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NQRE_ALISL
ID   NQRE_ALISL              Reviewed;         198 AA.
AC   B6EIC7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Na(+)-translocating NADH-quinone reductase subunit E {ECO:0000255|HAMAP-Rule:MF_00429};
DE            Short=Na(+)-NQR subunit E {ECO:0000255|HAMAP-Rule:MF_00429};
DE            Short=Na(+)-translocating NQR subunit E {ECO:0000255|HAMAP-Rule:MF_00429};
DE            EC=7.2.1.1 {ECO:0000255|HAMAP-Rule:MF_00429};
DE   AltName: Full=NQR complex subunit E {ECO:0000255|HAMAP-Rule:MF_00429};
DE   AltName: Full=NQR-1 subunit E {ECO:0000255|HAMAP-Rule:MF_00429};
GN   Name=nqrE {ECO:0000255|HAMAP-Rule:MF_00429}; OrderedLocusNames=VSAL_I0953;
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238;
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(2008).
CC   -!- FUNCTION: NQR complex catalyzes the reduction of ubiquinone-1 to
CC       ubiquinol by two successive reactions, coupled with the transport of
CC       Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are
CC       probably involved in the second step, the conversion of ubisemiquinone
CC       to ubiquinol. {ECO:0000255|HAMAP-Rule:MF_00429}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n
CC         Na(+)(out) + NAD(+); Xref=Rhea:RHEA:47748, Rhea:RHEA-COMP:9565,
CC         Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389,
CC         ChEBI:CHEBI:17976, ChEBI:CHEBI:29101, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=7.2.1.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00429};
CC   -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC       NqrF. {ECO:0000255|HAMAP-Rule:MF_00429}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00429}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00429}.
CC   -!- SIMILARITY: Belongs to the NqrDE/RnfAE family. {ECO:0000255|HAMAP-
CC       Rule:MF_00429}.
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DR   EMBL; FM178379; CAQ78638.1; -; Genomic_DNA.
DR   RefSeq; WP_012549723.1; NC_011312.1.
DR   AlphaFoldDB; B6EIC7; -.
DR   SMR; B6EIC7; -.
DR   STRING; 316275.VSAL_I0953; -.
DR   EnsemblBacteria; CAQ78638; CAQ78638; VSAL_I0953.
DR   KEGG; vsa:VSAL_I0953; -.
DR   eggNOG; COG2209; Bacteria.
DR   HOGENOM; CLU_095255_0_0_6; -.
DR   OMA; YFLGMCS; -.
DR   OrthoDB; 1814639at2; -.
DR   Proteomes; UP000001730; Chromosome 1.
DR   GO; GO:0009276; C:Gram-negative-bacterium-type cell wall; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR   GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00429; NqrE; 1.
DR   InterPro; IPR003667; NqrDE/RnfAE.
DR   InterPro; IPR010967; NqrE.
DR   PANTHER; PTHR30335:SF1; PTHR30335:SF1; 1.
DR   Pfam; PF02508; Rnf-Nqr; 1.
DR   PIRSF; PIRSF006102; NQR_DE; 1.
DR   TIGRFAMs; TIGR01940; nqrE; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Ion transport; Membrane; NAD; Sodium;
KW   Sodium transport; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Ubiquinone.
FT   CHAIN           1..198
FT                   /note="Na(+)-translocating NADH-quinone reductase subunit
FT                   E"
FT                   /id="PRO_1000191696"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
SQ   SEQUENCE   198 AA;  21536 MW;  E2CB18C8A5484437 CRC64;
     MEHYISLLVK SIFIENMALS FFLGMCTFLA VSKKVKTSFG LGVAVVVVLT LAVPLNNLVY
     TYLLKDGALV EGVDLSFLNF ITFIGVIAAL VQILEMVLDR FFPPLYNALG IFLPLITVNC
     AIFGGVSFMV QRDYNFTESI VYGFGSGVGW MLAIVALAGI REKMKYSDVP PGLRGLGITF
     ITVGLMALGF MSFSGVQL
 
 
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