KEFF_ECOLI
ID KEFF_ECOLI Reviewed; 176 AA.
AC P0A754; P31577; P75629;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
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}; Synonyms=yabF;
GN OrderedLocusNames=b0046, JW0045;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 79
RP AND 123.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION.
RC STRAIN=Frag5;
RX PubMed=11053405; DOI=10.1128/jb.182.22.6536-6540.2000;
RA Miller S., Ness L.S., Wood C.M., Fox B.C., Booth I.R.;
RT "Identification of an ancillary protein, YabF, required for activity of the
RT KefC glutathione-gated potassium efflux system in Escherichia coli.";
RL J. Bacteriol. 182:6536-6540(2000).
RN [5]
RP SUBUNIT.
RX PubMed=17679694; DOI=10.1073/pnas.0703709104;
RA Fujisawa M., Ito M., Krulwich T.A.;
RT "Three two-component transporters with channel-like properties have
RT monovalent cation/proton antiport activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:13289-13294(2007).
RN [6]
RP FUNCTION AS AN OXIDOREDUCTASE, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND
RP MUTAGENESIS OF GLY-107; HIS-112 AND PHE-149.
RX PubMed=21742892; DOI=10.1128/jb.05272-11;
RA Lyngberg L., Healy J., Bartlett W., Miller S., Conway S.J., Booth I.R.,
RA Rasmussen T.;
RT "KefF, the regulatory subunit of the potassium efflux system KefC, shows
RT quinone oxidoreductase activity.";
RL J. Bacteriol. 193:4925-4932(2011).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH KEFC AND FMN,
RP FUNCTION, SUBUNIT, INTERACTION WITH KEFC, MUTAGENESIS OF ASP-41, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=19523906; DOI=10.1016/j.str.2009.03.018;
RA Roosild T.P., Castronovo S., Miller S., Li C., Rasmussen T., Bartlett W.,
RA Gunasekera B., Choe S., Booth I.R.;
RT "KTN (RCK) domains regulate K+ channels and transporters by controlling the
RT dimer-hinge conformation.";
RL Structure 17:893-903(2009).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH KEFC AND FMN,
RP SUBUNIT, FMN-BINDING, AND INTERACTION WITH KEFC.
RX PubMed=21041667; DOI=10.1073/pnas.1012716107;
RA Roosild T.P., Castronovo S., Healy J., Miller S., Pliotas C., Rasmussen T.,
RA Bartlett W., Conway S.J., Booth I.R.;
RT "Mechanism of ligand-gated potassium efflux in bacterial pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:19784-19789(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. Can use a wide range of substrates,
CC including electrophilic quinones, and its function could be to reduce
CC the redox toxicity of electrophilic quinones in parallel with acting as
CC triggers for the KefC efflux system. {ECO:0000255|HAMAP-Rule:MF_01414,
CC ECO:0000269|PubMed:11053405, ECO:0000269|PubMed:19523906,
CC ECO:0000269|PubMed:21742892}.
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 ECO:0000269|PubMed:21742892};
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 ECO:0000269|PubMed:21742892};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01414,
CC ECO:0000269|PubMed:21742892};
CC -!- SUBUNIT: Homodimer. Interacts with KefC, forming a heterotetramer with
CC 2:2 stoichiometry. {ECO:0000255|HAMAP-Rule:MF_01414,
CC ECO:0000269|PubMed:17679694, ECO:0000269|PubMed:19523906,
CC ECO:0000269|PubMed:21041667, ECO:0000269|PubMed:21742892}.
CC -!- INTERACTION:
CC P0A754; P03819: kefC; NbExp=2; IntAct=EBI-562116, EBI-547193;
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; U00096; AAC73157.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96614.2; -; Genomic_DNA.
DR PIR; F64725; F64725.
DR RefSeq; NP_414588.1; NC_000913.3.
DR RefSeq; WP_000600725.1; NZ_STEB01000010.1.
DR PDB; 3EYW; X-ray; 2.40 A; A/B=1-176.
DR PDB; 3L9W; X-ray; 1.75 A; A/B=1-176.
DR PDB; 3L9X; X-ray; 2.10 A; A/B=1-176.
DR PDBsum; 3EYW; -.
DR PDBsum; 3L9W; -.
DR PDBsum; 3L9X; -.
DR AlphaFoldDB; P0A754; -.
DR SMR; P0A754; -.
DR BioGRID; 4262201; 9.
DR BioGRID; 849169; 1.
DR ComplexPortal; CPX-2543; Glutathione-regulated potassium-efflux system KefC-KefF complex.
DR DIP; DIP-35822N; -.
DR IntAct; P0A754; 8.
