGFIVTVAGFQIYFTGDTVFYDGIKEVAEKFKPQYVFIFAGAAKPRGPFNVTMGTNDAIDTAFAFPDATIIPVHFEGWSHYTETGEMLQQSFNALGIGGQLKILAPGIKTSL
>NZ_CP043450.1|WP_112568492.1|6136588_6137431_-|SDR-family-NAD(P)-dependent-oxidoreductase
MNSTKVWYVTGASQGLGLTLVKKLLDNGHRVAATSRNAQTLKQAVGLIDTDRFLPLAVDLSNPDCIEESIRETLKAFGQIDVLVNNAGYGMAGTVEEIEGQKIRDIFNVNVLAAIDVTKAVLPVMRGQGSGYVINIGSVAGFVGAPGWSVYSATKAAIAAFSEVLALDVKEFGIKVTVVEPSGFRTGFLTTGSLAFTESNIEGYQAVKNAQQRYLAADGKQPGDPEKASEIIMSLIDMDEPPLHLYLGEDAYKRASEKLRIMTAELEKWKEFTISADFKS
>NZ_CP043450.1|WP_121808191.1|6144395_6145115_-|hypothetical-protein
MKKSYTLLVFILFIGISICKAQDYQPGYVIMNDGTRVGGVIALNEAEPWYNQRYIRVKDSVAFAKDPNVKPKRIKADDMKFYVVGTRLFDKVHYVDLQNLQLKSMGTNDHMMERLAVGRITAHRFYEYPADVAVYVASEEEIERREKEKKDALIRGYFILAQKDNDKLRNAFDYDLQKYFEDTPEVLEKYKSGSYGNQPVKKGLAARMVAMAKKTAFKQEEADGIVAAFNDYNSKNATK
>NZ_CP043450.1|WP_112568466.1|6145211_6146372_-|MFS-transporter
MTRILPVIVLSQFFCTSLWFAGNAVMGDIAKQLQLEPSYLAYLTSAVQLGFITGTLVFAILSIADRFSPVRVFFICALIAAAVNALACLPGTDATIILVLRYTTGFFLAGIYPVGMKIASDHYPQGLGKALGFLVGALVLGTSFPHLLKSLMAALPWRYVILSTSILAAIGGCAMVLLVPDGPARKPGAALNPATFLKNFGNRQFRSAAFGYFGHMWELYAFWAFVPVMLSAYNSRYSDANLNVPLLSFLIIGVGAFACVGSGIISGYIGVKKVATMALTISGVCCLVSPLFLFAGSAWILIVFLLVWSMAVIADSPLFSTLIAQNADQQLKGTALTIVNCIGFAITIVSIQLITALRTVENARYIYMLLAIGPLLGLLALLKRSQ
>NZ_CP043450.1|WP_112568464.1|6146614_6147232_+|hypothetical-protein
MEKQQIIDQIKWMIADGNADHEIEALLVGEGVARAEAKYTLSVVKNELFPDEYPLIIEPKSNRAYLWAGLLIVAALVSLLAFHSWRKSSGTAEREINPADMIRLMKDGPGVYTTELNKINAGWTFNQDKDRWENNKRKTALAIRLEQLLYMCPVLHDHSFQDYLENHEFRDIIYTKPGSKIFQNDEFMFTIQTNADYTMISLAYR
>NZ_CP043450.1|WP_112568462.1|6147582_6150576_+|TonB-dependent-receptor
MEKHYRSILRLCHRSSKTICLFMLMFMATSMAFAQQRTIRGTVTDETNLPLPGVVVTVKSTGKATSTTANGIYQVTVSGPEDVIKFTFLGSLPKEVTVGDKKVVNVTMVTDTKQLKDVVVIGYGTASRKDVTGAITSVKAEDFNAGVLTTPAELLQGKVAGLNITKSGDPNKQPATILRGPSTLREGAAQQPFYVIDGVPGASIDLLAPADIESIDVLKDASSTAIYGSRAANGVIIVTTRRAKAGQTRLTYSAYAAVENVSKNIDVLTGDELRKYLTDNGVPKLSAADDDGSNTNWQKLAERTGYSQNHNLSYGGAGTNSEYGASVNYMKNNGILNNTSLERTIYKGYINQRFFNDRLKLGITLTNSATKNNDIFQSQVLSGILFYLPTVGPYNADGTYKENYSRTGSGPLNPLSLINNNFTRTENNKTLINGFASLDILKGLKFTVSGSTQKEQNNVNTYSTSQSGIYVNAGGVAVRSAYTNTSNVVEAYFNYDRVFGKHSLKLLGGYSYQQDRNNDGFGVQTQGFSNDALTYNYLALSNPTQLSQIVFNPAYISTLRFVSFYARAQYEFSDKYLLQASLREDGSSAFGINQRHGYFPAASAGWKIINEDFMKSIPVISDLKLRAGYGVSGNSLGFDAFTARLIYGVPPGGGKFLSNGNIVNPIGPVRNDNPDLKWESTATTNIGLDFGLFNNRLTGSVDYYIKKTSDLIYTYPVSTTLYFYPFYTANVGKIKNSGIEVVLNAVPVKSQAFTWRTSFNVSHNKNVVESLSNSQFGLNFIQTAQLGGKGQSGNYSQIIQPGYAIGTFDLWHYLGKNGNGVSTYEKADGSTTATQPLTTDQFIKYDAQPKLIYGWSNSFFYKGFDLNFLVRGVYGNKVLNATLASLNNPADSKLQNIPRFTLGESFKDINAYLISDRFLESGSYLRLDNATLGYTIKPHIQAIKSLRFYASGNNIFIITKYRGVDPEVNIGGLTPGIDNRDYYPKTRTFSLGITAQF
>NZ_CP043450.1|WP_112568460.1|6150597_6152226_+|RagB/SusD-family-nutrient-uptake-outer-membrane-protein
MKKIFLACAAFATMIGTYSCTKLDVPVESQYVTSNFPVTDADYTALLGTIYSNLSSSYAVPYWRMQDMSTDEAILPARDGNFDDGGQYRQLHYHSWTFDHPNVISVWQWGFGGINTCNRIISVINASSSSAAKKASSVAEVKAMRALYLYFMMDLYGNVPIITDFPVTTQPANQPRAKVYEFIESELKTVLPLLPAKSSNAATNVGQYGRPTKGMVFALLAKMYLNSGVYIGTNRYQETVAMCDSVQTNTNYFLDAKFRDIFLPTNGPQINETIFAVPYDQQIPGNQFTRFGFFYYLAQAYGFNVGLSIAMSTTPEFYNRFNIPGDDRTKTWLAGPQYYPDGNGGFTSQPVYYPTGTAGVPANTQINIKPDLILTGLKPMDLGNDVLNAQSEGVRSIKYYPDVNIIQATRLNSNDVPVFRLADIYLMKAEAILRGAAPTTINGDAQTPLTLVNKLRTRAHAQAATSIDLDGLLDERARELSWEAWRRNDLIRYGLFEKEYSLPVMGGKTDDLKMNTDPTRRLYPIPSTELKTNPNLKQNPGY
>NZ_CP043450.1|WP_112568458.1|6152304_6153399_+|hypothetical-protein
MKFTGGLIAGIVLSASALLNNPDDQKMNHFQVIGSHNSYKQAINPKLFRFLQQRDSVGMSKIDYEHISLSDQLNLGLNALEIDVYADPKGGKYAHPKGLDWVPGQPAFDTQGVMKEPGFKVFHIEDIDFRSNCATFKLCLQELKKWSDEHPDHNPIYITMNAKDEPMDKPGFTVPEKFTAQTFADLDKEILTYLGKQYLITPDDVRGSYKTLEAAVLHNNWPTLKAAKGKFIFILDEKGEKRATYIVGHPSLKGRVLFADALPGTPEAAIHIMNDAKKDLAAIQKLVKKGYIIRTRADSDTQEARANDMSSFEAAQKSGAQIISTDYYKKSTHFNSDYVISFNGGTYFKPDPLFQTGSQDSVGN
>NZ_CP043450.1|WP_112568454.1|6153462_6153744_-|DUF4242-domain-containing-protein
MKKFVIERELPGAGNLSPEELQAISQTSCSVVNDLGKPYHWIQSFVTADKIYCIHIAESEDVIREHAMKGGFPVTSIAEVKAVIDPTTSTVTV
>NZ_CP043450.1|WP_112568452.1|6154044_6156318_+|CRTAC1-family-protein
MRLQHIYISVIKGYLFFLTITFLACLIASCGGSSHQDMIDILHNESKRTFSRLNANCPEAQLLHCDSDLHTVTDQGNINFLNYAKASLLVRVGQEEKAVSIYQNLLDRMDPEVSKQMLPEVAIAYMRVGERNNCMLNHTGSSCVFPIRDEGVHVIKTGSTKAIEIYEQILKQNPGDLESRWLLNIAFMTLGKYPQEVPHNLLIPNLNADTGFKVKPFVDAGPSLNLSVNNKAGGVIADDFNGDGYIDLITSGMGFDDAMHYFRNNKDGTFTDIAETAGLKGITGGLNIQQTDYNNDGKPDIFVLRGAWLDKGFGNQPSSLLRNNGDGTFTDVTIPSGLLFYHSTQTATWADFNNDGWLDVFIGYESKTPDDIEKCALYINNHGEGFVNVAEQAHCDVVGFVKGVTSGDYDNDGKPDIFVSCIDGKKFLLHNTTQPGKNVNFENVTDKAGFANNTNPTFGTWFFDYNNDGYLDLVACNFNFKSYTTTLGYFAASEALGKPVKGAGNIFLFRNNKNGTFTDITDLAGLTRVVFAMGCNFGDIDNDGYPDMYFGTGNPDFRSLVPNKLFRNMSGKRFADVTTSARVGNLQKGHGIAFADFRNIGKQDIYAEMGGTYNGDSYANPLYVNPGQNDNNWIGLKLEGTKANKSAIGSRIKLTFMENGVKRSVYKDVNSGGSFGSSPLRQEIGIGQAKSIAEIEIKWAGTTEKQYFRNIAPNQFLQITEGNNTPRPIKLKSLEFKIKAGTTVCLPVSLTTQVKTN
>NZ_CP043450.1|WP_112568450.1|6156379_6156961_-|HPP-family-protein
MRRRIHRHIRTAKYIVYKETLVDFREHFWTFISSFSGIALIGLLNSRYFTASDNLFLIGSFGASSVLIYGVINSPLAQPRNLIGGHVLCALVGVTIHKLVPNELWLAAALSVSIAIVLMQVTKTLHPPGGATALIANIGSEKIKALGYMYVFSPVFSGALILLLVALLFNNMTKHRHYPNNKKWLQVWRRYQR
>NZ_CP043450.1|WP_112568448.1|6156974_6158228_-|cation:proton-antiporter
MHNADILGRLTQQFELPFSNPVLVFSLILLIILLAPIVMGKFRFPGIVGFILAGIAIGPHGLNLLKKNSAIDLFSTIGLLYIMFIAGVELDLNEFKQKKHRSLVFGFFTFCIPILIGFPICYYLLGYPLITSALTASMFATHTLVAYPIVSKYGMAKNEAVAISVGGTILTDTAVLILLPVIMGAKNGGLGFSFWLQLMISLSIFAFIMFVLIPPLARWFFNRYRDSKTLPYVFVLFIVFLSAFLSQLAGVEPIIGAFVAGLALNKAVQQSQQLMHRIDFVGNAIFIPFFLISVGMLVDLRVLTRGPQATIVALSLTLGALLGKWLAALSTQKIFKYSATQRTLIFGLSSAHAAATLAIILVGFKAQIIDDNILNGTIILILVTCVVASFATEHAGKKLVKRLEEPPVLTEEEQTIG

