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Database: UniProt
Entry: F9REB9_VIBSN
LinkDB: F9REB9_VIBSN
Original site: F9REB9_VIBSN 
ID   F9REB9_VIBSN            Unreviewed;       446 AA.
AC   F9REB9;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=VIBRN418_12612 {ECO:0000313|EMBL:EGU32497.1};
OS   Vibrio sp. (strain N418).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=701176 {ECO:0000313|EMBL:EGU32497.1, ECO:0000313|Proteomes:UP000003627};
RN   [1] {ECO:0000313|EMBL:EGU32497.1, ECO:0000313|Proteomes:UP000003627}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N418 {ECO:0000313|EMBL:EGU32497.1,
RC   ECO:0000313|Proteomes:UP000003627};
RA   Strain E.A., Brown E., Allard M.W.;
RL   Submitted (AUG-2011) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGU32497.1}.
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DR   EMBL; AFWD01000061; EGU32497.1; -; Genomic_DNA.
DR   RefSeq; WP_005592807.1; NZ_AFWD01000061.1.
DR   AlphaFoldDB; F9REB9; -.
DR   eggNOG; COG1726; Bacteria.
DR   OMA; IKQRPYD; -.
DR   Proteomes; UP000003627; Unassembled WGS sequence.
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   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          261..309
FT                   /note="Na(+)-translocating NADH-quinone reductase subunit A
FT                   C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11973"
SQ   SEQUENCE   446 AA;  48538 MW;  09E92A6FB28B00D6 CRC64;
     MITIKKGLDL PIAGTPAQVI SDGKAIKKVA LLGEEYVGMR PTMHVRVGDE VKKAQVLFED
     KKNPGVKFTS PASGKVIEVN RGAKRVLQSV VIEVAGEEQV TFDKFEAAQL KGLDRQVIKS
     QLVESGLWTA LRTRPFSKVP AIESSTKAIF VTAMDTNPLA AQPELIINEQ QEAFIAGLEI
     LSALTEGKVY VCKSGSSLPR CSQSNVEEHV FDGPHPAGLA GTHMHFLYPV NAENVAWSIN
     YQDVIAFGQL FLTGELNVER VVSLAGPVVN KPRLIRTVVG ASLDELTDNE LMPGEVRVIS
     GSVLNGTQAA GPHAYLGRYH QQVSVLREGR EKELFGWAVP GKNKFSVTKS FLGHIFKGQL
     FNMTTTTNGS DRAMVPIGNY ERVMPLDMEP TLLLRDLCAG DTDSAQALGA LELDEEDLAL
     CTFVCPGKYE YGQLLRECLD TIVKEG
//
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