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KEFG_YERP3
ID   KEFG_YERP3              Reviewed;         182 AA.
AC   A7FNQ1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   25-MAY-2022, entry version 76.
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};
GN   OrderedLocusNames=YpsIP31758_3931;
OS   Yersinia pseudotuberculosis serotype O:1b (strain IP 31758).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP 31758;
RX   PubMed=17784789; DOI=10.1371/journal.pgen.0030142;
RA   Eppinger M., Rosovitz M.J., Fricke W.F., Rasko D.A., Kokorina G.,
RA   Fayolle C., Lindler L.E., Carniel E., Ravel J.;
RT   "The complete genome sequence of Yersinia pseudotuberculosis IP31758, the
RT   causative agent of Far East scarlet-like fever.";
RL   PLoS Genet. 3:1508-1523(2007).
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; CP000720; ABS49752.1; -; Genomic_DNA.
DR   RefSeq; WP_012105870.1; NC_009708.1.
DR   AlphaFoldDB; A7FNQ1; -.
DR   SMR; A7FNQ1; -.
DR   EnsemblBacteria; ABS49752; ABS49752; YpsIP31758_3931.
DR   KEGG; ypi:YpsIP31758_3931; -.
DR   HOGENOM; CLU_058643_0_1_6; -.
DR   OMA; RYPMSDI; -.
DR   Proteomes; UP000002412; 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..182
FT                   /note="Glutathione-regulated potassium-efflux system
FT                   ancillary protein KefG"
FT                   /id="PRO_1000068486"
SQ   SEQUENCE   182 AA;  21226 MW;  64E410DF34EF943A CRC64;
     MLQPPKVLLL YAHPESQDSV ANRVLLQPVQ QLEHVTVHDL YAHYPDFFID IHHEQQLLRD
     HQVIVFQHPL YTYSCPALLK EWLDRVLARG FANGVGGHAL TGKYWRSVIT TGEQEGTYRI
     GGYNRYPMED ILRPFELTAA MCHMHWINPM IIYWARRQKP ETLASHAQAY VQWLQSPLTR
     GL
 
 
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