ID A0A1G9LGQ2_9FIRM Unreviewed; 358 AA.
AC A0A1G9LGQ2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=SAMN04488692_10655 {ECO:0000313|EMBL:SDL61066.1};
OS Halarsenatibacter silvermanii.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halarsenatibacteraceae;
OC Halarsenatibacter.
OX NCBI_TaxID=321763 {ECO:0000313|EMBL:SDL61066.1, ECO:0000313|Proteomes:UP000199476};
RN [1] {ECO:0000313|EMBL:SDL61066.1, ECO:0000313|Proteomes:UP000199476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLAS-1 {ECO:0000313|EMBL:SDL61066.1,
RC ECO:0000313|Proteomes:UP000199476};
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; FNGO01000006; SDL61066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9LGQ2; -.
DR STRING; 321763.SAMN04488692_10655; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000199476; 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; 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; PF13180; PDZ_2; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
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:SDL61066.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199476};
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..26
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 106..131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 331..350
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 129..187
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 358 AA; 39702 MW; C51FF03187E62E69 CRC64;
MLTTVIAFII FLGILIFVHE LGHFLMARRM DIRVEEFALG FGPKLLSRKK GETRYSIRII
PLGGFCSMTG EMPVDKEDLD QEEREIYEEA RENERCFFQK SPLKRLAVLV AGPLMNVALA
ILAFVLIFGI YGVPVEHAHD AVVGEMFPGE PAARSGIRGG DEILAIEGEE VSSWQEMTNM
IRENPGEELN ITLQRDEEIK EIQVTPELDE ETGYGMIGVL PRVVRERVGP ITAVHRGVAQ
TGQVVVLTVR GFIHIISQAS TDELGGPVMI ASIVGQAART GPENVLNWLG IISINLAIIN
LIPFPALDGG RVIFVLAELI SGKKIPQEKE GWVHMVGFVL LILLMIFIIY QDIITTFF
//
