ID A0A430A138_9ENTE Unreviewed; 426 AA.
AC A0A430A138;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, 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=CBF37_02165 {ECO:0000313|EMBL:RSU00125.1};
OS Vagococcus vulneris.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=1977869 {ECO:0000313|EMBL:RSU00125.1, ECO:0000313|Proteomes:UP000287857};
RN [1] {ECO:0000313|EMBL:RSU00125.1, ECO:0000313|Proteomes:UP000287857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS1995 {ECO:0000313|EMBL:RSU00125.1,
RC ECO:0000313|Proteomes:UP000287857};
RA Gulvik C.A.;
RT "Vagococcus spp. assemblies.";
RL Submitted (MAY-2017) 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:RSU00125.1}.
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DR EMBL; NGJS01000002; RSU00125.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430A138; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000287857; 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; PF00595; PDZ; 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:RSU00125.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000287857};
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 179..197
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 348..369
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 398..417
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 207..242
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 426 AA; 46609 MW; 495C00023C3A00DF CRC64;
MKTLITFIFV FGLIVLIHEF GHFIFAKRGG ILVREFSIGM GPKLFSHRHN GTAYTIRLLP
VGGYVRMAGE GDEDVELAPG MPVSLVLNNN GEVIKINQSK KVQLENSIPV EILETDLEDQ
LFIRAYENGD ETQEKRYPVN HDATIVEEDG VEVQIAPRDV QFQSASLGRR LMTNIAGPMN
NFILAFVLFV IVAFMQGGTY EPSTSTVIGG VAEGLPAAKA NIKPGDEILS INGQKQKDFE
SMAKIISENP GNKLRIELKT NNGQEKNVEV IPVKSETDPK VGVIGINISN DFVPLSFFGK
IKDGFIKTFT NSLVIFKALG DLITGFSLNK LGGPVMIFKL SESVSNSGII AVLSFTAMLS
VNLGIMNLIP LPGLDGGKII LNLLEGIRGK PLSQEKEMMI TMIGVVVLVV LMVAVTWNDI
NRFFIR
//
