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Database: UniProt
Entry: A0A0K6GW76_9GAMM
LinkDB: A0A0K6GW76_9GAMM
Original site: A0A0K6GW76_9GAMM 
ID   A0A0K6GW76_9GAMM        Unreviewed;       451 AA.
AC   A0A0K6GW76;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN   ORFNames=Ga0061064_0350 {ECO:0000313|EMBL:CUA82981.1};
OS   Pseudidiomarina woesei.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Pseudidiomarina.
OX   NCBI_TaxID=1381080 {ECO:0000313|EMBL:CUA82981.1, ECO:0000313|Proteomes:UP000182598};
RN   [1] {ECO:0000313|Proteomes:UP000182598}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27808 {ECO:0000313|Proteomes:UP000182598};
RA   Varghese N.;
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU362031};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family.
CC       {ECO:0000256|ARBA:ARBA00007931, ECO:0000256|RuleBase:RU362031}.
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DR   EMBL; CYHB01000001; CUA82981.1; -; Genomic_DNA.
DR   RefSeq; WP_055438058.1; NZ_LIPW01000001.1.
DR   AlphaFoldDB; A0A0K6GW76; -.
DR   OrthoDB; 9782003at2; -.
DR   Proteomes; UP000182598; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00989; PDZ_metalloprotease; 2.
DR   CDD; cd06163; S2P-M50_PDZ_RseP-like; 2.
DR   Gene3D; 2.30.42.10; -; 2.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   NCBIfam; TIGR00054; RIP metalloprotease RseP; 1.
DR   PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; PDZ domain-like; 2.
DR   PROSITE; PS50106; PDZ; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362031};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362031};
KW   Metal-binding {ECO:0000256|RuleBase:RU362031};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU362031};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CUA82981.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362031};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362031};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU362031}.
FT   TRANSMEM        6..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        98..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        427..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   DOMAIN          177..290
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   451 AA;  48895 MW;  3F239823AD4E8EB8 CRC64;
     MGSIIWSLGA FVVTLGILVT FHEFGHFWVA RRCGVKVLTF SVGFGKPIWQ RQGQDGTVYQ
     VGIVPLGGYV RMLDERVDNV SENERQVTFN SKTVWQRAAI IAAGPIANFV LAIAVLWLMF
     VIGVPSVKPI IGTVQENSIA AQAGIQSPAE IIAIDGVETA DWQQVNLRFA AALGNDLVEV
     KTRDEGNRER TYQLQISAWR LEDNKQPTYT ALGLQPFRPE VSLVLSYIAP DSPAAAANLQ
     VGDKIIAFDG TPLVDWPQTR DLILQAAGQD VTITLERSGQ TMTQQVQLGS REANGQRYGF
     LGVEPTVAAY PEQYRFTQQY GIVDGLIHGA ERTWELMTLS VNMLGKLLVG TVSVSNLSGP
     VAIAEGAGAT ASYGLVYFLG FLALISVNLG IINLVPLPVL DGGHLAFLAI EGVRGKPVSE
     RVQEVCYRIG GILIFALMAI AISNDILRLS Q
//
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