ID   A0A3S0R806_9BACI        Unreviewed;       419 AA.
AC   A0A3S0R806;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN   Name=rseP {ECO:0000313|EMBL:RUL55771.1};
GN   ORFNames=EK386_02865 {ECO:0000313|EMBL:RUL55771.1};
OS   Lysinibacillus antri.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=2498145 {ECO:0000313|EMBL:RUL55771.1, ECO:0000313|Proteomes:UP000287910};
RN   [1] {ECO:0000313|EMBL:RUL55771.1, ECO:0000313|Proteomes:UP000287910}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SYSU K30002 {ECO:0000313|EMBL:RUL55771.1,
RC   ECO:0000313|Proteomes:UP000287910};
RA   Narsing Rao M.P., Zhang H., Dong Z.-Y., Niu X.-K., Zhang K., Fang B.-Z.,
RA   Kang Y.-Q., Xiao M., Li W.-J.;
RT   "Lysinibacillus antri sp. nov., isolated from a cave soil.";
RL   Submitted (DEC-2018) 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:RUL55771.1}.
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DR   EMBL; RYYR01000003; RUL55771.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S0R806; -.
DR   Proteomes; UP000287910; 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.
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:RUL55771.1};
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        168..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        392..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   DOMAIN          186..256
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
SQ   SEQUENCE   419 AA;  46454 MW;  68ADC46ED8A040CE CRC64;
     MQTVIAFIIV FGSLVFFHEL GHFIFAKRAG IMVREFAIGM GPKIFGMTKG ETLYTIRLLP
     LGGYVRMAGE DIDKIELQPG YRVGIILNRD NVAEKIYLNQ KVQNPNVLFM EVERADLEAG
     LWIEGYDEED QFIRIDVSRT AKIVENGTET IIAPLDRQFN SKTVGQRAMA IFAGPLFNFI
     LAFAIFIVLA LLTGIPTTDP LIKGIVDDSP AQQAGLQDGD LVKSIDGVAV QDWQGIVNIV
     QENPGEKLTF TIDRDGQAQQ FTVIPKAFEN EQGVVVGQIG VYSPIEDANI LDAIVFGAQK
     TLEFSTLIFT LLYELIVINF DIDALSGPVG IYKATEEVAQ YGIYNLMNWA AVLSINLGIM
     NLLPLPALDG GRLLFFGLEA LRGKPVDRQK EGLVHFVGIV LLMILMVIVT WKDIKLFFF
//