ID   A0A318N245_9PROT        Unreviewed;       368 AA.
AC   A0A318N245;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN   Name=rseP {ECO:0000313|EMBL:PXZ01633.1};
GN   ORFNames=DK869_01075 {ECO:0000313|EMBL:PXZ01633.1};
OS   Commensalibacter melissae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae.
OX   NCBI_TaxID=2070537 {ECO:0000313|EMBL:PXZ01633.1, ECO:0000313|Proteomes:UP000247565};
RN   [1] {ECO:0000313|EMBL:PXZ01633.1, ECO:0000313|Proteomes:UP000247565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ESL0284 {ECO:0000313|EMBL:PXZ01633.1,
RC   ECO:0000313|Proteomes:UP000247565};
RA   Ellegaard K.M.;
RT   "Reference genomes for bee gut microbiota database.";
RL   Submitted (MAY-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:PXZ01633.1}.
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DR   EMBL; QGLT01000001; PXZ01633.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A318N245; -.
DR   OrthoDB; 9782003at2; -.
DR   Proteomes; UP000247565; 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.
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:PXZ01633.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000247565};
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..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        105..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        286..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        332..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   DOMAIN          124..192
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
SQ   SEQUENCE   368 AA;  41023 MW;  6E970E29A4179581 CRC64;
     MHAFIVTIIS FIFVLGVLVF IHELGHYLAA RWRGVHVDVF SIGFGKPLYK WRDKVGTEWR
     LCPIPLGGYV KPHGFEDPED ATDEQKANWI PGRTFHAKSV LDRSIVIFAG PFFNFVLAVI
     LFAGVFAISG KPFIKPVVEN IVPNSAASQA GMKPHDIIIQ IDKYKNPDAQ SLALFAKKHP
     GMTTTVIVKR EGKEVSLPIT ISSKLIDHKS IGQLGIVMGR IFVEKHRLSI EDSVVYAFRE
     TWNITADTVI GLGQMVTRQR SLSELGGPIK IAQISGQVAE KGFDQLILMM AVLSINLGLI
     NLFPIPMLDG GRLLFYVIEA VCRKPVHKKI QVWAFQIGFG LILLLFLFST YNDISQLGLI
     SWFTSHSK
//