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Crispr_ID: NZ_CP043450_11

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043450_11

6434952-6435033

Unclear

Consensus_repeat	Method
AATCTTTGAAGGTCAAATGACAT	CRISPRCasFinder

1 spacers

cas3

The CRISPR arrays of NZ_CP043450_11

>merge|NZ_CP043450|11|6434952-6435033|CRISPRCasFinder
AATCTTTGAAGGTCAAATGACATCAGCCCTAATTGTTATGCTGAGTGGAAGAAAATAGAAATCTGTGAAGGTCAAATGACAT

>NZ_CP043450|11|11|6434952-6435033|CRISPRCasFinder
AATCTTTGAAGGTCAAATGACAT	CAGCCCTAATTGTTATGCTGAGTGGAAGAAAATAGA
AATCTGTGAAGGTCAAATGACAT

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043450.1\|WP_112572744.1\|6431159_6431648_-\|thioredoxin-fold-domain-containing-protein	unknown	unknown	gnl\|CDD\|379034
NZ_CP043450.1\|WP_112572747.1\|6428855_6429575_-\|2-phosphosulfolactate-phosphatase	unknown	unknown	gnl\|CDD\|377205
NZ_CP043450.1\|WP_112572751.1\|6425836_6427051_-\|HAMP-domain-containing-histidine-kinase	unknown	unknown	gnl\|CDD\|223715
NZ_CP043450.1\|WP_112572738.1\|6433633_6434239_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_090532309.1\|6445206_6445584_-\|30S-ribosome-binding-factor-RbfA	unknown	unknown	gnl\|CDD\|376719
NZ_CP043450.1\|WP_112572736.1\|6434278_6434938_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112572746.1\|6429665_6430745_-\|glycine-cleavage-system-aminomethyltransferase-GcvT	unknown	unknown	gnl\|CDD\|234742
NZ_CP043450.1\|WP_112575584.1\|6437788_6438583_+\|S1/P1-nuclease	unknown	unknown	gnl\|CDD\|211382
NZ_CP043450.1\|WP_112574690.1\|6444495_6445203_-\|peptidoglycan-DD-metalloendopeptidase-family-protein	unknown	unknown	gnl\|CDD\|180426
NZ_CP043450.1\|WP_112572742.1\|6431687_6432704_-\|oxidoreductase	unknown	unknown	gnl\|CDD\|183212
NZ_CP043450.1\|WP_112575586.1\|6439214_6439715_-\|GNAT-family-N-acetyltransferase	unknown	unknown	gnl\|CDD\|379112
NZ_CP043450.1\|WP_112575585.1\|6438662_6439097_+\|low-molecular-weight-phosphotyrosine-protein-phosphatase	unknown	unknown	gnl\|CDD\|319971
NZ_CP043450.1\|WP_112574701.1\|6440138_6441323_+\|DEAD/DEAH-box-helicase	cas3	cd09639_cas3_CAS-I	gnl\|CDD\|223587
NZ_CP043450.1\|WP_112575582.1\|6435756_6437154_+\|class-II-fumarate-hydratase	unknown	unknown	gnl\|CDD\|234779
NZ_CP043450.1\|WP_112572749.1\|6427220_6428741_+\|glutamate--tRNA-ligase	unknown	unknown	gnl\|CDD\|234953
NZ_CP043450.1\|WP_112574692.1\|6441408_6442404_+\|family-43-glycosylhydrolase	unknown	unknown	gnl\|CDD\|350148
NZ_CP043450.1\|WP_112575583.1\|6437360_6437789_+\|fumarate-hydratase	unknown	unknown	unknown
NZ_CP043450.1\|WP_112574691.1\|6442788_6444405_+\|aminopeptidase-P-family-protein	unknown	unknown	gnl\|CDD\|238520
NZ_CP043450.1\|WP_112572837.1\|6425346_6425859_-\|DinB-family-protein	unknown	unknown	gnl\|CDD\|378981
NZ_CP043450.1\|WP_112572740.1\|6432827_6433433_-\|DUF4142-domain-containing-protein	unknown	unknown	gnl\|CDD\|379301

Protein	Function_ID	Function_description	E-value
NZ_CP043450.1\|WP_112572744.1\|6431159_6431648_-\|thioredoxin-fold-domain-containing-protein	gnl\|CDD\|379034	pfam13098, Thioredoxin_2, Thioredoxin-like domain.	7.51938e-05
NZ_CP043450.1\|WP_112572747.1\|6428855_6429575_-\|2-phosphosulfolactate-phosphatase	gnl\|CDD\|377205	pfam04029, 2-ph_phosp, 2-phosphosulpholactate phosphatase. Thought to catalyze 2-phosphosulpholactate = sulpholactate + phosphate. Probable magnesium cofactor. Involved in the second step of coenzyme M biosynthesis. Inhibited by vanadate in Methanococcus jannaschii. Also known as the ComB family.	5.44867e-104
NZ_CP043450.1\|WP_112572751.1\|6425836_6427051_-\|HAMP-domain-containing-histidine-kinase	gnl\|CDD\|223715	COG0642, BaeS, Signal transduction histidine kinase [Signal transduction mechanisms].	2.90304e-31
NZ_CP043450.1\|WP_112572740.1\|6432827_6433433_-\|DUF4142-domain-containing-protein	gnl\|CDD\|379301	pfam13628, DUF4142, Domain of unknown function (DUF4142). This is a bacterial family of unknown function.	3.68563e-43
NZ_CP043450.1\|WP_090532309.1\|6445206_6445584_-\|30S-ribosome-binding-factor-RbfA	gnl\|CDD\|376719	pfam02033, RBFA, Ribosome-binding factor A.	2.1861e-29
NZ_CP043450.1\|WP_112575586.1\|6439214_6439715_-\|GNAT-family-N-acetyltransferase	gnl\|CDD\|379112	pfam13302, Acetyltransf_3, Acetyltransferase (GNAT) domain. This domain catalyzes N-acetyltransferase reactions.	1.27201e-33
NZ_CP043450.1\|WP_112572742.1\|6431687_6432704_-\|oxidoreductase	gnl\|CDD\|183212	PRK11579, PRK11579, putative oxidoreductase; Provisional.	5.15094e-74
NZ_CP043450.1\|WP_112575584.1\|6437788_6438583_+\|S1/P1-nuclease	gnl\|CDD\|211382	cd11010, S1-P1_nuclease, S1/P1 nucleases and related enzymes. This family summarizes both S1 and P1 nucleases (EC:3.1.30.1) which cleave RNA and single stranded DNA with no base specificity. S1 nuclease is more active on DNA than RNA. Its reaction products are oligonucleotides or single nucleotides with 5' phosphoryl groups. Although its primary substrate is single-stranded, it may also introduce single-stranded breaks in double-stranded DNA or RNA, or DNA-RNA hybrids. It is used as a reagent in nuclease protection assays and in removing single stranded tails from DNA molecules to create blunt ended molecules and opening hairpin loops generated during synthesis of double stranded cDNA. P1 nuclease cleaves its substrate at every position yielding nucleoside 5' monophosphates, and it does not recognize or act on double-stranded DNA. It is useful at removing single stranded strands hanging off the end of double stranded DNA and at completely cleaving melted DNA for simple DNA composition analysis.	2.75629e-78
NZ_CP043450.1\|WP_112574690.1\|6444495_6445203_-\|peptidoglycan-DD-metalloendopeptidase-family-protein	gnl\|CDD\|180426	PRK06148, PRK06148, hypothetical protein; Provisional.	2.91227e-41
NZ_CP043450.1\|WP_112572746.1\|6429665_6430745_-\|glycine-cleavage-system-aminomethyltransferase-GcvT	gnl\|CDD\|234742	PRK00389, gcvT, glycine cleavage system aminomethyltransferase GcvT.	0
NZ_CP043450.1\|WP_112575585.1\|6438662_6439097_+\|low-molecular-weight-phosphotyrosine-protein-phosphatase	gnl\|CDD\|319971	cd16343, LMWPTP, Low molecular weight protein tyrosine phosphatase. Low molecular weight protein tyrosine phosphatases (LMW-PTP) are a family of small soluble single-domain enzymes that are characterized by a highly conserved active site motif (V/I)CXGNXCRS and share no sequence similarity with other types of protein tyrosine phosphatases (PTPs). LMW-PTPs play important roles in many biological processes and are widely distributed in prokaryotes and eukaryotes.	1.26958e-67
NZ_CP043450.1\|WP_112574701.1\|6440138_6441323_+\|DEAD/DEAH-box-helicase	gnl\|CDD\|223587	COG0513, SrmB, Superfamily II DNA and RNA helicases [DNA replication, recombination, and repair / Transcription / Translation, ribosomal structure and biogenesis].	2.16652e-133
NZ_CP043450.1\|WP_112575582.1\|6435756_6437154_+\|class-II-fumarate-hydratase	gnl\|CDD\|234779	PRK00485, fumC, fumarate hydratase; Reviewed.	0
NZ_CP043450.1\|WP_112572749.1\|6427220_6428741_+\|glutamate--tRNA-ligase	gnl\|CDD\|234953	PRK01406, gltX, glutamyl-tRNA synthetase; Reviewed.	0
NZ_CP043450.1\|WP_112574692.1\|6441408_6442404_+\|family-43-glycosylhydrolase	gnl\|CDD\|350148	cd18827, GH43_XlnD-like, Glycosyl hydrolase family 43 protein such as Aspergillus niger DMS1957 xylanase D (XlnD); includes mostly xylanases. This glycosyl hydrolase family 43 (GH43) subgroup includes enzymes that have mostly been annotated as xylanases (endo-alpha-L-arabinanase, EC 3.2.1.8). It belongs to the GH43_bXyl-like subgroup of the glycosyl hydrolase clan F (according to carbohydrate-active enzymes database (CAZY)) which includes family 43 (GH43) and 62 (GH62) families. The GH43_bXyl-like subgroup includes enzymes that have been annotated as xylan-digesting beta-xylosidases (EC 3.2.1.37) and xylanases, as well the Bacteroides thetaiotaomicron VPI-5482 alpha-L-arabinofuranosidases (EC 3.2.1.55) (BT3675;BT_3675) and (BT3662;BT_3662). 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.	0
NZ_CP043450.1\|WP_112574691.1\|6442788_6444405_+\|aminopeptidase-P-family-protein	gnl\|CDD\|238520	cd01087, Prolidase, Prolidase. E.C. 3.4.13.9. Also known as Xaa-Pro dipeptidase, X-Pro dipeptidase, proline dipeptidase., imidodipeptidase, peptidase D, gamma-peptidase. Catalyses hydrolysis of Xaa-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-Pro.	6.95527e-95
NZ_CP043450.1\|WP_112572837.1\|6425346_6425859_-\|DinB-family-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.	1.22832e-19

