NQRE_VIBC3
ID NQRE_VIBC3 Reviewed; 198 AA.
AC A5F5Y5; C3M415;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 83.
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, ECO:0000269|PubMed:11888296};
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, ECO:0000303|PubMed:11888296};
GN OrderedLocusNames=VC0395_A1880, VC395_2407;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
RN [3]
RP CATALYTIC ACTIVITY, AND SUBUNIT.
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=11888296; DOI=10.1021/bi011873o;
RA Barquera B., Hellwig P., Zhou W., Morgan J.E., Haese C.C., Gosink K.K.,
RA Nilges M., Bruesehoff P.J., Roth A., Lancaster C.R., Gennis R.B.;
RT "Purification and characterization of the recombinant Na(+)-translocating
RT NADH:quinone oxidoreductase from Vibrio cholerae.";
RL Biochemistry 41:3781-3789(2002).
RN [4]
RP SUBUNIT.
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=20558724; DOI=10.1074/jbc.m109.071126;
RA Casutt M.S., Huber T., Brunisholz R., Tao M., Fritz G., Steuber J.;
RT "Localization and function of the membrane-bound riboflavin in the Na+-
RT translocating NADH:quinone oxidoreductase (Na+-NQR) from Vibrio cholerae.";
RL J. Biol. Chem. 285:27088-27099(2010).
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, ECO:0000269|PubMed:11888296};
CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC NqrF. {ECO:0000255|HAMAP-Rule:MF_00429, ECO:0000269|PubMed:11888296,
CC ECO:0000269|PubMed:20558724}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00429, ECO:0000305}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00429}.
CC -!- SIMILARITY: Belongs to the NqrDE/RnfAE family. {ECO:0000255|HAMAP-
CC Rule:MF_00429, ECO:0000305}.
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DR EMBL; CP000627; ABQ20943.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP10397.1; -; Genomic_DNA.
DR RefSeq; WP_000401432.1; NZ_JAACZH010000008.1.
DR AlphaFoldDB; A5F5Y5; -.
DR SMR; A5F5Y5; -.
DR STRING; 345073.VC395_2407; -.
DR EnsemblBacteria; ABQ20943; ABQ20943; VC0395_A1880.
DR GeneID; 57740912; -.
DR KEGG; vco:VC0395_A1880; -.
DR KEGG; vcr:VC395_2407; -.
DR PATRIC; fig|345073.21.peg.2320; -.
DR eggNOG; COG2209; Bacteria.
DR HOGENOM; CLU_095255_0_0_6; -.
DR OMA; YFLGMCS; -.
DR Proteomes; UP000000249; Chromosome 2.
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; IDA:UniProtKB.
DR GO; GO:0022904; P:respiratory electron transport chain; IEA:InterPro.
DR GO; GO:0006814; P:sodium ion transport; IDA:UniProtKB.
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 1: Evidence at protein level;
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_1000072311"
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; 21470 MW; E7928F7E3BF339AD CRC64;
MEHYISLLVK SIFIENMALS FFLGMCTFLA VSKKVKTSFG LGIAVIVVLT ISVPVNNLVY
NLVLKPDALV EGVDLSFLNF ITFIGVIAAL VQILEMILDR FFPPLYNALG IFLPLITVNC
AIFGGVSFMV QRDYSFAESV VYGFGSGVGW MLAIVALAGI REKMKYSDVP PGLRGLGITF
ITAGLMALGF MSFSGVQL
