ID   KEFG_CROS8              Reviewed;         184 AA.
AC   A7ME22;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Glutathione-regulated potassium-efflux system ancillary protein KefG {ECO:0000255|HAMAP-Rule:MF_01415};
DE   AltName: Full=Putative quinone oxidoreductase KefG {ECO:0000255|HAMAP-Rule:MF_01415};
DE            EC=1.6.5.2 {ECO:0000255|HAMAP-Rule:MF_01415};
GN   Name=kefG {ECO:0000255|HAMAP-Rule:MF_01415}; OrderedLocusNames=ESA_04388;
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894;
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(2010).
CC   -!- FUNCTION: Regulatory subunit of a potassium efflux system that confers
CC       protection against electrophiles. Required for full activity of KefB.
CC       {ECO:0000255|HAMAP-Rule:MF_01415}.
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_01415};
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_01415};
CC   -!- SUBUNIT: Interacts with KefB. {ECO:0000255|HAMAP-Rule:MF_01415}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01415}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01415}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01415}.
CC   -!- SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family. KefG
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01415}.
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DR   EMBL; CP000783; ABU79567.1; -; Genomic_DNA.
DR   RefSeq; WP_007852589.1; NC_009778.1.
DR   AlphaFoldDB; A7ME22; -.
DR   SMR; A7ME22; -.
DR   EnsemblBacteria; ABU79567; ABU79567; ESA_04388.
DR   KEGG; esa:ESA_04388; -.
DR   HOGENOM; CLU_058643_0_1_6; -.
DR   OMA; RYPMSDI; -.
DR   OrthoDB; 1143659at2; -.
DR   Proteomes; UP000000260; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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_01415; K_H_efflux_KefG; 1.
DR   InterPro; IPR003680; Flavodoxin_fold.
DR   InterPro; IPR029039; Flavoprotein-like_sf.
DR   InterPro; IPR023947; K_H_efflux_KefG.
DR   Pfam; PF02525; Flavodoxin_2; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Oxidoreductase.
FT   CHAIN           1..184
FT                   /note="Glutathione-regulated potassium-efflux system
FT                   ancillary protein KefG"
FT                   /id="PRO_1000145578"
SQ   SEQUENCE   184 AA;  21109 MW;  8391A77F215366F6 CRC64;
     MMSQTAKVLL LYAHPESQDS VANRVLLKPA LQLPNVTVHD LYAHYPDFFI DISHEQALLR
     DHDVIVFQFP LYTYSCPALL KEWFDRVLSR GFASGVGGNQ LAGKYWRCVI TTGEPETAYR
     PDGFNRYALS DILRPFELTA AMCRMHWMTP LIIYWARRQS LSELASHGRA YERWLADPLT
     PGGF