KEFF_ECO45
ID KEFF_ECO45 Reviewed; 176 AA.
AC B7MAG9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=ECS88_0049;
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928161; CAR01415.1; -; Genomic_DNA.
DR RefSeq; WP_000600749.1; NC_011742.1.
DR AlphaFoldDB; B7MAG9; -.
DR SMR; B7MAG9; -.
DR EnsemblBacteria; CAR01415; CAR01415; ECS88_0049.
DR KEGG; ecz:ECS88_0049; -.
DR HOGENOM; CLU_058643_0_1_6; -.
DR OMA; YFAVHNT; -.
DR Proteomes; UP000000747; 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_1000145553"
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; 20196 MW; 0355A68E35F013F0 CRC64;
MILIIYAHPY PHYSHANKRM LEQARTLEGV EIRSLYQLYP DFNIDIAAEQ EALSRADLIV
WQHPMQWYSI PPLLKLWIDK VFSHGWAYGH GGTALHGKHL LWAVTTGGGE SHFEIGAHPG
FDVLSQPLQA TAIYCGLNWL PPFAMHCTFI CDDETLEGQA RHYKQRLLEW QEAHHG
