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Database: UniProt
Entry: U4KB12_9VIBR
LinkDB: U4KB12_9VIBR
Original site: U4KB12_9VIBR 
ID   U4KB12_9VIBR            Unreviewed;       415 AA.
AC   U4KB12;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=P/Homo B domain-containing protein {ECO:0000259|PROSITE:PS51829};
GN   ORFNames=VIBNI_B0105 {ECO:0000313|EMBL:CCO59937.1};
OS   Vibrio nigripulchritudo.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO59937.1, ECO:0000313|Proteomes:UP000016895};
RN   [1] {ECO:0000313|EMBL:CCO59937.1, ECO:0000313|Proteomes:UP000016895}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX   PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA   Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA   Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT   "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT   identifies virulence-associated traits.";
RL   ISME J. 7:1985-1996(2013).
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DR   EMBL; FO203527; CCO59937.1; -; Genomic_DNA.
DR   RefSeq; WP_022560612.1; NZ_AP027053.1.
DR   AlphaFoldDB; U4KB12; -.
DR   STRING; 28173.VIBNI_B0105; -.
DR   KEGG; vni:VIBNI_B0105; -.
DR   PATRIC; fig|1260221.3.peg.3794; -.
DR   eggNOG; COG4935; Bacteria.
DR   OrthoDB; 7067851at2; -.
DR   Proteomes; UP000016895; Chromosome 2.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR002884; P_dom.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF13582; Reprolysin_3; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016895};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..415
FT                   /note="P/Homo B domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004650904"
FT   DOMAIN          293..415
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
SQ   SEQUENCE   415 AA;  46159 MW;  E007B89B1C07FC8E CRC64;
     MNKTLLAAVI TSSLVAPSVY ATTNIDILGV YTKATSDWFA TEQNKTEHIT QIQHRFNVGN
     QILKKSGLDV KVNLVGTKEY NYDSAPGRRL NQEAALDAIT PSYKQDAIFS DIEQVRKEKG
     ADMVALFRNL DVKNSPDYVR EGNTISLSCG LAWVVPAFRW DASNTSWVKS QMYSHSYLNE
     CGDDTFIHEL GHNFGINHAR EQYTVPPHTQ NGTEKDAYGY GVNGKFATTM AYGFLFNVYN
     RSYTFSNPET QCGDQACGVK DKSNATRAIG LTAPKIANIY QSKDGGTDTT DPVEPKEPQE
     TKNVFSLESP VAVPDHTQIE IPLEVSYTGE VTEPTIALDI EHEFIGDISV RLIAPDNAYW
     VLKKANRSDR GKKFNVTFTL QDMQGVDVTG QWKLQVTDHF RNDVGVVKNA TLTLK
//
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