NQRD_VIBCH
ID NQRD_VIBCH Reviewed; 210 AA.
AC Q9X4Q6;
DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Na(+)-translocating NADH-quinone reductase subunit D {ECO:0000255|HAMAP-Rule:MF_00428};
DE Short=Na(+)-NQR subunit D {ECO:0000255|HAMAP-Rule:MF_00428};
DE Short=Na(+)-translocating NQR subunit D {ECO:0000255|HAMAP-Rule:MF_00428};
DE EC=7.2.1.1 {ECO:0000255|HAMAP-Rule:MF_00428};
DE AltName: Full=NQR complex subunit D {ECO:0000255|HAMAP-Rule:MF_00428};
DE AltName: Full=NQR-1 subunit D {ECO:0000255|HAMAP-Rule:MF_00428};
GN Name=nqrD {ECO:0000255|HAMAP-Rule:MF_00428}; OrderedLocusNames=VC_2292;
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_00428}.
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_00428};
CC -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC NqrF. {ECO:0000255|HAMAP-Rule:MF_00428}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00428}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00428}.
CC -!- SIMILARITY: Belongs to the NqrDE/RnfAE family. {ECO:0000255|HAMAP-
CC Rule:MF_00428}.
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DR EMBL; AF117331; AAD29965.1; -; Genomic_DNA.
DR EMBL; AE003852; AAF95436.1; -; Genomic_DNA.
DR PIR; D82094; D82094.
DR RefSeq; NP_231923.1; NC_002505.1.
DR RefSeq; WP_000092895.1; NZ_LT906614.1.
DR PDB; 4P6V; X-ray; 3.50 A; D=1-210.
DR PDBsum; 4P6V; -.
DR AlphaFoldDB; Q9X4Q6; -.
DR SMR; Q9X4Q6; -.
DR DIP; DIP-61340N; -.
DR IntAct; Q9X4Q6; 1.
DR STRING; 243277.VC_2292; -.
DR PRIDE; Q9X4Q6; -.
DR DNASU; 2613214; -.
DR EnsemblBacteria; AAF95436; AAF95436; VC_2292.
DR GeneID; 57740913; -.
DR KEGG; vch:VC_2292; -.
DR PATRIC; fig|243277.26.peg.2186; -.
DR eggNOG; COG1347; Bacteria.
DR HOGENOM; CLU_046659_1_1_6; -.
DR OMA; CIIMGRF; -.
DR BioCyc; MetaCyc:MON-16200; -.
DR BioCyc; VCHO:VC2292-MON; -.
DR BRENDA; 7.2.1.1; 15862.
DR Proteomes; UP000000584; Chromosome 1.
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:0006814; P:sodium ion transport; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00428; NqrD; 1.
DR InterPro; IPR011292; NqrD.
DR InterPro; IPR003667; NqrDE/RnfAE.
DR PANTHER; PTHR30586:SF1; PTHR30586:SF1; 1.
DR Pfam; PF02508; Rnf-Nqr; 1.
DR PIRSF; PIRSF006102; NQR_DE; 1.
DR TIGRFAMs; TIGR01939; nqrD; 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..210
FT /note="Na(+)-translocating NADH-quinone reductase subunit
FT D"
FT /id="PRO_0000214241"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00428"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00428"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00428"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00428"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00428"
FT HELIX 9..17
FT /evidence="ECO:0007829|PDB:4P6V"
FT TURN 21..25
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 28..34
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 38..62
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 72..89
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 98..109
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 130..155
FT /evidence="ECO:0007829|PDB:4P6V"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:4P6V"
FT HELIX 184..199
FT /evidence="ECO:0007829|PDB:4P6V"
SQ SEQUENCE 210 AA; 22837 MW; 61BF56367FCE21C6 CRC64;
MSSAKELKKS VLAPVLDNNP IALQVLGVCS ALAVTTKLET AFVMTLAVMF VTALSNFFVS
LIRNHIPNSV RIIVQMAIIA SLVIVVDQIL KAYLYDISKQ LSVFVGLIIT NCIVMGRAEA
FAMKSEPIPS FIDGIGNGLG YGFVLMTVGF FRELLGSGKL FGLEVLPLIS NGGWYQPNGL
MLLAPSAFFL IGFMIWAIRT FKPEQVEAKE