>NZ_CP043450.1|WP_112572736.1|6434278_6434938_+|hypothetical-protein
MKNLILALLLLMACTASAQQKFNPVLKKQLDSVLALDQKYREILTYLMDPGKKDSILKTLPVKPEEATGYYWKLQTQADSTNLVFIENVVAKYGYPGKSLVGEPTNEAVWSVVQHSPKIDKYLPAIKTAAENKEMPFRLYAMMLDRQLMYEGKEQIYGSQATSKPLRNGQKVGYYVWPIKDAAKVNERRKQAGFDQTVEQNAKRLGFDYKVVKIEDVKW
>NZ_CP043450.1|WP_112572738.1|6433633_6434239_+|hypothetical-protein
MLIGSLFLGKVHEVNGQWIETKFVVIGIPLFPTSSMLVTRSAWRSRNGFNIPLNYQSIIAGYARMFSLIIAFIAFILFFIERDSTASIIGGAGLLLWLYFYFVFGSADTAEAEERKKMGDLTGLYIKPEWLDHDDAYRIYERLEKKYRNEFDGADWLTDLQQNEIAPAKLPLLYALSRFNYSLGATECNRKLFEKADSLYL
>NZ_CP043450.1|WP_112572740.1|6432827_6433433_-|DUF4142-domain-containing-protein
MKKLSLIAMMALAALSFQACNGGAKNGAADSSAAVKDTADSANKVKDTTTTGATGIAVTADDAKFATGAANAGLAEVAIGQLASEKATNAKVKDFAKMMVTDHTKANDELMALAKTKNISLPTEPDADHQKKKTELAAKSGADFDKAYVDAMVDGHKKVASMFEDASKNCKDPDLKAWAAKTLPTIQHHLAEIEAIQKGMK
>NZ_CP043450.1|WP_112572742.1|6431687_6432704_-|oxidoreductase
MSKPIVTGLMAYGMSGRIFHAPFLTTNPGFTFKAVVERHEKKAGKKYPDVISYDTIDELLNDDELELIIVNTPNNTHFDYAVQALNAGKHVLIEKPAAVTSHEVKALYDLGKKLDLKVMIYQNRRYDSGFLSVKEVIESGRLGELMEVHFRLDRYRMAIGVKKFKETAGVPGGGLTYDLGAHLVDNAISIFGRPLSYEKTTAAYRPGSQVDDYFNIHLKYPNQLNVFLTSGLLIAEHTYGFVVHGTLGSFVKMRTDVQEAQLDADMMPTDEGFGIEPEGSDGKLVLMGADGQKTVEWIKSPKGNYNGIFDAVYHTVRENALFPVAEEHVAWQIELLES
>NZ_CP043450.1|WP_112572744.1|6431159_6431648_-|thioredoxin-fold-domain-containing-protein
MKKLYLLLCLIIATGCSQAQTPPANSGLPPYHILTTDSVYVTPANLKKNKPVMVIYFSPDCSHCQHLMYDLKPELPKLKDVQIVMITFMPMLKGIQTFQRDFDLAKYHNITIGTEGYTYLVQRFYAVQTTPYIAIYDKYGKLFQSYPKVPKIPVLMETLKKV
>NZ_CP043450.1|WP_112572746.1|6429665_6430745_-|glycine-cleavage-system-aminomethyltransferase-GcvT
MKNTALTDIHVKTGAKMVPFAGYNMPVQYAGINAEHETVRKAVGVFDVSHMGEFILKGDNALDLIQRVTSNDAAKLYDGKVQYSCLPNETGGIVDDLLVYRIDEKTYMLVVNASNIEKDWDWISKYNTNGVDMKNISDRTSLLAIQGPKAAEALQSLTEVDLVSMEYYTFQKGTFAGIDNVLISATGYTGAGGFEIYFENQYAEQIWDAIFKAGEPFGIKPIGLGARDTLRLEMGFCLYGNDIDDNTSPLEAGLGWVTKFNKEFTNAEALQAQKQAGVSRKLVGFEMIDRGIPRHDYAIVDADGNNIGKVTSGTQSPSLQKAIGMGYVDTAFAKEGTEIYISIRDNKIKAQIVKPPFYK
>NZ_CP043450.1|WP_112572747.1|6428855_6429575_-|2-phosphosulfolactate-phosphatase
MKKDLHVCLTPALLPLFNVEDYIVVVIDIFRATSSICYGIENGAEAIIPVSQVEECAAYREKGLDYLLAAERDGSVVDGFDFGNSPFSYTKEKVAGKTIVLTTTNGTHALHLSRSAKKIVIGSFLNLNALSNWLNTQNENILLVCAGWKNNFNLEDTLFAGAVVDQLKDKGFVLDDAAIAANDLFQAGKNDINVYLKKTSHGERLKKLGIEKDIEFCLQIDFTTAIPILEGEKLVKLAV
>NZ_CP043450.1|WP_112572749.1|6427220_6428741_+|glutamate--tRNA-ligase
MTDKKVRVRFAPSPTGGLHLGGVRTVLFNYLFAKKHGGDFVLRIEDTDQTRYVEGAEEYILDCLKWCGLHPDESPVAGGPYAPYRQSERKVLYREYAERLVMEGHAYYAFDTAEELDKNRKEVPNFQYGLAYRHTLRNSLSLPQHEVDELLAAGTPHVIRIKMPEGETVNFNDMIRGHVSFETSQVDDKVLLKADGMPTYHLAVVVDDYLMKITHAFRGEEWLPSAPVHLLLWEYLGWKADMPQWAHLPLILKPDGHGKLSKRDGARLGFPVYAMNWFDAKSGELTQGFRELGFLPEAFLNLLATLGWNDGTEQEIFTLDELIEKFSIERVNKSGAKFDFEKAKWFNAEWIKKLAVGDLQLAVKKVFADKGVAVNDDEYLAKVVGLIKDRCVLLPDFYQQAGFFFEQPAAYDLNAVKPKWTDTKTEFYREFIALLNNESTIDAHELEAKFKALSEQKGLKVGDVMLPFRIMLVGGKFGPHVFDIVALLGKEETISRIEKALVAFTA
>NZ_CP043450.1|WP_112572751.1|6425836_6427051_-|HAMP-domain-containing-histidine-kinase
MNPYQQKKRWKYLLLTFAVVIAIGSLVYTRYLVKNIARSERTRAQVWAMTMRQLLNSDDDDFFNYVIAVRDSLTVPAIITDEKGEIILSRGLDTSKAYTKLEAEYKKKKYDPSYFKEELAYMKEQHAPIKFKVLGDDNYVYYKDSALLTQLRLFPYVQLTVIAIFLLTAYTAFSSSRKSEQDQVWVGLAKETAHQLGTPISSLIAWIELMKEKFNAEDDVLIAEMENDVKRLEIVADRFSKIGSKSVLEEHGVYAVVKDFVDYFKVRVSKNISFELTGNPHLKAGLNIPLFDWVIENILKNAVNAIEGKGSIKVEISGNKVKNQIFIDITDTGKGIPRSKFDTVFQPGYTTRKRGWGLGLSLTKRIVENYHNGQIFVKDSEVGKGTTFRIVLKNTRNDNKTKTR
>NZ_CP043450.1|WP_112572837.1|6425346_6425859_-|DinB-family-protein
MTKPKPGDYSPFAAGYVGLVGDNNVINMLEQQMDTSYKLFSNLTNEQGLYAYAPDKWTVKQALGHMIDTERTFAYRALVFSRNYTELPGFDQDVYVNNTDFNSQDIKDLAEEFRALRQANLYMVKAFTDEQLARTGIASNHLFTVISFVYMLAGHERHHLNLFKERYGIE
>NZ_CP043450.1|WP_112575582.1|6435756_6437154_+|class-II-fumarate-hydratase
MSFRTEHDTMGEVQVPADKYWGAQTERSRNNFKIGPEASMPKEIIDAFAYLKKAAAFTNTDLGVLSAEKRDLIAQVCDEILAGGLASEFPLVIWQTGSGTQSNMNVNEVVANRAHVLQGNKLGEGKTFIHPNDDVNKSQSSNDTYPTAMHIAAYKILIDVTIPGIEKLRDTLQAKVEAFKSVVKIGRTHLMDATPLTLGQEFSGYVSQLNHGLKALRNTLDHLSELALGGTAVGTGINTPKGYDVKVAEYIAQFTGLPFITAENKFEALAAHDAIVESHGALKQIAVSLMKIANDIRMLASGPRSGIGEIHIPDNEPGSSIMPGKVNPTQNEAVTMVAAQVMGNDVAISIGGSNGHYELNVFKPVMAANFLQSARLIGDACVSFNDHCAVGIEPNYEGIKKHLENSLMLVTALNPHIGYENAAKIAKTALKNGSSLREAAIGLGLLTNEQFDEWVRPENMIGSLK
>NZ_CP043450.1|WP_112575583.1|6437360_6437789_+|fumarate-hydratase
MQEPGDSKLQGEWRQDSVPAQKSLVTYSLYDIKFSCDSFLLKISTVSKVNYGADTCMSKGHWAEYVRGTYSQRQDTLHIKGQFCNADGSYKNEQGCFRFGDYEEYFKVHRTGDSLIRFVSTSNVIPINAHLIKRTSCIPKPL
>NZ_CP043450.1|WP_112575584.1|6437788_6438583_+|S1/P1-nuclease
MKTQILKKLLLLVAIFYIPLQSMAWGTNGHRICGQVADSYLTPKARKAIEAILGNESVAITSNWADFIKSDPAYGYLYNWHFIDLDKAYTYPELQGYLKADTAVDAYTKMNFLIAELKKKTTTKTNKLLYLRMLIHIVEDVHQPLHTGHTSDKGGNDVKVQWFGKDSNLHSVWDSQLIDFQQLSYTEYATMINHTTAAQRAKLQKDPISQWLYESNQLAEKLYTDVKPGENLSYKYNFKYIGILNDQMVKAGVRLAGVLNQIFG
>NZ_CP043450.1|WP_112575585.1|6438662_6439097_+|low-molecular-weight-phosphotyrosine-protein-phosphatase
MKILMVCLGNICRSPLAEGIMQHLADENGLGWDVDSAGTGRWHIGEAPDRRSIRAARNHGIDISKQVCRQFKRSDFDEFDHIFVMDRNNLSDVLDMARNEEQAAKVKLLLGDKVVPDPYYDDSQFEPVFELIESGCKDIIKDLR
>NZ_CP043450.1|WP_112575586.1|6439214_6439715_-|GNAT-family-N-acetyltransferase
MNIITQTPRLLIRELTAEDEELLLTIDEDDRLTQYVKKRTPQESKQVFKDTLKEYKNGSGLGRWGIFNIADNDFIGVCALKPSDYDRSRIELGYRLHLKYWGQGVATELAEALVSYGLNKIGLKEVCAVTHPQNVASQRVLIKAGFAKEGIVFWYGEDVPFFRIER
>NZ_CP043450.1|WP_112574701.1|6440138_6441323_+|DEAD/DEAH-box-helicase
MGFVNPTPIQSMAIPAIMEGRDLIACAQTGTGKTGAYLLPVLNSISKTNKHHTSALILAPTRELAQQIDQQVEGLAYFTGISSIAVFGGGDGIVYEQQRRGIQNNVNIIVATPGRLIAHLTSGVLKLNHLTHLILDEADRMLDMGFSDDIMKIISYLPKERQTLLFSATMPGRIRSLAKAILKDPEQINIAISQPAVGIDQQVYRVHDQQKTPLVQHILKDSAFTSIIIFASRKEIVKSLYKELKAIKINAMSFHSDLEQKEREEILLKFKNKQLPVIIGTDALSRGIDVEGIDLVINYDVPGDPEDYIHRIGRTARAATTGTAITFVNHRDERKLKNIEKLIEKPIKLMVLPDELATIQPLKPEPVQGDAKKKPNRRWGKKKPKQQNTGNQKA
>NZ_CP043450.1|WP_112574692.1|6441408_6442404_+|family-43-glycosylhydrolase
MFISRKIMFLLGAGLALSSIANKAVAQEKKTSGNPIVEGWYADPEAKIFNKQYWVYPTYSAKYNDQVFMDAFSSPDLVNWTKHPRIIDTAAVKWAKRAMWAPAVTEKDGKYYIFFGANDIQNNNEVGGIGVAVGDKPEGPFKDLLGKPLIGQIINKAQPIDQFVFKDDDGQYYMIYGGWGQCNIVRLKNDFTGIEPFKDGETYKLITPKDYVEGPVMFKRKGKYYFMWSEGGWTGPDYRVAYAIGDSPFGPFNRIGTILKQDASIATGAGHHSVIQVPGKDEWYIVYHRRPLTETDGNHRVTCIDKMYFDKDGKILPVKITNEGVTARKIK
>NZ_CP043450.1|WP_112574691.1|6442788_6444405_+|aminopeptidase-P-family-protein
MTRSFFRALVFLLALAGSSHCFGQAAENLPTDYLSKEFHAGRRQALRDLMPANSVTVIFSYPEQVFSNDVNYVYHPNPDLYYFSGYKEPNSVLLVFKDTQADGDSSYNEVLFVRHRDAGREQWTGRRLGVEGAKSQLGFKRAYNSEDFAKFPVDFKKFANVYYDTLPEDVTGDGSTGELKKLIAAFKAKAGIPDVDRQAVNDMNLIANRTTPQNLSRMVTFFKSRYNNDITKASPLVQELLAKPDSVTLMAVKAKIGNTLGGNVGFSTFTSKLRGVKTTEELAVLKKAVQISSLAHLEVMKSVKPTMSEREVEGIMTYVHKRYGAEDEGYPPIVGAGGNGCILHYEENSATKINNQLLLMDVGAEYHGYSADVTRTVPANGKFTEEQKAIYQLVYDAQEEIFKLCKAGVPYASLEQKSAEVLADGLIKLGIIKNASEVRRYYPHGCSHHLGLDVHDKGGRSNLEENWVITVEPGIYIPAGSPCDKKWWNIGVRIEDDVQIGKDGGTILSIDAPRKWQDVEKAATEKSIFEAAKFPELK
>NZ_CP043450.1|WP_112574690.1|6444495_6445203_-|peptidoglycan-DD-metalloendopeptidase-family-protein
MDRHALLTNFINNHPEAIGKVVDFDHERDHLYQLDLTAANNELTAEVINNTPLFSSWVNSKLRDNNCRYGIGGYMEHRTIYAFSSHFDTDDEPRRLHLGVDIWGDAGTPIYTPLDGLVHSYQDNNNIGDYGPTIILQHDLDGLTLYSLYGHLSRKSLEGLLVGMPVFKDQQIATLGDINENGQWPPHLHFQLMFDMAGKQGDYPGVCKFSEKEIWQKNIPDPGLILRFPDAVNVE
>NZ_CP043450.1|WP_090532309.1|6445206_6445584_-|30S-ribosome-binding-factor-RbfA
MESKRQQKFAGVIQEDLAAIFQREGMNYLPNTLVTITKVRVTPDLAIARIFLSFLGNPNVQTALHTIKSHASEIRYKLGARIKDQVRIIPQLEFFVDDTSEYVERMDKIFDKISKEERQPDTEEN

