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KEFG_SHIF8
ID   KEFG_SHIF8              Reviewed;         183 AA.
AC   Q0SZW5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
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}; OrderedLocusNames=SFV_3357;
OS   Shigella flexneri serotype 5b (strain 8401).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8401;
RX   PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA   Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA   Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT   "Complete genome sequence of Shigella flexneri 5b and comparison with
RT   Shigella flexneri 2a.";
RL   BMC Genomics 7:173-173(2006).
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; CP000266; ABF05400.1; -; Genomic_DNA.
DR   RefSeq; WP_001445921.1; NC_008258.1.
DR   AlphaFoldDB; Q0SZW5; -.
DR   SMR; Q0SZW5; -.
DR   EnsemblBacteria; ABF05400; ABF05400; SFV_3357.
DR   KEGG; sfv:SFV_3357; -.
DR   HOGENOM; CLU_058643_0_1_6; -.
DR   OMA; RYPMSDI; -.
DR   BioCyc; SFLE373384:SFV_RS18500-MON; -.
DR   Proteomes; UP000000659; 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..183
FT                   /note="Glutathione-regulated potassium-efflux system
FT                   ancillary protein KefG"
FT                   /id="PRO_1000068484"
SQ   SEQUENCE   183 AA;  20854 MW;  FB70B4E4D44B9E43 CRC64;
     MSQPAKVLLL YAHPESQDSV ANRVLLKPAT QLSNVTVHDL YAHYPDFFID IPREQALLRE
     HEVIVFQHPL YTYSCPALLK EWLDRVLSRG FASGPGGNQL AGKYWRNVIT TGEPESAYRY
     DALNRYPMSD VLRPFELAAG MCRMHWLSPI IIYWARRQSA KELASHARAY GDWLANPLSP
     GGR
 
 
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