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KEFF_SALTY
ID   KEFF_SALTY              Reviewed;         176 AA.
AC   Q8ZRW3;
DT   03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=STM0085;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
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; AE006468; AAL19049.1; -; Genomic_DNA.
DR   RefSeq; NP_459090.1; NC_003197.2.
DR   RefSeq; WP_000600709.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZRW3; -.
DR   SMR; Q8ZRW3; -.
DR   STRING; 99287.STM0085; -.
DR   PaxDb; Q8ZRW3; -.
DR   EnsemblBacteria; AAL19049; AAL19049; STM0085.
DR   GeneID; 1251603; -.
DR   KEGG; stm:STM0085; -.
DR   PATRIC; fig|99287.12.peg.88; -.
DR   HOGENOM; CLU_058643_0_2_6; -.
DR   OMA; QHRSEVN; -.
DR   PhylomeDB; Q8ZRW3; -.
DR   BioCyc; SENT99287:STM0085-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR   GO; GO:0010181; F:FMN binding; IBA:GO_Central.
DR   GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..176
FT                   /note="Glutathione-regulated potassium-efflux system
FT                   ancillary protein KefF"
FT                   /id="PRO_0000071640"
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;  20005 MW;  9E5CF2FB7B684BE5 CRC64;
     MILIIYAHPY PHHSHANKRM LEQAGTLENV EIRSLYHLYP DFNIDVAAEQ EALSRASLIV
     WQHPMQWYSV PPLLKLWMDK VLTHGWAYGH GGTALHGKHL LWAVTTGGGE NHFAIGSHPG
     FDVLSQPLQA TALYCGLKWL SPFAMHCTFI CDDDTLQAQA RQYKQRLLAW QEVNHG
 
 
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