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KEFG_PECCP
ID   KEFG_PECCP              Reviewed;         183 AA.
AC   C6DG98;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   25-MAY-2022, entry version 70.
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=PC1_3846;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) 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 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; CP001657; ACT14861.1; -; Genomic_DNA.
DR   RefSeq; WP_015841946.1; NC_012917.1.
DR   AlphaFoldDB; C6DG98; -.
DR   SMR; C6DG98; -.
DR   STRING; 561230.PC1_3846; -.
DR   EnsemblBacteria; ACT14861; ACT14861; PC1_3846.
DR   KEGG; pct:PC1_3846; -.
DR   eggNOG; COG2249; Bacteria.
DR   HOGENOM; CLU_058643_0_1_6; -.
DR   OMA; RYPMSDI; -.
DR   OrthoDB; 1143659at2; -.
DR   Proteomes; UP000002736; 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_1000215227"
SQ   SEQUENCE   183 AA;  21276 MW;  D044C6AE26DAA0F0 CRC64;
     MSQPPKILLL YAHPEPQDSV ANRVLLQPAQ QLANVTVHDL YAHYPDFFID IHHEQQLLRE
     HQVIVFQHPF YTYSCPALLK EWLDRVLSRG FANGIGGNAL AGKYWRSVIT TGEPEDAYHP
     DGNNRYPMED LLRPFELTAA MCRMHWMHPM IVYWARRLQP DVLSSQARAY GEWLASPLPE
     EER
 
 
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