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KEFF_ENT38
ID   KEFF_ENT38              Reviewed;         176 AA.
AC   A4W6F2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=Ent638_0595;
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638;
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(2010).
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; CP000653; ABP59282.1; -; Genomic_DNA.
DR   RefSeq; WP_012016004.1; NC_009436.1.
DR   AlphaFoldDB; A4W6F2; -.
DR   SMR; A4W6F2; -.
DR   STRING; 399742.Ent638_0595; -.
DR   EnsemblBacteria; ABP59282; ABP59282; Ent638_0595.
DR   KEGG; ent:Ent638_0595; -.
DR   eggNOG; COG2249; Bacteria.
DR   HOGENOM; CLU_058643_0_2_6; -.
DR   OMA; QHRSEVN; -.
DR   OrthoDB; 1143659at2; -.
DR   Proteomes; UP000000230; 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.
FT   CHAIN           1..176
FT                   /note="Glutathione-regulated potassium-efflux system
FT                   ancillary protein KefF"
FT                   /id="PRO_1000068468"
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;  20132 MW;  C007DEBD0EEA1456 CRC64;
     MILIIYAHPY PRHSHANKRM LDQVKVLDGV EIRSLYELYP DFNIDIAAEQ EAISRADLIV
     WQHPMQWYST PALLKLWIDK VFSHGWAYGH NGHALKGKSV LWAVTTGGGE AHFDIGSHPG
     FEVLAQPLQA TALYCGLQWL PPFAMHCTFV CDDETLQAQA RHYKQRLLDW QETHNG
 
 
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