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KEFF_CITK8
ID   KEFF_CITK8              Reviewed;         176 AA.
AC   A8ALQ5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Glutathione-regulated potassium-efflux system ancillary protein KefF {ECO:0000255|HAMAP-Rule:MF_01414};
DE   AltName: Full=Quinone oxidoreductase KefF {ECO:0000255|HAMAP-Rule:MF_01414};
DE            EC=1.6.5.2 {ECO:0000255|HAMAP-Rule:MF_01414};
GN   Name=kefF {ECO:0000255|HAMAP-Rule:MF_01414}; OrderedLocusNames=CKO_03335;
OS   Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter.
OX   NCBI_TaxID=290338;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-895 / CDC 4225-83 / SGSC4696;
RG   The Citrobacter koseri Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Latreille P., Courtney L., Wang C., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Regulatory subunit of a potassium efflux system that confers
CC       protection against electrophiles. Required for full activity of KefC.
CC       Shows redox enzymatic activity, but this enzymatic activity is not
CC       required for activation of KefC. {ECO:0000255|HAMAP-Rule:MF_01414}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H(+) + NADH = a quinol + NAD(+);
CC         Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01414};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + H(+) + NADPH = a quinol + NADP(+);
CC         Xref=Rhea:RHEA:46164, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:132124; EC=1.6.5.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01414};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01414};
CC   -!- SUBUNIT: Homodimer. Interacts with KefC. {ECO:0000255|HAMAP-
CC       Rule:MF_01414}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01414}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01414}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01414}.
CC   -!- SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family. KefF
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01414}.
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DR   EMBL; CP000822; ABV14418.1; -; Genomic_DNA.
DR   RefSeq; WP_012134121.1; NC_009792.1.
DR   AlphaFoldDB; A8ALQ5; -.
DR   SMR; A8ALQ5; -.
DR   STRING; 290338.CKO_03335; -.
DR   EnsemblBacteria; ABV14418; ABV14418; CKO_03335.
DR   GeneID; 45137099; -.
DR   KEGG; cko:CKO_03335; -.
DR   HOGENOM; CLU_058643_0_2_6; -.
DR   OMA; YFAVHNT; -.
DR   OrthoDB; 1143659at2; -.
DR   Proteomes; UP000008148; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:RHEA.
DR   GO; GO:0008753; F:NADPH dehydrogenase (quinone) activity; IEA:RHEA.
DR   GO; GO:0032414; P:positive regulation of ion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0006813; P:potassium ion transport; IEA:InterPro.
DR   Gene3D; 3.40.50.360; -; 1.
DR   HAMAP; MF_01414; K_H_efflux_KefF; 1.
DR   InterPro; IPR003680; Flavodoxin_fold.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR023948; K_H_efflux_KefF.
DR   PANTHER; PTHR47307:SF2; PTHR47307:SF2; 1.
DR   Pfam; PF02525; Flavodoxin_2; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Flavoprotein; FMN; Membrane; NAD;
KW   Oxidoreductase; Reference proteome.
FT   CHAIN           1..176
FT                   /note="Glutathione-regulated potassium-efflux system
FT                   ancillary protein KefF"
FT                   /id="PRO_1000068462"
FT   BINDING         8
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01414"
FT   BINDING         14..17
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01414"
FT   BINDING         65..68
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01414"
FT   BINDING         105..108
FT                   /ligand="FMN"
FT                   /ligand_id="ChEBI:CHEBI:58210"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01414"
SQ   SEQUENCE   176 AA;  20084 MW;  B732A3949CE18248 CRC64;
     MILIIYAHPY PQHSHANKRM LEQARTLDGV EIRSLYQLYP DFNIDVAAEQ QALARARLII
     WQHPMQWYSV PPLLKLWMDK VLAHGWAYGH GGTALRDKDL MWAVTTGGGE SHFAIGAYPG
     FDVLSQPLQA TALYCGLNWL PPFAMHCTFV CDDETLQAQA RHYKQRLLAW QEANHG
 
 
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