ID A0A085G2Z4_9ENTR Unreviewed; 176 AA.
AC A0A085G2Z4;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=ywrO {ECO:0000313|EMBL:KFC78089.1};
GN Synonyms=kefF {ECO:0000256|HAMAP-Rule:MF_01414};
GN ORFNames=GBAG_3471 {ECO:0000313|EMBL:KFC78089.1};
OS Buttiauxella agrestis ATCC 33320.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Buttiauxella.
OX NCBI_TaxID=1006004 {ECO:0000313|EMBL:KFC78089.1, ECO:0000313|Proteomes:UP000028653};
RN [1] {ECO:0000313|EMBL:KFC78089.1, ECO:0000313|Proteomes:UP000028653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33320 {ECO:0000313|EMBL:KFC78089.1,
RC ECO:0000313|Proteomes:UP000028653};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-2014) 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:KFC78089.1}.
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DR EMBL; JMPI01000060; KFC78089.1; -; Genomic_DNA.
DR RefSeq; WP_034498462.1; NZ_JMPI01000060.1.
DR AlphaFoldDB; A0A085G2Z4; -.
DR STRING; 1006004.GBAG_3471; -.
DR eggNOG; COG2249; Bacteria.
DR OrthoDB; 9798454at2; -.
DR Proteomes; UP000028653; 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,
KW ECO:0000313|EMBL:KFC78089.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000028653}.
FT DOMAIN 2..165
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 176 AA; 20222 MW; 0E182F411A1CDB05 CRC64;
MILIIYAHPY PQHSHANKKM LEQASLLPDV EVRSLYELYP DFNIDIAAEQ QALNRADLVI
WQHPMQWYSM PPLMKLWIDK VLAHGWAYGH GGTALRGKQV MWAVTTGGGD HHFDLGDHPG
FDVLGQPLQA TALYCGMNWI PHFTIHFTFV CDENTLEVQA EMYKQRLLDW QEANHG
//
