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Database: UniProt
Entry: G7LQL2_9GAMM
LinkDB: G7LQL2_9GAMM
Original site: G7LQL2_9GAMM 
ID   G7LQL2_9GAMM            Unreviewed;       454 AA.
AC   G7LQL2;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN   ORFNames=BrE312_3486 {ECO:0000313|EMBL:EHD22843.1};
OS   Brenneria sp. EniD312.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Brenneria.
OX   NCBI_TaxID=598467 {ECO:0000313|EMBL:EHD22843.1};
RN   [1] {ECO:0000313|EMBL:EHD22843.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EniD312 {ECO:0000313|EMBL:EHD22843.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Monk A.C., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Balakrishnan V.,
RA   Glasner J., Perna N., Woyke T.;
RT   "Complete sequence of Brenneria sp. EniD312.";
RL   Submitted (JUL-2011) 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; CM001230; EHD22843.1; -; Genomic_DNA.
DR   RefSeq; WP_009114141.1; NZ_CM001230.1.
DR   AlphaFoldDB; G7LQL2; -.
DR   STRING; 598467.BrE312_3486; -.
DR   MEROPS; M50.004; -.
DR   eggNOG; COG0750; Bacteria.
DR   HOGENOM; CLU_025778_0_2_6; -.
DR   Proteomes; UP000002759; Chromosome.
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; 1.
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:EHD22843.1};
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        98..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        380..400
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        430..448
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   DOMAIN          202..259
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   454 AA;  49351 MW;  6407B7618FF9AFFF CRC64;
     MMNFLWSLAA FIIALGVLIT VHEFGHFWVA RRCGVKVERF SVGFGRALWR RRDKLGTEYV
     IALIPLGGYV KMLDERVDTV APEFRHQSFN SKTVWQRAAI VSAGPVANFL LAIVVYWLVF
     IIGVPGVRPV VGEILPDSIA AQAEISAGIE LKSVDGIETP DWDTARLALI GKIGDDEVVL
     GTAPFGAGQS ARIAHKTLDL RNWQFEPDKQ DPVTSLGMVP RGPQVEAVLT QVQPGSAAEK
     AGLQAGDRIV KVGGEVLTHW NVFVTAVRDN PGRDIALEVE RGGITLPLTL TPVGKSVGNG
     RVEGLAGVMP SVAPLPEEYR TVRQYGPFSA IYQATDKTWQ LMKLTVSMLV KLVTGDVKLN
     NLSGPISIAQ GAGMSADYGL IYYLMFLALI SVNLGIINLF PLPVLDGGHL LFLAVEKLQG
     RPVSERVQDV SYRIGTVLLM LLMGLALFND FSRL
//
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