ID A0A094JGM8_9GAMM Unreviewed; 451 AA.
AC A0A094JGM8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=IDSA_03200 {ECO:0000313|EMBL:KFZ31711.1};
OS Pseudidiomarina salinarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=435908 {ECO:0000313|EMBL:KFZ31711.1, ECO:0000313|Proteomes:UP000054363};
RN [1] {ECO:0000313|EMBL:KFZ31711.1, ECO:0000313|Proteomes:UP000054363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISL-52 {ECO:0000313|EMBL:KFZ31711.1,
RC ECO:0000313|Proteomes:UP000054363};
RA Du J., Shao Z.;
RT "The draft genome sequence of Idiomarina salinarum ISL-52.";
RL Submitted (JUN-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFZ31711.1}.
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DR EMBL; JPER01000001; KFZ31711.1; -; Genomic_DNA.
DR RefSeq; WP_034774115.1; NZ_PIQD01000001.1.
DR AlphaFoldDB; A0A094JGM8; -.
DR STRING; 435908.IDSA_03200; -.
DR eggNOG; COG0750; Bacteria.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000054363; 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.
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}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000054363};
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 375..395
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 425..443
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 116..186
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT DOMAIN 206..279
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 451 AA; 48692 MW; 03E28D5E6602DDAA CRC64;
MLEILWAIGA FAVTLGILVT FHEFGHFWVA RRCGVKVLVF SVGFGKAIWQ RTAADGTVYQ
VGIIPLGGYV RMLDERVDEV PESERHLSFN SQSVRRRAAI IAAGPAANFV IAVVLLWVMF
VIGVPSVKPV IGSIQPDSVA AQADIQTPAE ILSVNGNETE DWQQVNLAFA AALGNEEATI
RVLDARDREQ SYVLDIDGWR IGDQQQPTFV ELGMLPWRPE ATTTINYIAE NSPAAAADFA
PGDKIIAVDG TPVEEWSQIR EQIMAAPGER LSFTVERGQT QIELTAAIGE RSTAQGTIGF
LGVEPQQTAY PDEYRFVQQY GIVGGLIKGA ERTWDLMVLS VQMIGKLVTG TVSLSNLSGP
VAIAEGAGAS ASYGLVYFLG FLALISVNLG IINLVPLPIL DGGHLVFLAI EGARKKAVSE
RVQELSYRIG GLLIFALMAI AISNDVLRLA Q
//