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Database: UniProt
Entry: A0A1E5D6T0_9VIBR
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ID   A0A1E5D6T0_9VIBR        Unreviewed;       201 AA.
AC   A0A1E5D6T0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
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=A130_11425 {ECO:0000313|EMBL:OEE79337.1};
OS   Vibrio genomosp. F6 str. FF-238.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=1191298 {ECO:0000313|EMBL:OEE79337.1, ECO:0000313|Proteomes:UP000094165};
RN   [1] {ECO:0000313|EMBL:OEE79337.1, ECO:0000313|Proteomes:UP000094165}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FF-238 {ECO:0000313|EMBL:OEE79337.1,
RC   ECO:0000313|Proteomes:UP000094165};
RX   PubMed=22955834; DOI=10.1126/science.1219385;
RA   Cordero O.X., Wildschutte H., Kirkup B., Proehl S., Ngo L., Hussain F.,
RA   Le Roux F., Mincer T., Polz M.F.;
RT   "Ecological populations of bacteria act as socially cohesive units of
RT   antibiotic production and resistance.";
RL   Science 337:1228-1231(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:OEE79337.1}.
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DR   EMBL; AJYW02000026; OEE79337.1; -; Genomic_DNA.
DR   RefSeq; WP_017053162.1; NZ_AJYW02000026.1.
DR   AlphaFoldDB; A0A1E5D6T0; -.
DR   Proteomes; UP000094165; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094165}.
FT   DOMAIN          13..179
FT                   /note="Flavodoxin-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF02525"
SQ   SEQUENCE   201 AA;  23138 MW;  56AF22E0129D84B3 CRC64;
     MSDTQPQVAS PLKILVIYAH PEPHSSIANQ AMIKAIEPLG HVRVHDLYAT YPDFFIDVNF
     EHQLLLEHDV IVFQHPLYMY SCPALLKEWF DRVLSKGFAF GHECALEGKY WRSVITTGGQ
     EGAFGAQGYN KYPLEEILQP FELTASLCRM HWLDPLVLHW ARNINDKERE HHADRYRHWL
     QDPLGKLSEQ LSTTDGDADG Q
//
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