ID   NQRD_NEIMB              Reviewed;         208 AA.
AC   Q9K0M6;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 113.
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=NMB0566;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(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}.
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; AE002098; AAF40994.1; -; Genomic_DNA.
DR   PIR; A81185; A81185.
DR   RefSeq; NP_273610.1; NC_003112.2.
DR   RefSeq; WP_002221365.1; NC_003112.2.
DR   AlphaFoldDB; Q9K0M6; -.
DR   SMR; Q9K0M6; -.
DR   STRING; 122586.NMB0566; -.
DR   PaxDb; Q9K0M6; -.
DR   EnsemblBacteria; AAF40994; AAF40994; NMB0566.
DR   KEGG; nme:NMB0566; -.
DR   PATRIC; fig|122586.8.peg.725; -.
DR   HOGENOM; CLU_046659_1_1_4; -.
DR   OMA; CIIMGRF; -.
DR   Proteomes; UP000000425; Chromosome.
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   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..208
FT                   /note="Na(+)-translocating NADH-quinone reductase subunit
FT                   D"
FT                   /id="PRO_0000214236"
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"
SQ   SEQUENCE   208 AA;  22682 MW;  009FA36C9030C11C CRC64;
     MADMKRLKHL MFSPFIDNNP IALQVLGICS ALAVTTKLQT AIVMGISVAL VTGFSSFFIS
     LVRNYIPNSI RIIVQMAIIA SLVTLVDQLL QAFAYELSKQ LSVFVGLIIT NCIVMGRAEA
     FAMKEPPLES LIDGIGNGAG YGIMLLVVAT VRELIGSGKL LGYTVFQTVQ DGGWYQTNGL
     FLLAPSAFFI IGFLIWGLRT WKPEQAEE