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Database: UniProt
Entry: A0A068QQ10_9GAMM
LinkDB: A0A068QQ10_9GAMM
Original site: A0A068QQ10_9GAMM 
ID   A0A068QQ10_9GAMM        Unreviewed;       447 AA.
AC   A0A068QQ10;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Na(+)-translocating NADH-quinone reductase subunit A {ECO:0000256|HAMAP-Rule:MF_00425};
DE            Short=Na(+)-NQR subunit A {ECO:0000256|HAMAP-Rule:MF_00425};
DE            Short=Na(+)-translocating NQR subunit A {ECO:0000256|HAMAP-Rule:MF_00425};
DE            EC=7.2.1.1 {ECO:0000256|HAMAP-Rule:MF_00425};
DE   AltName: Full=NQR complex subunit A {ECO:0000256|HAMAP-Rule:MF_00425};
DE   AltName: Full=NQR-1 subunit A {ECO:0000256|HAMAP-Rule:MF_00425};
GN   Name=nqrA {ECO:0000256|HAMAP-Rule:MF_00425,
GN   ECO:0000313|EMBL:CDG16874.1};
GN   ORFNames=XDD1_1171 {ECO:0000313|EMBL:CDG16874.1};
OS   Xenorhabdus doucetiae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351671 {ECO:0000313|EMBL:CDG16874.1, ECO:0000313|Proteomes:UP000032721};
RN   [1] {ECO:0000313|EMBL:CDG16874.1, ECO:0000313|Proteomes:UP000032721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FRM16 / DSM 17909 {ECO:0000313|Proteomes:UP000032721};
RA   Genoscope - CEA;
RL   Submitted (JUL-2013) 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:0000256|HAMAP-Rule:MF_00425}.
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:0000256|HAMAP-
CC         Rule:MF_00425};
CC   -!- SUBUNIT: Composed of six subunits; NqrA, NqrB, NqrC, NqrD, NqrE and
CC       NqrF. {ECO:0000256|HAMAP-Rule:MF_00425}.
CC   -!- SIMILARITY: Belongs to the NqrA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00425}.
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DR   EMBL; FO704550; CDG16874.1; -; Genomic_DNA.
DR   RefSeq; WP_045969382.1; NZ_VNHN01000003.1.
DR   AlphaFoldDB; A0A068QQ10; -.
DR   STRING; 351671.XDD1_1171; -.
DR   KEGG; xdo:XDD1_1171; -.
DR   HOGENOM; CLU_046656_0_0_6; -.
DR   OrthoDB; 9774536at2; -.
DR   Proteomes; UP000032721; Chromosome.
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_00425; NqrA; 1.
DR   InterPro; IPR008703; NqrA.
DR   InterPro; IPR022615; NqrA_C_domain.
DR   NCBIfam; TIGR01936; nqrA; 1.
DR   PANTHER; PTHR37839; NA(+)-TRANSLOCATING NADH-QUINONE REDUCTASE SUBUNIT A; 1.
DR   PANTHER; PTHR37839:SF1; NA(+)-TRANSLOCATING NADH-QUINONE REDUCTASE SUBUNIT A; 1.
DR   Pfam; PF05896; NQRA; 1.
DR   Pfam; PF11973; NQRA_SLBB; 1.
PE   3: Inferred from homology;
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_00425};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00425};
KW   Oxidoreductase {ECO:0000313|EMBL:CDG16874.1};
KW   Sodium {ECO:0000256|ARBA:ARBA00023053, ECO:0000256|HAMAP-Rule:MF_00425};
KW   Sodium transport {ECO:0000256|ARBA:ARBA00023201, ECO:0000256|HAMAP-
KW   Rule:MF_00425};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|HAMAP-
KW   Rule:MF_00425};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00425};
KW   Ubiquinone {ECO:0000256|ARBA:ARBA00023075, ECO:0000256|HAMAP-
KW   Rule:MF_00425}.
FT   DOMAIN          262..310
FT                   /note="Na(+)-translocating NADH-quinone reductase subunit A
FT                   C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11973"
SQ   SEQUENCE   447 AA;  48802 MW;  15B633EB5FA7F0C6 CRC64;
     MIKIKKGLDL PIAGAPAQVI EDGPTICHVA LLGEEYVGMR PSMLVKEGEH VKKGQMLFED
     KKNPGVVFTS PASGKVITIG RGERRVLQSV VIEVSGDEKV TFDRYEHAEL AGLSREQVEK
     NLLASGLWTA LRTRPFSRSP APGSTPKAIF VTAMDTQPLA ADPLVVIATQ EEAFVDGLNV
     LSKLTEGKIH VCHGAGTIPT AGNNAQITYN QFVGPHPAGL VGTHIHFIEP VSAQKMVWHL
     GYQDVIAIGK LFTTGELYTD RVVSLAGPQV KSPRLVRTRL GADLLELTQN QLKEGENRIV
     SGSVLYGMRS DDARHYLGRF HTLVSVLAEG REKELFGWIA PGVNKFSITR TTIGHFLKKK
     RFAFSTTTHG GERSMVPIGN YERVMPLDIM ATHLLRDLLA GDSDSAQALG CLELDEEDLA
     LCTYVCPGKY EYGPVLRDVL TKIEQEG
//
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