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
//