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Database: UniProt
Entry: A0A1G5Q9Y3_9RHOB
LinkDB: A0A1G5Q9Y3_9RHOB
Original site: A0A1G5Q9Y3_9RHOB 
ID   A0A1G5Q9Y3_9RHOB        Unreviewed;       451 AA.
AC   A0A1G5Q9Y3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN   ORFNames=SAMN04488118_103278 {ECO:0000313|EMBL:SCZ58386.1};
OS   Epibacterium ulvae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Epibacterium.
OX   NCBI_TaxID=1156985 {ECO:0000313|EMBL:SCZ58386.1, ECO:0000313|Proteomes:UP000198767};
RN   [1] {ECO:0000313|EMBL:SCZ58386.1, ECO:0000313|Proteomes:UP000198767}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U95 {ECO:0000313|EMBL:SCZ58386.1,
RC   ECO:0000313|Proteomes:UP000198767};
RA   de Groot N.N.;
RL   Submitted (OCT-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; FMWG01000003; SCZ58386.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5Q9Y3; -.
DR   STRING; 1156985.SAMN04488118_103278; -.
DR   OrthoDB; 9782003at2; -.
DR   Proteomes; UP000198767; 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; 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};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SCZ58386.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198767};
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..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        113..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        384..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   DOMAIN          202..281
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
SQ   SEQUENCE   451 AA;  47381 MW;  A856ADEA330E21C6 CRC64;
     MDLASFLPQI SGFAFTIVSF IAVISIVVAV HEYGHYIVGR WSGIHAEVFS LGFGPVLCSR
     VDRHGTRWQI ALLPFGGFVK FLGDANAASG KDADAMAEID PAQLRRTMHG APLWARAATV
     AAGPVFNFVL SAVIFTVLIL SSGAARDPLT VGQVIDLPAA STGEVYGLQA GDEILAVEGI
     KVPSLANGEA WTRFTDAIPM QEVLGYRVLR DGVEQEVAGP VLSPTLVRFV APRSAASDIN
     LQPGDVITAI DGAPVYEFSQ LREAVEGGNG APLVLDIWRN GAEFEETLTP RRTDEPQPGG
     GFEVKWRIGI GGGMAFDPAT ETVGVGTAIG SGVAQVGNVI QMSLSGLGHM ILGNISTCNL
     SGPIGIAETS GAVASQGIDS FFRLVALISA GIGMLNLFPI PALDGGHLVF YAYEAVVGRP
     PRDRVMQVLM TVGIALVLSM MVFSLSNDLF C
//
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