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Crispr_ID: NZ_CP043450_12

CRISPR_ID

CRISPR_location

CRISPR_type

Repeat_type

Spacer_info

Cas_protein_info

CRISPR-Cas_info

NZ_CP043450_12

6510253-6510353

Orphan

Consensus_repeat	Method
TTAATTAGTAGCAGGTTTTAGTTGCAGTAGCAG	CRISPRCasFinder

1 spacers

The CRISPR arrays of NZ_CP043450_12

>merge|NZ_CP043450|12|6510253-6510353|CRISPRCasFinder
TTAATTAGTAGCAGGTTTTAGTTGCAGTAGCAGCGGAGCTGTTTAAAAAAAATAAAGGCCCGGTTCACTTAATTAGTAGCAGGTTTTAGTTGCAGTAGCAG

>NZ_CP043450|12|12|6510253-6510353|CRISPRCasFinder
TTAATTAGTAGCAGGTTTTAGTTGCAGTAGCAG	CGGAGCTGTTTAAAAAAAATAAAGGCCCGGTTCAC
TTAATTAGTAGCAGGTTTTAGTTGCAGTAGCAG

Protein	Signature genes	Signature genes Name	Protein_function
NZ_CP043450.1\|WP_112574633.1\|6514692_6515037_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112574640.1\|6507359_6509339_-\|dehydrogenase	unknown	unknown	gnl\|CDD\|223101
NZ_CP043450.1\|WP_112574644.1\|6501974_6503576_-\|monooxygenase	unknown	unknown	gnl\|CDD\|366675
NZ_CP043450.1\|WP_112574628.1\|6517757_6518414_-\|metal-dependent-transcriptional-regulator	unknown	unknown	gnl\|CDD\|224240
NZ_CP043450.1\|WP_112574638.1\|6510429_6510825_-\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112574630.1\|6516508_6517102_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112574643.1\|6503572_6504289_-\|SAM-dependent-methyltransferase	unknown	unknown	gnl\|CDD\|381176
NZ_CP043450.1\|WP_112574641.1\|6505293_6507237_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112574631.1\|6516252_6516471_+\|alkylphosphonate-utilization-protein	unknown	unknown	gnl\|CDD\|225380
NZ_CP043450.1\|WP_112574646.1\|6498992_6499694_+\|response-regulator-transcription-factor	unknown	unknown	gnl\|CDD\|225818
NZ_CP043450.1\|WP_112574634.1\|6513498_6514686_+\|DUF5009-domain-containing-protein	unknown	unknown	gnl\|CDD\|226749
NZ_CP043450.1\|WP_112574632.1\|6515189_6516173_+\|pyruvate-dehydrogenase-complex-E1-component-subunit-beta	unknown	unknown	gnl\|CDD\|237011
NZ_CP043450.1\|WP_112574647.1\|6497805_6498987_+\|sensor-histidine-kinase	unknown	unknown	gnl\|CDD\|377675
NZ_CP043450.1\|WP_112574645.1\|6499934_6501851_+\|gliding-motility-associated-C-terminal-domain-containing-protein	unknown	unknown	gnl\|CDD\|372639
NZ_CP043450.1\|WP_112574629.1\|6517169_6517667_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112574635.1\|6512359_6513415_+\|4-hydroxythreonine-4-phosphate-dehydrogenase-PdxA	unknown	unknown	gnl\|CDD\|377232
NZ_CP043450.1\|WP_112574698.1\|6497018_6497603_+\|tRNA-(ms[2]io[6]A)-hydroxylase	unknown	unknown	gnl\|CDD\|153119
NZ_CP043450.1\|WP_112574639.1\|6509398_6510250_+\|DUF4198-domain-containing-protein	unknown	unknown	gnl\|CDD\|378467
NZ_CP043450.1\|WP_112574642.1\|6504343_6505060_+\|hypothetical-protein	unknown	unknown	unknown
NZ_CP043450.1\|WP_112574636.1\|6511343_6512123_-\|16S-rRNA-(adenine(1518)-N(6)/adenine(1519)-N(6))--dimethyltransferase-RsmA	unknown	unknown	gnl\|CDD\|234708

