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NQRE_CHLTR
ID   NQRE_CHLTR              Reviewed;         244 AA.
AC   O84283;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 116.
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}; Synonyms=nqr5;
GN   OrderedLocusNames=CT_281;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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; AE001273; AAC67874.1; -; Genomic_DNA.
DR   PIR; F71535; F71535.
DR   RefSeq; NP_219786.1; NC_000117.1.
DR   RefSeq; WP_009871628.1; NC_000117.1.
DR   AlphaFoldDB; O84283; -.
DR   SMR; O84283; -.
DR   STRING; 813.O172_01515; -.
DR   EnsemblBacteria; AAC67874; AAC67874; CT_281.
DR   GeneID; 884844; -.
DR   KEGG; ctr:CT_281; -.
DR   PATRIC; fig|272561.5.peg.300; -.
DR   HOGENOM; CLU_095255_0_0_0; -.
DR   InParanoid; O84283; -.
DR   OMA; YFLGMCS; -.
DR   Proteomes; UP000000431; 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; IBA:GO_Central.
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;
KW   Reference proteome; Sodium; Sodium transport; Translocase; Transmembrane;
KW   Transmembrane helix; Transport; Ubiquinone.
FT   CHAIN           1..244
FT                   /note="Na(+)-translocating NADH-quinone reductase subunit
FT                   E"
FT                   /id="PRO_0000214250"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT   TRANSMEM        50..70
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        191..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00429"
FT   REGION          222..244
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   244 AA;  26438 MW;  021A5684794B1974 CRC64;
     MWLGDYSLLN LLGIFLQATF IQNILLSTFL GMCSYLACSS RLSTANGLGM SVALVLTITG
     SINWLVHYFI TKPGALAWLS PALANIDLSF LELIMFIVVI AAFTQILEVL LERFSRNLYL
     ALGIFLPLIA VNCAILGGVL FGITRNYPFL PMVVFSLGSG CGWWLAIVLF ATIREKLAYS
     DVPQHLRGTG ISFITTGLMA MAFMGLTGID ISKPTTSKPA FVTNIATDSP QPNTHSSSEE
     PKAS
 
 
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