DR STRING; 511145.b0046; -.
DR TCDB; 2.A.37.1.1; the monovalent cation:proton antiporter-2 (cpa2) family.
DR PaxDb; P0A754; -.
DR PRIDE; P0A754; -.
DR EnsemblBacteria; AAC73157; AAC73157; b0046.
DR EnsemblBacteria; BAB96614; BAB96614; BAB96614.
DR GeneID; 66671664; -.
DR GeneID; 944767; -.
DR KEGG; ecj:JW0045; -.
DR KEGG; eco:b0046; -.
DR PATRIC; fig|1411691.4.peg.2237; -.
DR EchoBASE; EB1528; -.
DR eggNOG; COG2249; Bacteria.
DR HOGENOM; CLU_058643_0_2_6; -.
DR InParanoid; P0A754; -.
DR OMA; QHRSEVN; -.
DR PhylomeDB; P0A754; -.
DR BioCyc; EcoCyc:EG11568-MON; -.
DR BioCyc; MetaCyc:EG11568-MON; -.
DR EvolutionaryTrace; P0A754; -.
DR PRO; PR:P0A754; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1903103; C:potassium:proton antiporter complex; IPI:ComplexPortal.
DR GO; GO:0009055; F:electron transfer activity; IMP:EcoliWiki.
DR GO; GO:0010181; F:FMN binding; IDA:EcoCyc.
DR GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IDA:EcoCyc.
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:0051454; P:intracellular pH elevation; IC:ComplexPortal.
DR GO; GO:0032414; P:positive regulation of ion transmembrane transporter activity; IDA:EcoCyc.
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 GO; GO:0051453; P:regulation of intracellular pH; IC:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Flavoprotein; FMN;
KW Membrane; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..176
FT /note="Glutathione-regulated potassium-efflux system
FT ancillary protein KefF"
FT /id="PRO_0000071635"
FT BINDING 8
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01414,
FT ECO:0000269|PubMed:19523906, ECO:0000269|PubMed:21041667"
FT BINDING 14..17
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01414,
FT ECO:0000269|PubMed:19523906, ECO:0000269|PubMed:21041667"
FT BINDING 65..68
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01414,
FT ECO:0000269|PubMed:19523906, ECO:0000269|PubMed:21041667"
FT BINDING 105..108
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01414,
FT ECO:0000269|PubMed:19523906, ECO:0000269|PubMed:21041667"
FT MUTAGEN 41
FT /note="D->K: Strongly reduced potassium efflux."
FT /evidence="ECO:0000269|PubMed:19523906"
FT MUTAGEN 107
FT /note="G->S: Does not bind FMN. Lacks oxidoreductase
FT activity, but is still able to activate potassium efflux."
FT /evidence="ECO:0000269|PubMed:21742892"
FT MUTAGEN 112
FT /note="H->W: Lacks oxidoreductase activity, but is still
FT able to activate potassium efflux."
FT /evidence="ECO:0000269|PubMed:21742892"
FT MUTAGEN 149
FT /note="F->W: Lacks oxidoreductase activity, but is still
FT able to activate potassium efflux."
FT /evidence="ECO:0000269|PubMed:21742892"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:3L9W"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:3L9W"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:3L9W"
FT STRAND 27..34
FT /evidence="ECO:0007829|PDB:3L9W"
FT HELIX 35..38
FT /evidence="ECO:0007829|PDB:3L9W"
FT HELIX 46..54
FT /evidence="ECO:0007829|PDB:3L9W"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:3L9W"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3EYW"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:3L9W"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:3L9W"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:3L9W"
FT TURN 94..97
FT /evidence="ECO:0007829|PDB:3L9W"
FT STRAND 99..105
FT /evidence="ECO:0007829|PDB:3L9W"
FT HELIX 110..113
FT /evidence="ECO:0007829|PDB:3L9W"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:3L9W"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:3L9W"
FT HELIX 126..134
FT /evidence="ECO:0007829|PDB:3L9W"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:3L9W"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:3L9X"
FT HELIX 153..172
FT /evidence="ECO:0007829|PDB:3L9W"
SQ SEQUENCE 176 AA; 20170 MW; F641E3952F4EFC41 CRC64;
MILIIYAHPY PHHSHANKRM LEQARTLEGV EIRSLYQLYP DFNIDIAAEQ EALSRADLIV
WQHPMQWYSI PPLLKLWIDK VFSHGWAYGH GGTALHGKHL LWAVTTGGGE SHFEIGAHPG
FDVLSQPLQA TAIYCGLNWL PPFAMHCTFI CDDETLEGQA RHYKQRLLEW QEAHHG