Protein	Function_ID	Function_description	E-value
NZ_CP043450.1\|WP_112574628.1\|6517757_6518414_-\|metal-dependent-transcriptional-regulator	gnl\|CDD\|224240	COG1321, TroR, Mn-dependent transcriptional regulator [Transcription].	5.47697e-43
NZ_CP043450.1\|WP_112574640.1\|6507359_6509339_-\|dehydrogenase	gnl\|CDD\|223101	COG0022, AcoB, Pyruvate/2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component, eukaryotic type, beta subunit [Energy production and conversion].	3.1429e-144
NZ_CP043450.1\|WP_112574644.1\|6501974_6503576_-\|monooxygenase	gnl\|CDD\|366675	pfam01494, FAD_binding_3, FAD binding domain. This domain is involved in FAD binding in a number of enzymes.	1.97834e-86
NZ_CP043450.1\|WP_112574636.1\|6511343_6512123_-\|16S-rRNA-(adenine(1518)-N(6)/adenine(1519)-N(6))--dimethyltransferase-RsmA	gnl\|CDD\|234708	PRK00274, ksgA, 16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase RsmA.	9.71795e-106
NZ_CP043450.1\|WP_112574634.1\|6513498_6514686_+\|DUF5009-domain-containing-protein	gnl\|CDD\|226749	COG4299, COG4299, Uncharacterized protein conserved in bacteria [Function unknown].	2.00442e-11
NZ_CP043450.1\|WP_112574631.1\|6516252_6516471_+\|alkylphosphonate-utilization-protein	gnl\|CDD\|225380	COG2824, PhnA, Uncharacterized Zn-ribbon-containing protein involved in phosphonate metabolism [Inorganic ion transport and metabolism].	6.64899e-32
NZ_CP043450.1\|WP_112574646.1\|6498992_6499694_+\|response-regulator-transcription-factor	gnl\|CDD\|225818	COG3279, LytT, Response regulator of the LytR/AlgR family [Transcription / Signal transduction mechanisms].	4.76094e-44
NZ_CP043450.1\|WP_112574632.1\|6515189_6516173_+\|pyruvate-dehydrogenase-complex-E1-component-subunit-beta	gnl\|CDD\|237011	PRK11892, PRK11892, pyruvate dehydrogenase subunit beta; Provisional.	0
NZ_CP043450.1\|WP_112574647.1\|6497805_6498987_+\|sensor-histidine-kinase	gnl\|CDD\|377675	pfam06580, His_kinase, Histidine kinase. This family represents a region within bacterial histidine kinase enzymes. Two-component signal transduction systems such as those mediated by histidine kinase are integral parts of bacterial cellular regulatory processes, and are used to regulate the expression of genes involved in virulence. Members of this family often contain pfam02518 and/or pfam00672.	3.01735e-30
NZ_CP043450.1\|WP_112574645.1\|6499934_6501851_+\|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.	2.38334e-31
NZ_CP043450.1\|WP_112574635.1\|6512359_6513415_+\|4-hydroxythreonine-4-phosphate-dehydrogenase-PdxA	gnl\|CDD\|377232	pfam04166, PdxA, Pyridoxal phosphate biosynthetic protein PdxA. In Escherichia coli the coenzyme pyridoxal 5'-phosphate is synthesized de novo by a pathway that is thought to involve the condensation of 4-(phosphohydroxy)-L-threonine and 1-deoxy-D-xylulose, catalyzed by the enzymes PdxA and PdxJ, to form either pyridoxine (vitamin B6) or pyridoxine 5'-phosphate.	1.41606e-143
NZ_CP043450.1\|WP_112574698.1\|6497018_6497603_+\|tRNA-(ms[2]io[6]A)-hydroxylase	gnl\|CDD\|153119	cd07910, MiaE, MiaE tRNA-modifying nonheme diiron monooxygenase, ferritin-like diiron-binding domain. MiaE is a nonheme diiron monooxygenase that catalyzes the posttranscriptional allylic hydroxylation of a modified nucleoside in tRNA called 2-methylthio-N-6-isopentenyl adenosine (ms2i6A). ms2i6A is found at position 37, next to the anticodon at the 3' position in almost all eukaryotic and bacterial tRNA's that read codons beginning with uridine. The miaE gene is absent in Escherichia coli, a finding consistent with the absence of the hydroxylated derivative of ms2i6A in this species.	1.2511e-80
NZ_CP043450.1\|WP_112574639.1\|6509398_6510250_+\|DUF4198-domain-containing-protein	gnl\|CDD\|378467	pfam10670, DUF4198, Domain of unknown function (DUF4198). This family was previously missannotated in Pfam as NikM.	1.52158e-20
NZ_CP043450.1\|WP_112574643.1\|6503572_6504289_-\|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.	1.30152e-139

