ID   A0A1M4WRY4_9FLAO        Unreviewed;       438 AA.
AC   A0A1M4WRY4;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN   ORFNames=SAMN05444278_106126 {ECO:0000313|EMBL:SHE83742.1};
OS   Psychroflexus salarius.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Psychroflexus.
OX   NCBI_TaxID=1155689 {ECO:0000313|EMBL:SHE83742.1, ECO:0000313|Proteomes:UP000184462};
RN   [1] {ECO:0000313|EMBL:SHE83742.1, ECO:0000313|Proteomes:UP000184462}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25661 {ECO:0000313|EMBL:SHE83742.1,
RC   ECO:0000313|Proteomes:UP000184462};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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; FQTW01000006; SHE83742.1; -; Genomic_DNA.
DR   RefSeq; WP_073193235.1; NZ_FQTW01000006.1.
DR   AlphaFoldDB; A0A1M4WRY4; -.
DR   STRING; 1155689.SAMN05444278_106126; -.
DR   OrthoDB; 9782003at2; -.
DR   Proteomes; UP000184462; 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; 1.
DR   CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR   Gene3D; 2.30.42.10; -; 1.
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; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 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:SHE83742.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184462};
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        104..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        369..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        408..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   DOMAIN          202..279
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
SQ   SEQUENCE   438 AA;  49367 MW;  3747E5B36C18E51B CRC64;
     MDPFYIKAIQ LLLSLSLLIV LHELGHFIPA KLFKTRVEKF YLFFDLKFSL FKKKIGETVY
     GIGWLPLGGY VKISGMIDES MDKEQMAKPP QPWEFRSKPA WQRLIIMLGG VTVNIILGFV
     IYMMILLVFG RDYVKPESLS NGFTVAEPLK AYGFEDGDNF LSVDGEALEN PMNINEVFML
     RDFEKVEVQH ADGSIEVLQV PEDVGVELFK AGYQIPFTPV FEAKLDSIVP ESPAGLAGLQ
     PGDQVIGVDN QPIQFWHELT SVVKNSVGQE LLIKYQRDNA IDSVEVSVPK EAVIGIYVDA
     NLERGHRDYS FTESLVGGFS FGMRQLTNYA AQFKYIFTEK GASQVGGFGA IGGLFPDTWD
     WVSFWETTAF ISIILAFMNI LPIPALDGGH VMFLLYEMVS GRKPNEKVME YAQMIGFFII
     IALVLYANGN DVYRYFFE
//