ID A0A1I0E6P7_9BACI Unreviewed; 419 AA.
AC A0A1I0E6P7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=SAMN05421676_104317 {ECO:0000313|EMBL:SET40673.1};
OS Salinibacillus kushneri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salinibacillus.
OX NCBI_TaxID=237682 {ECO:0000313|EMBL:SET40673.1, ECO:0000313|Proteomes:UP000199095};
RN [1] {ECO:0000313|EMBL:SET40673.1, ECO:0000313|Proteomes:UP000199095}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3566 {ECO:0000313|EMBL:SET40673.1,
RC ECO:0000313|Proteomes:UP000199095};
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; FOHJ01000004; SET40673.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0E6P7; -.
DR STRING; 237682.SAMN05421676_104317; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000199095; 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.
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:SET40673.1};
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 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 172..193
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 391..410
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 195..268
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 419 AA; 46772 MW; 853131343419E24B CRC64;
MNTVIAFIFM FGLLVFIHEF GHMIFAKRAG MLVREFAIGF GPKIFSYRKK ETLYTIRLLP
IGGYVRVAGE DPEIIELKPG HHIGLEFNES DKVEKIIVNN KSKHPNARVI EVEGADLDHE
LVITGYDVDS EERLTFDVDP KAFFIMDENE TQIAPYDRQF ASKSVPKKAM QIFAGPMMNF
VLAIIVFIIL GFAQGVPVEE AQLGEISENY PAAESGLQQG DRILQVDNQS IDTWVDFVME
IQEHPNEEVE LMVDRNGEVM SVPITPDAIE EQGKEIGQIG VRQAFEHSPG EIVKFGFTET
YELSTLILTS VGQLVTGQLS IDSLAGPVGI YDVTDQAVQT GFYTFLTWTA MLSVNLGIIN
LLPLPALDGG RLIFIGYEAV RGKPIDPQKE GIVHFLGFAL LMLLMIVVTW NDIQRLFTP
//
