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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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