NQRE_VIBCH
ID NQRE_VIBCH Reviewed; 198 AA.
AC Q9X4Q7;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=VC_2291;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10077658; DOI=10.1073/pnas.96.6.3183;
RA Haese C.C., Mekalanos J.J.;
RT "Effects of changes in membrane sodium flux on virulence gene expression in
RT Vibrio cholerae.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:3183-3187(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(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; AF117331; AAD29966.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF95435.1; -; Genomic_DNA.
DR PIR; C82094; C82094.
DR RefSeq; NP_231922.1; NC_002505.1.
DR RefSeq; WP_000401432.1; NZ_LT906614.1.
DR PDB; 4P6V; X-ray; 3.50 A; E=1-198.
DR PDBsum; 4P6V; -.
DR AlphaFoldDB; Q9X4Q7; -.
DR SMR; Q9X4Q7; -.
DR DIP; DIP-61341N; -.
DR IntAct; Q9X4Q7; 1.
DR STRING; 243277.VC_2291; -.
DR DNASU; 2613213; -.
DR EnsemblBacteria; AAF95435; AAF95435; VC_2291.
DR GeneID; 57740912; -.
DR KEGG; vch:VC_2291; -.
DR PATRIC; fig|243277.26.peg.2185; -.
DR eggNOG; COG2209; Bacteria.
DR HOGENOM; CLU_095255_0_0_6; -.
DR OMA; YFLGMCS; -.
DR BioCyc; MetaCyc:MON-16201; -.
DR BioCyc; VCHO:VC2291-MON; -.
DR BRENDA; 7.2.1.1; 15862.
DR Proteomes; UP000000584; 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; 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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW NAD; Reference proteome; Sodium; Sodium transport; Translocase;
KW Transmembrane; Transmembrane helix; Transport; Ubiquinone.
FT CHAIN 1..198
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT E"
FT /id="PRO_0000214259"
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"
FT HELIX 5..14
FT /evidence="ECO:0007829|PDB:4P6V"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 35..63
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 79..100
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 104..109
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 120..132
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 135..165
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 175..189
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 190..194
FT /evidence="ECO:0007829|PDB:4P6V"
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
