ID   NQRD_SHESM              Reviewed;         210 AA.
AC   Q0HLP8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 85.
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};
GN   OrderedLocusNames=Shewmr4_0939;
OS   Shewanella sp. (strain MR-4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=60480;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA   Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella sp. MR-4.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000446; ABI38019.1; -; Genomic_DNA.
DR   RefSeq; WP_011621733.1; NC_008321.1.
DR   AlphaFoldDB; Q0HLP8; -.
DR   SMR; Q0HLP8; -.
DR   KEGG; she:Shewmr4_0939; -.
DR   HOGENOM; CLU_046659_1_1_6; -.
DR   OMA; CIIMGRF; -.
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; 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; Sodium;
KW   Sodium transport; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Ubiquinone.
FT   CHAIN           1..210
FT                   /note="Na(+)-translocating NADH-quinone reductase subunit
FT                   D"
FT                   /id="PRO_1000060173"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00428"
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   210 AA;  22641 MW;  7A0C794BCF5B15F6 CRC64;
     MSDAKELKQV LTGPIVNNNP IALQVLGVCS ALAVTSKLET ALVMALALTA VTAFSNLFIS
     MIRNHIPSSV RIIVQMTIIA SLVIVVDQLL QAYAYQISKQ LSVFVGLIIT NCIVMGRAEA
     YAMKTPPMMS FMDGIGNGLG YGAILLAVGF VRELFGNGSL FGVQILHKIS EGGWYQPNGL
     LLLPPSAFFL IGILIWIIRT YKPEQVEAKG