ID A0A142EID7_9BACT Unreviewed; 449 AA.
AC A0A142EID7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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 ORFNames=AO498_00710 {ECO:0000313|EMBL:AMQ54892.1};
OS Algoriphagus sanaruensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Algoriphagus.
OX NCBI_TaxID=1727163 {ECO:0000313|EMBL:AMQ54892.1, ECO:0000313|Proteomes:UP000073816};
RN [1] {ECO:0000313|Proteomes:UP000073816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8-2 {ECO:0000313|Proteomes:UP000073816};
RA Shintani M.;
RT "Complete sequence of Algoriphagus sp. M8-2.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMQ54892.1, ECO:0000313|Proteomes:UP000073816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8-2 {ECO:0000313|EMBL:AMQ54892.1,
RC ECO:0000313|Proteomes:UP000073816};
RX PubMed=27174266;
RA Muraguchi Y., Kushimoto K., Ohtsubo Y., Suzuki T., Dohra H., Kimbara K.,
RA Shintani M.;
RT "Complete Genome Sequence of Algoriphagus sp. Strain M8-2, Isolated from a
RT Brackish Lake.";
RL Genome Announc. 4:0-0(2016).
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; CP012836; AMQ54892.1; -; Genomic_DNA.
DR RefSeq; WP_067542327.1; NZ_CP012836.1.
DR AlphaFoldDB; A0A142EID7; -.
DR STRING; 1727163.AO498_00710; -.
DR KEGG; alm:AO498_00710; -.
DR PATRIC; fig|1727163.4.peg.146; -.
DR OrthoDB; 9774536at2; -.
DR Proteomes; UP000073816; 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 Reference proteome {ECO:0000313|Proteomes:UP000073816};
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 265..313
FT /note="Na(+)-translocating NADH-quinone reductase subunit A
FT C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11973"
SQ SEQUENCE 449 AA; 48916 MW; D5C1E867F48A6CE4 CRC64;
MSKIVKLKKG FDLKLAGKAP LEHINLPAVQ TFAIKPTDFP GIQRPKVLVN EGDTVKAGTP
ILIDKAMDQV IYAAPVSGEI VEIKRGEKRK LLEIKILADQ TISYEEFGKI DLNQDRDALA
AKLASCGVWP NVIQRPFGVV ANPAETPRAI FISGFDSHPL APDFGFTLAG EENYFQAGID
ALAKLTSGKV HLSVDGSKSV PSIYSGIKNA EIHQFSGPHP AGNVGTQIHH IAPINKGELV
WTVTPIGVVQ IGKAVLEGVY DASKVIVLTG SELTKTGYVK TFVGANVSSF VKGNLNSGHV
RVISGNVLTG EKVPMEGYMG FYHNQVTVIP EGDYEEFLGW LKPSSAKLSF HKAIGMLSFL
NKGEFKVDTN THGEERPFVV TGVFEKVMPM DILPTYLFKA IISEDFDEME ELGLYELVEE
DVALCEFVDP SKNDLQGLVR NGIELLMYS
//
