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Database: UniProt
Entry: D4ZF67_SHEVD
LinkDB: D4ZF67_SHEVD
Original site: D4ZF67_SHEVD 
ID   D4ZF67_SHEVD            Unreviewed;       721 AA.
AC   D4ZF67;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Immune inhibitor A-like metalloprotease {ECO:0000313|EMBL:BAJ04231.1};
GN   OrderedLocusNames=SVI_4260 {ECO:0000313|EMBL:BAJ04231.1};
OS   Shewanella violacea (strain JCM 10179 / CIP 106290 / LMG 19151 / DSS12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=637905 {ECO:0000313|EMBL:BAJ04231.1, ECO:0000313|Proteomes:UP000002350};
RN   [1] {ECO:0000313|Proteomes:UP000002350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10179 / CIP 106290 / LMG 19151 / DSS12
RC   {ECO:0000313|Proteomes:UP000002350};
RX   PubMed=20458400; DOI=10.1039/c000396d;
RA   Aono E., Baba T., Ara T., Nishi T., Nakamichi T., Inamoto E., Toyonaga H.,
RA   Hasegawa M., Takai Y., Okumura Y., Baba M., Tomita M., Kato C., Oshima T.,
RA   Nakasone K., Mori H.;
RT   "Complete genome sequence and comparative analysis of Shewanella violacea,
RT   a psychrophilic and piezophilic bacterium from deep sea floor sediments.";
RL   Mol. Biosyst. 6:1216-1226(2010).
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; AP011177; BAJ04231.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4ZF67; -.
DR   STRING; 637905.SVI_4260; -.
DR   KEGG; svo:SVI_4260; -.
DR   eggNOG; COG3291; Bacteria.
DR   eggNOG; COG4412; Bacteria.
DR   HOGENOM; CLU_010858_1_0_6; -.
DR   Proteomes; UP000002350; Chromosome.
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; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR020008; GlyGly_CTERM.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR048665; InhA-like_VEG.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
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; TIGR03501; GlyGly_CTERM; 1.
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; PF18911; PKD_4; 1.
DR   PIRSF; PIRSF007519; Protease_InhA; 1.
DR   SMART; SM00089; PKD; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   SUPFAM; SSF49299; PKD domain; 1.
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:BAJ04231.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:BAJ04231.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002350};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          598..684
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
SQ   SEQUENCE   721 AA;  77089 MW;  B1B44F1A2B2750C4 CRC64;
     MFYPSYPVSH YKNLMFSTTG FTGPQGQNLI TGYQYYKAES GERFNFTGDV KGWFTAANNA
     AFYGGNDPDN NNDDKAVDVL VKEAVTLAVA SMSASELASY DVEDPFDVDG DFNFNEPDGD
     IDHVMLFHSS IGEEAGGGAV LGADAIWSHR FFVYTGNTPG YAIPGTGKKV YGYTIQPIDA
     AAGVVVHEFG HDLGLPDEYD TTNTGDGSPV GSWSVMSGGS WTGSISGTEP TGFSPYARSY
     LQDRYKGRWI NEQQVLLASL GTSGVDVVIN EAVNHSSVNQ ISIPLPVATI PFKLAYGGVY
     QYYSGQGHLI NNALSFEIDL PSSTPLTLKM KAHWDIEQDY DYAQIMVDGV TIVGNHTKAS
     NMRNTARDII TGNSGDIAGA EGANNWVDLE YDISAYAGRA NAQISIIYRT DPAVGGYGFV
     FDNLEIASGA SLVYSDDAET ANAMMLNGFS RIDDERPGAA RRYIIQLRSH NGVDVGLDSH
     TYEPGVLIWL ENLSYSDNDS ANHPGVGLIG VVDADQNLIS NQVSDVQIRD ATFSMFNQST
     YIGDAHLTSV SLFDDTQDYS APTKPMAGII LPVLGLTIEV VAQSSDSSSA TVRMKLDTPV
     QPTASFASAI DDLRVIFTNT TSNGVGELTY RWDFGDSGTS TARSPTHTYL TGGTYTVSLT
     VTDFADNEST AMETVVVTEA AVTPPVIIPP VTPPSSGSGG GSLGWLSLGL LALLGFRRAS
     S
//
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