(data stored in SCRATCH zone)

SWISSPROT: C8U1C0_ECO10

ID   C8U1C0_ECO10            Unreviewed;       176 AA.
AC   C8U1C0;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 57.
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=kefF {ECO:0000256|HAMAP-Rule:MF_01414,
GN   ECO:0000313|EMBL:BAI28928.1};
GN   OrderedLocusNames=ECO103_0048 {ECO:0000313|EMBL:BAI28928.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28928.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28928.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- FUNCTION: Regulatory subunit of a potassium efflux system that
CC       confers protection against electrophiles. Required for full
CC       activity of KefC. Shows redox enzymatic activity, but this
CC       enzymatic activity is not required for activation of KefC.
CC       {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;
CC         EC=1.6.5.2; 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;
CC         EC=1.6.5.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01414};
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000256|HAMAP-
CC         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-
CC       Rule:MF_01414}.
CC   -!- SIMILARITY: Belongs to the NAD(P)H dehydrogenase (quinone) family.
CC       KefF subfamily. {ECO:0000256|HAMAP-Rule:MF_01414}.
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DR   EMBL; AP010958; BAI28928.1; -; Genomic_DNA.
DR   RefSeq; WP_000600725.1; NC_013353.1.
DR   SMR; C8U1C0; -.
DR   EnsemblBacteria; BAI28928; BAI28928; ECO103_0048.
DR   KEGG; eoh:ECO103_0048; -.
DR   HOGENOM; HOG000149972; -.
DR   KO; K11746; -.
DR   OMA; YWYSTPS; -.
DR   BioCyc; ECOL585395:ECO103_RS00250-MONOMER; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003955; F:NAD(P)H dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
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_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   PANTHER; PTHR47307:SF2; PTHR47307:SF2; 1.
DR   Pfam; PF02525; Flavodoxin_2; 1.
DR   SUPFAM; SSF52218; SSF52218; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U1C0.
DR   SWISS-2DPAGE; C8U1C0.
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01414};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01414};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
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}.
FT   DOMAIN        2    167       Flavodoxin_2. {ECO:0000259|Pfam:PF02525}.
FT   NP_BIND      14     17       FMN. {ECO:0000256|HAMAP-Rule:MF_01414}.
FT   NP_BIND      65     68       FMN. {ECO:0000256|HAMAP-Rule:MF_01414}.
FT   NP_BIND     105    108       FMN. {ECO:0000256|HAMAP-Rule:MF_01414}.
FT   BINDING       8      8       FMN. {ECO:0000256|HAMAP-Rule:MF_01414}.
SQ   SEQUENCE   176 AA;  20170 MW;  F641E3952F4EFC41 CRC64;
     MILIIYAHPY PHHSHANKRM LEQARTLEGV EIRSLYQLYP DFNIDIAAEQ EALSRADLIV
     WQHPMQWYSI PPLLKLWIDK VFSHGWAYGH GGTALHGKHL LWAVTTGGGE SHFEIGAHPG
     FDVLSQPLQA TAIYCGLNWL PPFAMHCTFI CDDETLEGQA RHYKQRLLEW QEAHHG
//

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