ID A0A1N6F6K7_9RHOB Unreviewed; 455 AA.
AC A0A1N6F6K7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=SAMN05444002_1414 {ECO:0000313|EMBL:SIN90836.1};
OS Vannielia litorea.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Vannielia.
OX NCBI_TaxID=1217970 {ECO:0000313|EMBL:SIN90836.1, ECO:0000313|Proteomes:UP000184932};
RN [1] {ECO:0000313|Proteomes:UP000184932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29440 {ECO:0000313|Proteomes:UP000184932};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FSRL01000001; SIN90836.1; -; Genomic_DNA.
DR RefSeq; WP_074255489.1; NZ_FSRL01000001.1.
DR AlphaFoldDB; A0A1N6F6K7; -.
DR STRING; 1217970.SAMN05444002_1414; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000184932; 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.
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:SIN90836.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184932};
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..27
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..395
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 416..437
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 133..203
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT DOMAIN 204..272
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 455 AA; 48069 MW; 45F97F50FA73EEBF CRC64;
MDFFGIVGGT AGYVVAFIVA LSIIVAVHEY GHYIVGRWCG IHAEVFSLGF GKVLYTRTDK
RGTEWQVAAL PFGGYVKFMG DANAASAGAD GEAMAGLSAA EKRRTMPGAP LWARAATVAA
GPVFNFILSL VIFSAMVALR GVPTEPVQVG ALQPLPQQVR VLEAGDTILE IGGTEITDIG
SLYDATAALD LTRPVSYRIE REGAEMIVEG TTPFPPLIAS VSPHSAAIDA GLEVGDVITS
VDGVAITAFK ELQEAVRLGE GKPVALKVWR DGQVLDFTMT PRRTDLPTAD GGFETRYLIG
INGGLAFEPA TDRLGPFAAL GYGVKQTWFI VTSSINGLAK MISGAISSCN LSGPLKIATT
AGQMASQGGE SFIWFVAVLS TAVGLLNLFP IPVLDGGHLV FHAWEAVSGK PPPEKALNIL
MMIGLTLILS LMVFALGNDL FCEGGLFWKI RSWFA
//
