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Database: UniProt
Entry: E8LRC8_9VIBR
LinkDB: E8LRC8_9VIBR
Original site: E8LRC8_9VIBR 
ID   E8LRC8_9VIBR            Unreviewed;       195 AA.
AC   E8LRC8;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Glutathione-regulated potassium-efflux system ancillary protein KefG {ECO:0000256|HAMAP-Rule:MF_01415};
DE   AltName: Full=Putative quinone oxidoreductase KefG {ECO:0000256|HAMAP-Rule:MF_01415};
DE            EC=1.6.5.2 {ECO:0000256|HAMAP-Rule:MF_01415};
GN   Name=kefG {ECO:0000256|HAMAP-Rule:MF_01415};
GN   ORFNames=VIBR0546_14942 {ECO:0000313|EMBL:EGA66771.1};
OS   Vibrio brasiliensis LMG 20546.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio; Vibrio oreintalis group.
OX   NCBI_TaxID=945543 {ECO:0000313|EMBL:EGA66771.1, ECO:0000313|Proteomes:UP000004371};
RN   [1] {ECO:0000313|EMBL:EGA66771.1, ECO:0000313|Proteomes:UP000004371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 20546 {ECO:0000313|EMBL:EGA66771.1,
RC   ECO:0000313|Proteomes:UP000004371};
RX   PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA   Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA   McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT   "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT   Scleritoderma cyanea.";
RL   Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
CC   -!- FUNCTION: Regulatory subunit of a potassium efflux system that confers
CC       protection against electrophiles. Required for full activity of KefB.
CC       {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01415};
CC   -!- SUBUNIT: Interacts with KefB. {ECO:0000256|HAMAP-Rule:MF_01415}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01415}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01415}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_01415}.
CC   -!- SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family. KefG
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_01415}.
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:EGA66771.1}.
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DR   EMBL; AEVS01000031; EGA66771.1; -; Genomic_DNA.
DR   RefSeq; WP_006878375.1; NZ_AEVS01000031.1.
DR   AlphaFoldDB; E8LRC8; -.
DR   STRING; 945543.VIBR0546_14942; -.
DR   eggNOG; COG2249; Bacteria.
DR   OrthoDB; 9798454at2; -.
DR   Proteomes; UP000004371; Unassembled WGS sequence.
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: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   InterPro; IPR046980; KefG/KefF.
DR   PANTHER; PTHR47307; GLUTATHIONE-REGULATED POTASSIUM-EFFLUX SYSTEM ANCILLARY PROTEIN KEFG; 1.
DR   PANTHER; PTHR47307:SF1; 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_01415};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01415};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01415};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01415};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01415}.
FT   DOMAIN          10..177
FT                   /note="Flavodoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF02525"
SQ   SEQUENCE   195 AA;  22414 MW;  884CA3AEE4255C83 CRC64;
     MKNLSSDKPK VLVLYAHPES QTSVANQIMI KKIESLDHVT VHDLYAHYPD FFIDVSAEHQ
     LLNEHDVIVF HHPLFMYSCP ALLKEWLDRV LGKGFAFGKG EALKGKYWRS VITTGGQEGA
     FAKTGYNRYP LAEILQPFEL TAALCQMHWI EPLVLYWARN VSEMERYQHA ERYRQWLNDP
     LQIDLPDVVG GENGA
//
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