ID A0A4U8SE73_9HELI Unreviewed; 356 AA.
AC A0A4U8SE73;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN Name=rseP {ECO:0000313|EMBL:TLD84459.1};
GN ORFNames=LS70_002620 {ECO:0000313|EMBL:TLD84459.1};
OS Helicobacter sp. MIT 11-5569.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1548151 {ECO:0000313|EMBL:TLD84459.1, ECO:0000313|Proteomes:UP000029923};
RN [1] {ECO:0000313|EMBL:TLD84459.1, ECO:0000313|Proteomes:UP000029923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 11-5569 {ECO:0000313|EMBL:TLD84459.1,
RC ECO:0000313|Proteomes:UP000029923};
RX PubMed=25428971;
RA Sheh A., Shen Z., Fox J.G.;
RT "Draft genome sequences of eight enterohepatic helicobacter species
RT isolated from both laboratory and wild rodents.";
RL Genome Announc. 2:e01218-e01214(2014).
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:TLD84459.1}.
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DR EMBL; JRPB02000002; TLD84459.1; -; Genomic_DNA.
DR RefSeq; WP_034290475.1; NZ_JRPB02000002.1.
DR AlphaFoldDB; A0A4U8SE73; -.
DR STRING; 1548151.LS70_07930; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000029923; 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; 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:TLD84459.1};
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 94..119
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 273..295
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 322..343
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 126..180
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 356 AA; 39076 MW; BDEF207E6C7B311A CRC64;
MGLIGSILVL SFLIFFHELG HFLAAKLFGV RVEAFSIGFG KTRIFKKQIG ETEYSLRPIP
LGGFVQLKGQ SDIDPKLRNE DKDSLYGIAH WKRLVILAAG SFFNLLLAFL LFMAIGLMGK
NELVPIVGKV QENMPAALAG LKSGDRILEI DGEKIVTWNA LSSVIAESKG TLEIVFLRNN
QEFITRITPK LGESKNLFGE SIERPLVGIS ASGDVEIVSY SFLDSMLYAF RETKESSKLI
LQSIEKIFVG VVPLSEVGGV VSIVSITKKA TELGIVTLFA FSALISVNLG ILNLLPIPAL
DGGHIIFTLY EMVSKRIPTQ ETLYRLSMAG WIVLLGLMGL GFYNDILRII NGTMPF
//
