KEFF_ECOLC
ID KEFF_ECOLC Reviewed; 176 AA.
AC B1IRD0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=EcolC_3609;
OS Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS WDCM 00012 / Crooks).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=481805;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Ingram L., Richardson P.;
RT "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL Submitted (FEB-2008) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000946; ACA79223.1; -; Genomic_DNA.
DR RefSeq; WP_000600735.1; NZ_CP022959.1.
DR AlphaFoldDB; B1IRD0; -.
DR SMR; B1IRD0; -.
DR KEGG; ecl:EcolC_3609; -.
DR HOGENOM; CLU_058643_0_2_6; -.
DR OMA; QHRSEVN; -.
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_1000087400"
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; 20163 MW; 06A0036D55123091 CRC64;
MILIIYAHPY PHHSHANKRM LEQARTLEGV EIRSLYQLYP DFNIDIAAEQ EALSRADLIV
WQHPMQWYSI PPLLKLWIDK VLSHGWAYGH GGKALHGKHL LWAVTTGGGE SHFEIGAHPG
FDVLSQPLQA TAIYCGLNWL PPFAMHCTFI CDDETLEGQA RHYKQRLLEW QEAHHG
