ID E5YJ16_9ENTR Unreviewed; 190 AA.
AC E5YJ16;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Glutathione-regulated potassium-efflux system ancillary protein KefF {ECO:0000256|HAMAP-Rule:MF_01414};
DE AltName: Full=Quinone oxidoreductase KefF {ECO:0000256|HAMAP-Rule:MF_01414};
DE EC=1.6.5.2 {ECO:0000256|HAMAP-Rule:MF_01414};
GN Name=kefF {ECO:0000256|HAMAP-Rule:MF_01414};
GN ORFNames=HMPREF0864_02526 {ECO:0000313|EMBL:EFV40070.1};
OS Enterobacteriaceae bacterium 9_2_54FAA.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae.
OX NCBI_TaxID=469613 {ECO:0000313|EMBL:EFV40070.1, ECO:0000313|Proteomes:UP000004908};
RN [1] {ECO:0000313|EMBL:EFV40070.1, ECO:0000313|Proteomes:UP000004908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9_2_54FAA {ECO:0000313|EMBL:EFV40070.1,
RC ECO:0000313|Proteomes:UP000004908};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C.,
RA Allen-Vercoe E., Ambrose C., Strauss J., Sibley C., Haas B., Nusbaum C.,
RA Birren B.;
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EFV40070.1, ECO:0000313|Proteomes:UP000004908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9_2_54FAA {ECO:0000313|EMBL:EFV40070.1,
RC ECO:0000313|Proteomes:UP000004908};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Allen-Vercoe E., Ambrose C.,
RA Strauss J., Sibley C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterobacteriaceae bacterium 9_2_54FAA.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01414};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01414};
CC -!- SUBUNIT: Homodimer. Interacts with KefC. {ECO:0000256|HAMAP-
CC Rule:MF_01414}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01414}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01414}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01414}.
CC -!- SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family. KefF
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01414}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFV40070.1}.
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DR EMBL; ADCU02000001; EFV40070.1; -; Genomic_DNA.
DR AlphaFoldDB; E5YJ16; -.
DR Proteomes; UP000004908; Unassembled WGS sequence.
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: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 InterPro; IPR046980; KefG/KefF.
DR PANTHER; PTHR47307:SF2; GLUTATHIONE-REGULATED POTASSIUM-EFFLUX SYSTEM ANCILLARY PROTEIN KEFF; 1.
DR PANTHER; PTHR47307; GLUTATHIONE-REGULATED POTASSIUM-EFFLUX SYSTEM ANCILLARY PROTEIN KEFG; 1.
DR Pfam; PF02525; Flavodoxin_2; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01414};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_01414};
KW Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01414};
KW FMN {ECO:0000256|HAMAP-Rule:MF_01414};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_01414};
KW NAD {ECO:0000256|HAMAP-Rule:MF_01414};
KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01414}.
FT DOMAIN 2..166
FT /note="Flavodoxin-like fold"
FT /evidence="ECO:0000259|Pfam:PF02525"
FT BINDING 8
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01414"
FT BINDING 14..17
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01414"
FT BINDING 65..68
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01414"
FT BINDING 105..108
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01414"
SQ SEQUENCE 190 AA; 21788 MW; 660DC666CD02D8E5 CRC64;
MILIIYAHPY PRHSHANKRL LDAVSNIPEV KVRSLYDLYP DFNINVAAEQ QALSQADLII
LQHPMQWYSV PPLLKLWMDK VLEHGWAYGH NGKALEGKDF MWAVTTGGND RHFDLGDHPT
FPVLSQPIQA TALYCGMNWL PYFAEHNTFS CDEPALIRAS ESYRRRLMNY LMLHAETELP
STDAEEPTHG
//