>NZ_CP043450.1|WP_112574639.1|6509398_6510250_+|DUF4198-domain-containing-protein
MKRTGILLLVLLLLIGFAASSQDFFLLPHNFYVHKGDKLNLHLLSGNEFKPENEFIYAKAKATKFMLYEGSKKTDLSKSSNPADSSLLTYELQNSGLALFELVREDETESERNKFIRALESEGLDKMAEEARASSQQYFVERYHQSSKTLISVDKANGKDFDKPLGEDYEIVIQQNPYKSAYGDDVTAQILFKGKPMKDAAVIQYVRTLNGTIIPQKLLSDNNGLVFFKLSREGVYMISSTHVEPAQDKKADYENWTATFTFAFSNTDDTPNTYREFGFGNKH
>NZ_CP043450.1|WP_112574640.1|6507359_6509339_-|dehydrogenase
MIFDRKNLDNDTLLAFYKKLLFPRMVEEKMLILLRQGRIGKWFSGIGQEAIAVGSALAMNPDEYILPMHRNLGVFTSRGIPLSRLMAQWQGKPSGFTKGRDRSFHFGTQEYKIIGMISHLGPQLALADGIALADVLSGKKKSTLVFTGEGATSEGDFHEALNIASVWKLPVIFLIENNGYALSTPTNEQYNCRELIDKAIGYGMEGRRIDGNNLLEVYNTITTLNKAIRENPRPILLECMTFRMRGHEEASGTKYVPNNLFEWWAGKDPVANFEKYLLTEGVLLKDMIPAIRKEFAAIIETEIEKVYAEADIIPDIATEVQDMYKPYSFPAAKPQPAAVTNKRYIDAISDGLKQAMRKHPNLVIMGQDIAEYGGAFKITQGFVEEFGKARIRNTPICESAIVGAGMGLAINGYKAVVEMQFADFVTCGFNQVVNNLAKTHYRWGQGVDVVIRMPTGAGTGAGPFHSQSNEAWFTKTPGLKVVYPATPADAKGLLLAAIDDPNPVIYFEHKYLYRSISADVPDNEVMIEIGKANVIKQGEKASIITFGLGVHWALEYADKHPDQSIEIIDLRSLQPWDQEAVEASVKKTGRALILHEDTLTSGFGAEIAAHIAEHCFKYLDAPVIRCGSLDTAIPMNKALEDQFMAKARLEQTMERLLAY
>NZ_CP043450.1|WP_112574641.1|6505293_6507237_+|hypothetical-protein
MRKLLIAFLLLNGFVSQAQIKPSGILLNDKNARVKTAKEFSVVSASDSNHPVELTFQTHTCVGVSREDNKWYVLPLNDASGKISANTNLWILPQNALSKDNSYLIKLSGSDSVTAVSENDRLKVNVYSKKFELYTAEARPHSDCFNNRYALNIQGGDAFANTLAGFYWGTMLQSVIEKTKAKNYPYSSGYVISTLNPKAYAGSYPDVDHEFQIKGRLAFASDLDIDVVRRMMELQFKLMQDDPEGLFRDPCSVQPSGEREYHIRRNSQNNKVNANMFLLTGNMEIQEEAFHYFEATKDSAWLSKNIENLEKAAALTIANTDQYGRVWSDVYYEDQVMKDGRETMSGALAAYTFQLLAQMESILNRGNKSDYYAGFSKKIAHQLVQPLPQGFWDEQEQRFVDWVDRSGVKHNHIHLLANILPAMFGYTTEAQTQAVAKLVNSNLAEFQRFPSFISADVAAYDKNEIGDGGPYDLCAAGRYWWWDASYWKWLNNNEMLYNQLKTVAAEAVKDSYYMGERYDMNHVYYVDNKDWHGADMYYEYPCVYTSILIDNYLGIQHTLNADLSIKPKVNGYGTIEFTNPLYNIRYTITAKGFKLKNLSNKPRRFAVDLSSVFKGKQLKLAGKLRIESPDAVITLAANEEANWVLSN
>NZ_CP043450.1|WP_112574642.1|6504343_6505060_+|hypothetical-protein
MRQLGANWFIEGHIDFEYKKYILLSYLQEINSHFDNSRLYPNLADLIFHYNNLIDFKTNKSLLQQAFPQRLSQADIDAVKLTYQKIITDDQSMQEIEHIITYALGKIDPAIKTGRDIYDFVERHVNIDPVGIIPLMPYHGYFSLRNGKESTNRIYEYQITIFEGKDDKYRGINISFVDTYEQSIANTPESIKLHLINRNKFIPNPAVYYVHSDITFPLEQTLLPVAKRSLVKFISNAA
>NZ_CP043450.1|WP_112574643.1|6503572_6504289_-|SAM-dependent-methyltransferase
MPYGTLYLIPVPLADDAAAKSFTPYLVDTINSIKEYIVENEKTARRFLKEAGLKTPQSELVIHDYGKHNRDMGNADFFKGLQAGNDVGLMSEAGCPGVADPGAEIVDKAHRMGIKVVPLVGPSSILLALMASGFSGQSFAFHGYLPIDKVLRAKKIKELESTAIKLDQTQMFIETPFRNNPMLEEILKSGNPKTKLCIACDLTAATELVQTKTIADWQKKVPDLHKRPTIFLLYHGNK
>NZ_CP043450.1|WP_112574644.1|6501974_6503576_-|monooxygenase
MTISQQHTPVVIVGAGPSGLMMAAQLLRYGVQPVIIDSRQGPTSHSKALAVQARSMEIYRQMGIIDKVLIDGKRGGGVQFNQEGEEVAGLSLSNVGEAQTAFPFIQMYPQSKNERLLLDFITLNCCPVYWNTSLLSLNQNTEKVTLQLQSGEDKQTITCDWLIGADGAHSTVRKQLNIPFNGDTYQHQFYLADIKIDADFGDKVNLFLSKKGFAGFFPMPDERSYRVVGNLPDAFDKKDELQIEEALPHLREVTKQQIIVEQTNWFTTYRLHHRMADKFREQRCFLIGDAAHIHSPVGGQGMNTGLQDAYNLAWKLAGIVNNQLKASVLDSYAQERMPVAKDLLNTTDRIFKMILSRNWFINLLKKYLLPVVLKWVWSKPHLREAFFKRVSQTGIAYRDSSINLNLSHASQIKAGDRLPYLKVFDEKRQLETDLHEWCSKPGFTLICLGKLKEIDLFTLAKWITQNYGASLNFFYLPPSTKNQHIFDAFDVKENQKKALIIRPDMHIGFLNDVVDIDMMDNYLLNVAGVVHGL
>NZ_CP043450.1|WP_112574645.1|6499934_6501851_+|gliding-motility-associated-C-terminal-domain-containing-protein
MEAKKLLPLISFFLILLVRKTNAQSLGDPVVSITFGSGTSTHSGALPADSGSTSYPYSSADFPSDGYYTIENTTAGAGNVWWSATDHTGNTGGYMMVVNASRSLTDYFYKRTITGLCSNTTYQFSAWVVNLLRSNDISPPNITFAIEKTDGTTIQSYNTGTIARTSGTYKWVQESFNFTLPAGVGDVVIKMINNSAGGAPANDLAIDDIVFRPYGPVIAASFSSSSSTLTAAACSDVPQTYTLSTTIPSGYTVLWQSKNGNGAWTDLTGTNSTSSTYQIVSPTVAGTYYYRAVTAQAGNINSALCRSASNVLTLTVGAPPSSTATANTPVCAGTTLSLNASTGVSYKWTGPNGFTSVLQNPTIDNVTAAAAGNYSVTIKSSSGCEVTVPLSVIVNAQPVAAVAPVEPICEGSSVTLNASGGSTYSWSPTTGLSDAGIANPVASPTDTTLYTVTVSNGTCTSTAQVQVNVLKKPVANAGPDRHITHGQSVTLNGSAKGTNVSYYWTPTDNLSSSLELKPTASPLEDITYTLHVVSNSGCGDEATDEVFVRVYKKVVIPNTFTPNGDGVNDTWNIEALDTYPTSTTQVFNRYGGLVFKSTGYPKAWDGKYSGQDIPSGTYYYVIDLKNGNVMSGWVMVMR
>NZ_CP043450.1|WP_112574646.1|6498992_6499694_+|response-regulator-transcription-factor
MVLKCIAIDDEPLALRLINDYVSRFPALQMVNTFEDAISGAEFLKHNPVDLLFVDINMPDITGIDLVRSLDVKPMVIFTTAHKNFAYEGFELEALDYVLKPIDIKRFTKAVEKAVDYYKYRSKPAEEAAEESLYVYSEYRMVKIDLGTIEYIESMEDYIKIHITNEKTILTLMPMKKVLEKLPASKFQRIHRSYIVPVNKIRSIQNRKVQLTDVELPISESYNDFARNWAKQK
>NZ_CP043450.1|WP_112574647.1|6497805_6498987_+|sensor-histidine-kinase
MSRFKAFSVVIHIAGWLLFMAFPLVFLNSRAFYNTSITTFLQKPAYWVFCVTYMVLFYSNAYVFIPRFFLKKKYAIYSVIVVVLLAGVYLLRPFDKLMRSTDGWRMMNGMMMRHRPPFGGERFGNGSFGVPPDDTAAAFDRPPFRSDSAYFKAQSQWRRHRMRPLDSTSLFIFLMIMALSMAIKTVQQWQLTEQRAARAEADKTNAELSFLKAQINPHFLFNTLNNIYTLAAIKDDNAADSIMKLSNIMRYVTDDVAEDFVPLQSEIDCISDYIELQRLRIGKNTKVNFEVKGDIDHKQIAPLVMMTFVENVFKYGVSKHEPSDIDISVDIQGVKISFYCKNRIFGVQKSDYQRTGIGINNTKKRLDHLYPNKHLLSISSLNNEYIVQLTLQA
>NZ_CP043450.1|WP_112574698.1|6497018_6497603_+|tRNA-(ms[2]io[6]A)-hydroxylase
MLKLQLPTDPLWVKNVVESNIEEILTDHAFCEQKAASNAITLIVQNPNLSELVQEMALLVQEEMDHFKRVHDIILERGYILGRERKDNYVNELRKFIIVGGGREAQLIDRLLFSAMIEARSCERFKVLSENINDEQLAAFYHELMISEATHYSMFIRLAKKYAEEIDVDARWKQFLEYEAHVIQNYGKGETIHG
>NZ_CP043450.1|WP_112574638.1|6510429_6510825_-|hypothetical-protein
MKTSIKLSALFVLLTAGVFATKVAKADEGNADVNPKAKEVVSFKALDHDRGLKINFAKSENGKSVVKVYNKDNELLLKDIVPSKTDVSKGYVLNGLADGEYTMEIYSNNQVVKKSIHVYQDGDQKSFYIAQ
>NZ_CP043450.1|WP_112574636.1|6511343_6512123_-|16S-rRNA-(adenine(1518)-N(6)/adenine(1519)-N(6))--dimethyltransferase-RsmA
MTLVRAKKHLGQHFLTDKNIAAKIVDSLKPERRFGHVLEVGPGMGVLSDFLLQKTEYETSLIDIDTESYDFLKKKYPQLGNRLINADFLELDFKSIFPESFAIIGNFPYNISSQILFKVLDNRQQVVEVVGMFQKEVAERCAAKAGSKEYGILSVFLQAYYKVEYLFTVKAGVFNPPPKVLSAVIRLTRNEKQTLDCDEKLFWQIVKAGFNQRRKTLRNAISSLINKEKLTDEPMLELRAERLSVADFVALTNKVSATR
>NZ_CP043450.1|WP_112574635.1|6512359_6513415_+|4-hydroxythreonine-4-phosphate-dehydrogenase-PdxA
MSDKLKIGISIGDVNGIGLEIIIKTLADNKIYEYCTPIVYGHTKVASFHRRATQVNELNFLVINDPSQTHFRKPNMINCWEEDVKIELGQVTEAGGKYAFKSLERAVYDLKEGYIDALVTAPINKDNIQNEKFQFPGHTEYLQQYDGAAESLMFLVSDTLRVGVVTGHIPVSKIAESITAEKILAKLKLMNNSLQTDFWIRKPKIAVLGLNPHAGDNGLIGSEEKDIIIPAIEEARSNNILAFGPYSADGFFANGTYLQFDAVLAMYHDQGLIPFKQIAFESGVNFTAGLNFVRTSPDHGTAYDIAGKNQASEISFREALFTAIHIVKNRREGLELNENPLLFSKLSRDRD
>NZ_CP043450.1|WP_112574634.1|6513498_6514686_+|DUF5009-domain-containing-protein
MSNFLSRIRSIDAFRAVTMFLMIFVNDLDGIPNTPNWLKHAGSNVDALGLADTIFPAFLFIVGLSIPFAFQNRLKQGDNFKLLSRIVSRSFALIFIGFFHANMETYNEATTLLPKPVWESLVTFSFFFIFLDYSKDTPPRRRYLLQGFGILLLAGMAALYRTSDPGHVWLHFTWWGILGLIGWSYMLCALIYYYSEGHLWIQLAAWMFFMFFNLDVHFGFLDFIDRLQGYIWIAGNGAMQSFTMAGVFISVLYMRLKANNEMKMLWVAMILIAIILFNLGFIVRYFSGGISKERDTPSWVLICTGISLVVYAFFIFLVDVKNKYNWFKVIEPAGTNTFTCYIVPFLFYPIYEMSRIGYPEYLSQGTGGLIKCIVFAFVMVWLTGLLDKINIRIKI
>NZ_CP043450.1|WP_112574633.1|6514692_6515037_-|hypothetical-protein
MAYSKNGNQITFSNGNSVDFEYPVDEIFEIDDILVVILRIPSNVRDRRNVFAFSRTGDFLWQINDVPLYHNGDFCPFVGALINKENEFVLFNWCDTAVIIDPQTGDVMRRYQTK
>NZ_CP043450.1|WP_112574632.1|6515189_6516173_+|pyruvate-dehydrogenase-complex-E1-component-subunit-beta
MREIQFREALREAMVEEMRSDENIYLMGEEVAEYNGAYKVSQGMLDEFGAKRVIDTPISELGFAGIGIGSAMNGLRPIIEFMTFNFSLVAIDQIINGAAKMMSMSGGQFSVPIVFRGPTGNAGMLSSQHSQCFENWYANCPGLKVVVPSNPYDAKGLLKSAILDPDPVIFMESELMYGDKGEVPEETYYIPLGKAKVVKEGTDVTLVGFGKIMKVVVAAAAELEKEGIHAEVIDLRTVRPIDYATVIESVKKTNRLVIIEESWPLGSIATEVAFKVQKDAFDYLDAPILRITGGDVPLPYAPTLIQEYLPNPERVIKAVKQVMYVTK
>NZ_CP043450.1|WP_112574631.1|6516252_6516471_+|alkylphosphonate-utilization-protein
MDELIVKDSNGNILKDGDSVTLIKSLKVKGGGVTLKQGTLVKKIRLTDNDEEVDCKVDGMSIVLRTEFLKKR
>NZ_CP043450.1|WP_112574630.1|6516508_6517102_+|hypothetical-protein
MKYFIACVFLFTGLWAYGQKITPLEYVDAGTILKENQAIIYGSFIQRLTFWQNGYDQRIRIRNLETNELFSFEVKPATRTRKENPFCFFIKPGTYEVVNFYYSKAKWYGTEDNTRPVFRGIDFEVNVKNKIDSGLVKMEDLHRIVFKVENNTLTYLGKWHFESGAPSFSNDKAVLDKKLKEDYFFLEFEKAAMVLPD
>NZ_CP043450.1|WP_112574629.1|6517169_6517667_+|hypothetical-protein
MQYTYFKAFKPLFFIVSALIIAGNAAAQAQPAAATTAAPVAAVAGVQTHIDKFFKEYDKQSTARAVIDIFKTNKLMDSTRLTGLIVKIDSMRSVIGKYLGKDLIMQRKASNSLVLYSYLLKHESQPARITFMFYKPKNEWEIYRLYFDVDVDGELAESSRVTGKP
>NZ_CP043450.1|WP_112574628.1|6517757_6518414_-|metal-dependent-transcriptional-regulator
MYTLSEENYLKAIYRLASQGKDFKITPTAIADALSNNPASVVDMIRKLTEKQLIEYDKKKGVRLTPQGLKDAVLIVRRHRLWEVFLLEKLGYHWDEIHDIAEELEHINDATLADRLEKFLGFPEYDPHGDPIPKANGKVPKSYSVTLSELKPGSQSKVAAVRDTSSSFLQYLQKLNIGIGTKIQLIEKIPYDNSLVIKIEDREDTTVSQKFGENILVD

