ID   B0FSQ2_VIBSP            Unreviewed;       918 AA.
AC   B0FSQ2;
DT   26-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2008, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Putative M6 secreted metalloprotease {ECO:0000313|EMBL:ABY61046.1};
OS   Vibrio splendidus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=29497 {ECO:0000313|EMBL:ABY61046.1};
RN   [1] {ECO:0000313|EMBL:ABY61046.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LGP32 {ECO:0000313|EMBL:ABY61046.1};
RX   PubMed=18836018; DOI=10.1128/AEM.01261-08;
RA   Binesse J., Delsert C., Saulnier D., Champomier-Verges M.C., Zagorec M.,
RA   Munier-Lehmann H., Mazel D., Le Roux F.;
RT   "Metalloprotease vsm is the major determinant of toxicity for extracellular
RT   products of Vibrio splendidus.";
RL   Appl. Environ. Microbiol. 74:7108-7117(2008).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR   EMBL; EU349011; ABY61046.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0FSQ2; -.
DR   SMR; B0FSQ2; -.
DR   MEROPS; M06.002; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00146; PKD; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR048665; InhA-like_VEG.
DR   InterPro; IPR012300; Pept_M6_InhA.
DR   InterPro; IPR008757; Peptidase_M6-like_domain.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   NCBIfam; TIGR03296; M6dom_TIGR03296; 1.
DR   PANTHER; PTHR13062; COLLAGENASE; 1.
DR   PANTHER; PTHR13062:SF12; PRE-PRO-METALLOPROTEASE PRTV; 1.
DR   Pfam; PF20773; InhA-like_MAM; 1.
DR   Pfam; PF20774; InhA-like_VEG; 1.
DR   Pfam; PF05547; Peptidase_M6; 1.
DR   Pfam; PF00801; PKD; 1.
DR   Pfam; PF18911; PKD_4; 1.
DR   PIRSF; PIRSF007519; Protease_InhA; 1.
DR   SMART; SM00089; PKD; 2.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF49299; PKD domain; 2.
DR   PROSITE; PS50093; PKD; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000313|EMBL:ABY61046.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:ABY61046.1};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..918
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002748354"
FT   DOMAIN          777..840
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
SQ   SEQUENCE   918 AA;  101360 MW;  A1D89FF33294BDF3 CRC64;
     MKMMRKTLLA SAMLTLFSVS SYAKTPIDLG VVNEDKLIEM LVRQGLVDQD ATDVAKHDAL
     DHYLKNKINS GFKGDAQFGK KALEQRAKIL KAIEKGSGVK KASVFALEVG TKRTDKVLAL
     LVDFPDLNWD NNKLTEEHTQ MLYESYNPEH YQELLFSNSG YTGPNGENLI SMRQYYQSES
     GDSYSVAGQA AGWYRASKPA SFYGGNSPTT DNDLNAQELV REALNQLAQD PSINLADYDI
     EDRYDYDGDG NFREPDGVID HLMVFHASVG EEAGGGVLGP DAIWSHRFNL GRTHVLKGTS
     SSLPDRFGGQ YAAFDYTIQP IDAAAGVCAH EYGHDLGLPD EYDTQYTGKG EPVSYWSIMS
     SGSWAGQIGG TQPTAFSSWA KHFLQKSIGG RWVNDDQISI DDLEDNPQVY TLFQTTDNNR
     PNMIKVDLPE KQIEGLKPFA GEYSFHSQKG DDLKNSMTRK LVIPAGDSAL LSFKTWYEIE
     KDYDFARVLV NGQAIAGNIT SLDDPYNTGL VPAIGGESGG WIDAEFDVSQ WAGQEVELSF
     EYITDGGLAM EGFYLDNLSV VVDGEITLID DGESNSTFAL NGYKLSNGFH QAQHYYLLQW
     RSHMDVDEGL ANIKRMGQLI SFDPGLIIWY VDESLTDNWV GKHPGEGWLG VVDADQNAMT
     WEKSGEVAQT RYQVRDAAFS LKDHTPMRLV NSDNDVLEDT SLVGNASFSD DQDYTSPQAP
     DSGRILTEFG LAVDIVNQSD NNEYGVVRLS KVSQHNVAPT ANFELNVTGL NVSARNFSSD
     QDGEITSYLW DLGNGTTSNE VTPTWSYEQA GEYTVNLTVV DDKGNTDSFS SVVSVESPNA
     LPEASAKYIH LGRWVTMWST SSDSNGRIVD TEWTLPNGKV KRGRTFTSIF PSYGKHKVTL
     KIIDDQGGIT TKTILVDL
//