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Database: UniProt
Entry: A0A2T6KS26_9RHOB
LinkDB: A0A2T6KS26_9RHOB
Original site: A0A2T6KS26_9RHOB 
ID   A0A2T6KS26_9RHOB        Unreviewed;       444 AA.
AC   A0A2T6KS26;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, 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=C8N45_101959 {ECO:0000313|EMBL:PUB19361.1};
OS   Yoonia sediminilitoris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Yoonia.
OX   NCBI_TaxID=1286148 {ECO:0000313|EMBL:PUB19361.1, ECO:0000313|Proteomes:UP000244523};
RN   [1] {ECO:0000313|EMBL:PUB19361.1, ECO:0000313|Proteomes:UP000244523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29955 {ECO:0000313|EMBL:PUB19361.1,
RC   ECO:0000313|Proteomes:UP000244523};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (APR-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:PUB19361.1}.
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DR   EMBL; QBUD01000001; PUB19361.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T6KS26; -.
DR   Proteomes; UP000244523; 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; -; 2.
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; 2.
DR   SUPFAM; SSF50156; PDZ domain-like; 2.
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:PUB19361.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244523};
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..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        111..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        372..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        415..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   DOMAIN          197..260
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   444 AA;  47701 MW;  AAFCA968BE945439 CRC64;
     MDLLTQFAPM FGGFAFMIVA FVVALSVIVA IHEYGHYIVG RWCGIHADVF SLGFGPVLYS
     RTDKRGTVWQ VAALPIGGYV KFMGDADAAS AGSDGSVAEA DMRKTMMGAP LWARAATVAA
     GPAFNFILAI LIFAGSIMYQ GRAIDPPTFG AMQDLPPSYA SDLRRGDVMV AVEGIPFVDA
     EREESLIDLL PAKERLAYEI ERDGQTLVID GPYLRPTAVS SVSPRSAADD AGLRVGDVIT
     AVNGEPIFAF SQLQEMVRNA EGAELTLGIW RDGDTLPVTL APRRVDLPTA DGFETRWLIG
     ITGRIFFEEM TESIGPVEAV KIGAEQLWYT ATTSLSALEH VIMGQISTCN LSGPVGIAET
     SGSMARQGAQ SFIWFIGALS AAVGLVNLFP IPVLDGGHLA FYAYEAVTRR KPNERVLQVF
     MFVGLGLILS LMSFTILNDV LLCP
//
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