You can click texts colored in the table to view more detailed information

Click the colored protein region to show detailed information

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
NZ_CP043450_10	10.1\|6143865\|30\|NZ_CP043450\|CRISPRCasFinder	6143865-6143894	30	AP013618	Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C26D-MedDCM-OCT-S37-C143, * SEQUENCING IN PROGRESS *	11943-11972	6	0.8
NZ_CP043450_10	10.1\|6143865\|30\|NZ_CP043450\|CRISPRCasFinder	6143865-6143894	30	AP013610	Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C26-MedDCM-OCT-S45-C147, * SEQUENCING IN PROGRESS *	9274-9303	6	0.8
NZ_CP043450_10	10.1\|6143865\|30\|NZ_CP043450\|CRISPRCasFinder	6143865-6143894	30	AP013619	Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C26D-MedDCM-OCT-S43-C253, * SEQUENCING IN PROGRESS *	921-950	6	0.8
NZ_CP043450_9	9.1\|6143703\|30\|NZ_CP043450\|CRISPRCasFinder	6143703-6143732	30	NZ_CP041978	Bacillus pacificus strain NCCP 15909 plasmid unnamed1, complete sequence	165256-165285	7	0.767
NZ_CP043450_9	9.1\|6143703\|30\|NZ_CP043450\|CRISPRCasFinder	6143703-6143732	30	CP041980	Bacillus paranthracis strain NCCP 15910 plasmid unnamed, complete sequence	148209-148238	7	0.767
NZ_CP043450_9	9.1\|6143703\|30\|NZ_CP043450\|CRISPRCasFinder	6143703-6143732	30	NZ_CP040343	Bacillus cereus strain DLOU-Weihai plasmid unnamed1, complete sequence	295212-295241	7	0.767
NZ_CP043450_9	9.1\|6143703\|30\|NZ_CP043450\|CRISPRCasFinder	6143703-6143732	30	NZ_CP013927	Alteromonas stellipolaris strain LMG 21861 plasmid pASTE61-200, complete sequence	79512-79541	7	0.767
NZ_CP043450_9	9.1\|6143703\|30\|NZ_CP043450\|CRISPRCasFinder	6143703-6143732	30	NZ_CP013139	Pseudoalteromonas sp. Bsw20308 plasmid pPBSW1, complete sequence	567553-567582	7	0.767
NZ_CP043450_9	9.1\|6143703\|30\|NZ_CP043450\|CRISPRCasFinder	6143703-6143732	30	NZ_CP013709	Clostridium botulinum strain F634 plasmid pRSJ2_2, complete sequence	136315-136344	8	0.733
NZ_CP043450_9	9.1\|6143703\|30\|NZ_CP043450\|CRISPRCasFinder	6143703-6143732	30	NZ_CP013682	Clostridium botulinum strain 1169 plasmid pRSJ8_1, complete sequence	139392-139421	8	0.733
NZ_CP043450_9	9.1\|6143703\|30\|NZ_CP043450\|CRISPRCasFinder	6143703-6143732	30	NZ_CP013295	Clostridium botulinum strain CDC_54064 plasmid pNPD1_1, complete sequence	150108-150137	8	0.733
NZ_CP043450_9	9.1\|6143703\|30\|NZ_CP043450\|CRISPRCasFinder	6143703-6143732	30	NZ_CP013844	Clostridium botulinum strain A634 plasmid pRSJ19_2, complete sequence	181752-181781	8	0.733
NZ_CP043450_6	6.1\|4515169\|34\|NZ_CP043450\|CRISPRCasFinder	4515169-4515202	34	NZ_CP045303	Azotobacter salinestris strain KACC 13899 plasmid unnamed1, complete sequence	212251-212284	9	0.735
NZ_CP043450_7	7.1\|5186540\|34\|NZ_CP043450\|CRISPRCasFinder	5186540-5186573	34	NZ_CP029429	Klebsiella quasipneumoniae strain CAV2018 plasmid pKPC_CAV2018-63, complete sequence	607-640	12	0.647
NZ_CP043450_7	7.1\|5186540\|34\|NZ_CP043450\|CRISPRCasFinder	5186540-5186573	34	NZ_CP029446	Serratia marcescens strain CAV1761 plasmid pKPC_CAV1761, complete sequence	67181-67214	12	0.647
NZ_CP043450_7	7.1\|5186540\|34\|NZ_CP043450\|CRISPRCasFinder	5186540-5186573	34	NZ_CP011639	Serratia marcescens strain CAV1492 plasmid pKPC_CAV1492, complete sequence	58072-58105	12	0.647
NZ_CP043450_7	7.1\|5186540\|34\|NZ_CP043450\|CRISPRCasFinder	5186540-5186573	34	NC_019899	Klebsiella pneumoniae strain BK31567 plasmid pBK31567, complete sequence	36301-36334	12	0.647
NZ_CP043450_7	7.1\|5186540\|34\|NZ_CP043450\|CRISPRCasFinder	5186540-5186573	34	NZ_CP029439	Klebsiella quasipneumoniae strain CAV1947 plasmid pKPC_CAV1947-56, complete sequence	55580-55613	12	0.647

1. spacer 10.1|6143865|30|NZ_CP043450|CRISPRCasFinder matches to AP013618 (Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C26D-MedDCM-OCT-S37-C143, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 6, identity: 0.8

gaggcgaaaaactgcaacggaaaaatcaga	CRISPR spacer
aataagaaaaactgcaatggaaaaagcaga	Protospacer
.* . ************.******* ****

2. spacer 10.1|6143865|30|NZ_CP043450|CRISPRCasFinder matches to AP013610 (Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C26-MedDCM-OCT-S45-C147, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 6, identity: 0.8

gaggcgaaaaactgcaacggaaaaatcaga	CRISPR spacer
aataagaaaaactgcaatggaaaaagcaga	Protospacer
.* . ************.******* ****

3. spacer 10.1|6143865|30|NZ_CP043450|CRISPRCasFinder matches to AP013619 (Uncultured Mediterranean phage uvMED isolate uvMED-CGF-C26D-MedDCM-OCT-S43-C253, *** SEQUENCING IN PROGRESS ***) position: , mismatch: 6, identity: 0.8

gaggcgaaaaactgcaacggaaaaatcaga	CRISPR spacer
aataagaaaaactgcaatggaaaaagcaga	Protospacer
.* . ************.******* ****

4. spacer 9.1|6143703|30|NZ_CP043450|CRISPRCasFinder matches to NZ_CP041978 (Bacillus pacificus strain NCCP 15909 plasmid unnamed1, complete sequence) position: , mismatch: 7, identity: 0.767

ggtctggataatttaaaaggtaacgagaaa	CRISPR spacer
atgtgggataatttaaaaggtgatgagaaa	Protospacer
.  . ****************.*.******

5. spacer 9.1|6143703|30|NZ_CP043450|CRISPRCasFinder matches to CP041980 (Bacillus paranthracis strain NCCP 15910 plasmid unnamed, complete sequence) position: , mismatch: 7, identity: 0.767

ggtctggataatttaaaaggtaacgagaaa	CRISPR spacer
atgtgggataatttaaaaggtgatgagaaa	Protospacer
.  . ****************.*.******

6. spacer 9.1|6143703|30|NZ_CP043450|CRISPRCasFinder matches to NZ_CP040343 (Bacillus cereus strain DLOU-Weihai plasmid unnamed1, complete sequence) position: , mismatch: 7, identity: 0.767

ggtctggataatttaaaaggtaacgagaaa	CRISPR spacer
atgtgggataatttaaaaggtgatgagaaa	Protospacer
.  . ****************.*.******

7. spacer 9.1|6143703|30|NZ_CP043450|CRISPRCasFinder matches to NZ_CP013927 (Alteromonas stellipolaris strain LMG 21861 plasmid pASTE61-200, complete sequence) position: , mismatch: 7, identity: 0.767

ggtctggataatttaaaaggtaacgagaaa	CRISPR spacer
gggggttataatttaaaacgtagcgagaaa	Protospacer
**     *********** ***.*******

8. spacer 9.1|6143703|30|NZ_CP043450|CRISPRCasFinder matches to NZ_CP013139 (Pseudoalteromonas sp. Bsw20308 plasmid pPBSW1, complete sequence) position: , mismatch: 7, identity: 0.767

ggtctggataatttaaaaggtaacgagaaa	CRISPR spacer
ggtatggataatttagaaggtaaaaattca	Protospacer
*** ***********.******* .*   *

9. spacer 9.1|6143703|30|NZ_CP043450|CRISPRCasFinder matches to NZ_CP013709 (Clostridium botulinum strain F634 plasmid pRSJ2_2, complete sequence) position: , mismatch: 8, identity: 0.733

ggtctggataatttaaaaggtaacgagaaa	CRISPR spacer
acattgaataatttaaaaggtaacgaagat	Protospacer
.  .**.*******************..*

10. spacer 9.1|6143703|30|NZ_CP043450|CRISPRCasFinder matches to NZ_CP013682 (Clostridium botulinum strain 1169 plasmid pRSJ8_1, complete sequence) position: , mismatch: 8, identity: 0.733

ggtctggataatttaaaaggtaacgagaaa	CRISPR spacer
acattgaataatttaaaaggtaacgaagat	Protospacer
.  .**.*******************..*

