KEFF_SALHS
ID KEFF_SALHS Reviewed; 176 AA.
AC B4TII5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=SeHA_C0090;
OS Salmonella heidelberg (strain SL476).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=454169;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SL476;
RX PubMed=21602358; DOI=10.1128/jb.00297-11;
RA Fricke W.F., Mammel M.K., McDermott P.F., Tartera C., White D.G.,
RA Leclerc J.E., Ravel J., Cebula T.A.;
RT "Comparative genomics of 28 Salmonella enterica isolates: evidence for
RT CRISPR-mediated adaptive sublineage evolution.";
RL J. Bacteriol. 193:3556-3568(2011).
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; CP001120; ACF70177.1; -; Genomic_DNA.
DR RefSeq; WP_000600706.1; NC_011083.1.
DR AlphaFoldDB; B4TII5; -.
DR SMR; B4TII5; -.
DR KEGG; seh:SeHA_C0090; -.
DR HOGENOM; CLU_058643_0_2_6; -.
DR OMA; QHRSEVN; -.
DR Proteomes; UP000001866; 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_1000145567"
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; 20015 MW; 9E5CF2F986479BE5 CRC64;
MILIIYAHPY PHHSHANKRM LEQAGTLENV EIRSLYHLYP DFNIDVAAEQ EALSRASLIV
WQHPMQWYSV PPLLKLWMDK VLTHGWAYGH GGTALHGKHL LWAVTTGGGE NHFAIGSHPG
FDVLSQPLQA TALYCGLKWL PPFAMHCTFI CDDDTLQAQA RQYKQRLLAW QEVNHG
