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Database: UniProt
Entry: B7VS43_VIBA3
LinkDB: B7VS43_VIBA3
Original site: B7VS43_VIBA3 
ID   B7VS43_VIBA3            Unreviewed;       918 AA.
AC   B7VS43;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 70.
DE   SubName: Full=M6 secreted metalloprotease {ECO:0000313|EMBL:CAV26928.1};
GN   OrderedLocusNames=VS_II1062 {ECO:0000313|EMBL:CAV26928.1};
OS   Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=575788 {ECO:0000313|EMBL:CAV26928.1, ECO:0000313|Proteomes:UP000009100};
RN   [1] {ECO:0000313|EMBL:CAV26928.1, ECO:0000313|Proteomes:UP000009100}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LGP32 {ECO:0000313|EMBL:CAV26928.1,
RC   ECO:0000313|Proteomes:UP000009100};
RA   Mazel D., Le Roux F.;
RT   "Vibrio splendidus str. LGP32 complete genome.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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; FM954973; CAV26928.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7VS43; -.
DR   SMR; B7VS43; -.
DR   STRING; 575788.VS_II1062; -.
DR   MEROPS; M06.002; -.
DR   KEGG; vsp:VS_II1062; -.
DR   PATRIC; fig|575788.5.peg.1003; -.
DR   eggNOG; COG3291; Bacteria.
DR   eggNOG; COG4412; Bacteria.
DR   HOGENOM; CLU_010858_1_0_6; -.
DR   Proteomes; UP000009100; Chromosome 2.
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:InterPro.
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:CAV26928.1}; Protease {ECO:0000256|ARBA:ARBA00022670};
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_5002864967"
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
//
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