11. spacer 9.1|6143703|30|NZ_CP043450|CRISPRCasFinder matches to NZ_CP013295 (Clostridium botulinum strain CDC_54064 plasmid pNPD1_1, complete sequence) position: , mismatch: 8, identity: 0.733

ggtctggataatttaaaaggtaacgagaaa	CRISPR spacer
acattgaataatttaaaaggtaacgaagat	Protospacer
.  .**.*******************..*

12. spacer 9.1|6143703|30|NZ_CP043450|CRISPRCasFinder matches to NZ_CP013844 (Clostridium botulinum strain A634 plasmid pRSJ19_2, complete sequence) position: , mismatch: 8, identity: 0.733

ggtctggataatttaaaaggtaacgagaaa	CRISPR spacer
acattgaataatttaaaaggtaacgaagat	Protospacer
.  .**.*******************..*

13. spacer 6.1|4515169|34|NZ_CP043450|CRISPRCasFinder matches to NZ_CP045303 (Azotobacter salinestris strain KACC 13899 plasmid unnamed1, complete sequence) position: , mismatch: 9, identity: 0.735

aagctgccatgccaatccgctctgtacagttcgc	CRISPR spacer
gagcacccatgccaatccgctctgtaactgttac	Protospacer
.***  ********************    *..*

14. spacer 7.1|5186540|34|NZ_CP043450|CRISPRCasFinder matches to NZ_CP029429 (Klebsiella quasipneumoniae strain CAV2018 plasmid pKPC_CAV2018-63, complete sequence) position: , mismatch: 12, identity: 0.647

gcagtagcagtgatttagcctccgcacaggcagt	CRISPR spacer
cggaaagcagtgatttagcctgcgcagagagcac	Protospacer
  .. **************** **** **.  ..

15. spacer 7.1|5186540|34|NZ_CP043450|CRISPRCasFinder matches to NZ_CP029446 (Serratia marcescens strain CAV1761 plasmid pKPC_CAV1761, complete sequence) position: , mismatch: 12, identity: 0.647

gcagtagcagtgatttagcctccgcacaggcagt	CRISPR spacer
cggaaagcagtgatttagcctgcgcagagagcac	Protospacer
  .. **************** **** **.  ..

16. spacer 7.1|5186540|34|NZ_CP043450|CRISPRCasFinder matches to NZ_CP011639 (Serratia marcescens strain CAV1492 plasmid pKPC_CAV1492, complete sequence) position: , mismatch: 12, identity: 0.647

gcagtagcagtgatttagcctccgcacaggcagt	CRISPR spacer
cggaaagcagtgatttagcctgcgcagagagcac	Protospacer
  .. **************** **** **.  ..

17. spacer 7.1|5186540|34|NZ_CP043450|CRISPRCasFinder matches to NC_019899 (Klebsiella pneumoniae strain BK31567 plasmid pBK31567, complete sequence) position: , mismatch: 12, identity: 0.647

gcagtagcagtgatttagcctccgcacaggcagt	CRISPR spacer
cggaaagcagtgatttagcctgcgcagagagcac	Protospacer
  .. **************** **** **.  ..

18. spacer 7.1|5186540|34|NZ_CP043450|CRISPRCasFinder matches to NZ_CP029439 (Klebsiella quasipneumoniae strain CAV1947 plasmid pKPC_CAV1947-56, complete sequence) position: , mismatch: 12, identity: 0.647

gcagtagcagtgatttagcctccgcacaggcagt	CRISPR spacer
cggaaagcagtgatttagcctgcgcagagagcac	Protospacer
  .. **************** **** **.  ..

Prophage detection

Region

Region Position

Protein_number

Hit_taxonomy

Key_proteins

Att_site

Prophage annotation

DBSCAN-SWA_1

3719716 : 3812667

Bacillus_phage(40.0%)

tail,protease

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_112573754.1\|3719716_3720175_-\|tail	phage tail protein	NA	NA	NA	NA
WP_112573755.1\|3720177_3720609_-\|tail	phage tail protein	A0A059XP41	uncultured_phage	7.7e-32	54.1
WP_112573756.1\|3720648_3722637_-\|tail	phage tail protein	NA	NA	NA	NA
WP_112573757.1\|3722648_3724103_-\|tail	phage tail sheath family protein	J9PVC2	Bacillus_phage	2.2e-22	26.7
WP_112573758.1\|3724121_3725306_-	hypothetical protein	NA	NA	NA	NA
WP_149301876.1\|3725344_3726034_-	DUF4255 domain-containing protein	NA	NA	NA	NA
WP_112573760.1\|3726349_3726946_+	FMN-dependent NADH-azoreductase	NA	NA	NA	NA
WP_112573998.1\|3726997_3728110_-	metallophosphoesterase	NA	NA	NA	NA
WP_112573761.1\|3728252_3728768_+\|protease	protease	NA	NA	NA	NA
WP_112573999.1\|3728974_3729910_-	sugar phosphate isomerase/epimerase	NA	NA	NA	NA
WP_112573762.1\|3729919_3730777_-	sugar phosphate isomerase/epimerase	NA	NA	NA	NA
WP_112573763.1\|3730804_3734245_-	carbohydrate-binding protein	NA	NA	NA	NA
WP_112573764.1\|3734761_3735106_-	hypothetical protein	NA	NA	NA	NA
WP_112573765.1\|3735136_3737098_-	OmpA family protein	NA	NA	NA	NA
WP_112573766.1\|3737108_3738104_-	type IX secretion system membrane protein PorP/SprF	NA	NA	NA	NA
WP_112573767.1\|3738100_3751027_-	gliding motility-associated C-terminal domain-containing protein	NA	NA	NA	NA
WP_112573768.1\|3751452_3754047_+	NACHT domain-containing protein	NA	NA	NA	NA
WP_112573769.1\|3754043_3754922_-	AraC family transcriptional regulator	NA	NA	NA	NA
WP_112573770.1\|3755142_3756372_+	mandelate racemase	NA	NA	NA	NA
WP_112573771.1\|3756381_3757146_+	SDR family oxidoreductase	NA	NA	NA	NA
WP_112573772.1\|3757158_3758457_+	L-fucose:H+ symporter permease	NA	NA	NA	NA
WP_112573773.1\|3758833_3760822_+	SGNH/GDSL hydrolase family protein	NA	NA	NA	NA
WP_112573774.1\|3761026_3764347_+	TonB-dependent receptor	NA	NA	NA	NA
WP_112573775.1\|3764373_3766284_+	RagB/SusD family nutrient uptake outer membrane protein	NA	NA	NA	NA
WP_112573776.1\|3766331_3767570_+	DUF4959 domain-containing protein	NA	NA	NA	NA
WP_112573777.1\|3767597_3768827_+	hypothetical protein	NA	NA	NA	NA
WP_112573778.1\|3768925_3770233_+	hypothetical protein	NA	NA	NA	NA
WP_112573779.1\|3770266_3772606_+	glycoside hydrolase family 95 protein	NA	NA	NA	NA
WP_112573780.1\|3772767_3774846_+	alpha-galactosidase	NA	NA	NA	NA
WP_112573781.1\|3775473_3776340_-	helix-turn-helix transcriptional regulator	NA	NA	NA	NA
WP_112573782.1\|3776352_3776718_-	hypothetical protein	NA	NA	NA	NA
WP_114937065.1\|3777133_3777496_-	cyanovirin	NA	NA	NA	NA
WP_112573784.1\|3777900_3778527_-	response regulator transcription factor	NA	NA	NA	NA
WP_146750073.1\|3778529_3781490_-	hypothetical protein	NA	NA	NA	NA
WP_112573786.1\|3781612_3782080_-	hypothetical protein	NA	NA	NA	NA
WP_112573787.1\|3782377_3784195_+	PAS domain-containing protein	W8CYF6	Bacillus_phage	2.7e-25	29.5
WP_112573788.1\|3784214_3785042_+	hypothetical protein	NA	NA	NA	NA
WP_112573789.1\|3785175_3786360_+	GAF domain-containing sensor histidine kinase	A0A1B0VMK3	Pseudomonas_phage	1.9e-24	32.1
WP_112573790.1\|3786344_3786737_-	VOC family protein	NA	NA	NA	NA
WP_112573791.1\|3787130_3788804_+	patatin-like phospholipase family protein	NA	NA	NA	NA
WP_112573792.1\|3788891_3789773_+	DMT family transporter	NA	NA	NA	NA
WP_112574000.1\|3789895_3791140_-	beta-ketoacyl-ACP synthase II	NA	NA	NA	NA
WP_112573793.1\|3791305_3792148_-	isocitrate lyase/phosphoenolpyruvate mutase family protein	NA	NA	NA	NA
WP_112573794.1\|3792301_3792928_+	chloramphenicol acetyltransferase	NA	NA	NA	NA
WP_112573795.1\|3793056_3794352_-	DUF885 domain-containing protein	NA	NA	NA	NA
WP_112573796.1\|3794468_3795440_+	hypothetical protein	NA	NA	NA	NA
WP_112573797.1\|3795446_3795881_-	CBS domain-containing protein	NA	NA	NA	NA
WP_112573798.1\|3796073_3797561_-	arabinan endo-1,5-alpha-L-arabinosidase	NA	NA	NA	NA
WP_112573799.1\|3797779_3799336_-	RagB/SusD family nutrient uptake outer membrane protein	NA	NA	NA	NA
WP_146750074.1\|3799366_3801832_-	SusC/RagA family TonB-linked outer membrane protein	NA	NA	NA	NA
WP_112573801.1\|3801952_3802711_-	hypothetical protein	NA	NA	NA	NA
WP_112573802.1\|3802871_3803945_-	FecR family protein	NA	NA	NA	NA
WP_112573803.1\|3804000_3804624_-	RNA polymerase sigma-70 factor	NA	NA	NA	NA
WP_112573804.1\|3805092_3806559_-	glycoside hydrolase family 30 protein	NA	NA	NA	NA
WP_112573805.1\|3806586_3807582_-	L-glyceraldehyde 3-phosphate reductase	NA	NA	NA	NA
WP_112573806.1\|3807712_3808291_+	Crp/Fnr family transcriptional regulator	NA	NA	NA	NA
WP_112573807.1\|3808456_3809326_-	hypothetical protein	NA	NA	NA	NA
WP_112573808.1\|3809382_3810915_-	serine hydrolase	A0A1V0SLG8	Klosneuvirus	2.1e-07	27.7
WP_112573809.1\|3811068_3812667_-\|protease	M48 family metalloprotease	NA	NA	NA	NA

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_CP043450

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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