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NQRE_CHLMU
ID   NQRE_CHLMU              Reviewed;         244 AA.
AC   Q9PKB3;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 118.
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=TC_0553;
OS   Chlamydia muridarum (strain MoPn / Nigg).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=243161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MoPn / Nigg;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF39392.1; -; Genomic_DNA.
DR   PIR; E81690; E81690.
DR   RefSeq; WP_010230822.1; NZ_CP027217.1.
DR   AlphaFoldDB; Q9PKB3; -.
DR   SMR; Q9PKB3; -.
DR   STRING; 243161.TC_0553; -.
DR   EnsemblBacteria; AAF39392; AAF39392; TC_0553.
DR   GeneID; 1245913; -.
DR   KEGG; cmu:TC_0553; -.
DR   eggNOG; COG2209; Bacteria.
DR   HOGENOM; CLU_095255_0_0_0; -.
DR   OMA; YFLGMCS; -.
DR   OrthoDB; 1814639at2; -.
DR   Proteomes; UP000000800; Chromosome.
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..244
FT                   /note="Na(+)-translocating NADH-quinone reductase subunit
FT                   E"
FT                   /id="PRO_0000214248"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT   TRANSMEM        90..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT   TRANSMEM        123..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
SQ   SEQUENCE   244 AA;  26466 MW;  F2801C64D595B323 CRC64;
     MWLGDYSLIN LLGIFLQATF IQNILLSTFL GMCSYLACSS RLSTANGLGM SVALVLTITG
     SINWLIHHFV TGPHALSWLS PALANIDLSF LELITFIVVI AAFTQILELL LERFSRNLYL
     ALGIFLPLIA VNCAILGGVL FGITRNYPFL PMVVFSLGSG CGWWLAIVLF ATIREKLAYS
     DIPQHLQGMG ISFITTGLIA MAFMGLTGID ISKPTAKSVV ISDTSTNKSK TTSAQERLSS
     NHKA
 
 
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