ID   NUOA_BACCR              Reviewed;         122 AA.
AC   Q814W6;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=NADH-quinone oxidoreductase subunit A {ECO:0000255|HAMAP-Rule:MF_01394};
DE            EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01394};
DE   AltName: Full=NADH dehydrogenase I subunit A {ECO:0000255|HAMAP-Rule:MF_01394};
DE   AltName: Full=NDH-1 subunit A {ECO:0000255|HAMAP-Rule:MF_01394};
DE   AltName: Full=NUO1 {ECO:0000255|HAMAP-Rule:MF_01394};
GN   Name=nuoA {ECO:0000255|HAMAP-Rule:MF_01394}; OrderedLocusNames=BC_5301;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS   15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC   / NCTC 2599 / NRRL B-3711;
RX   PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA   Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA   Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA   Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT   anthracis.";
RL   Nature 423:87-91(2003).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be a
CC       menaquinone. Couples the redox reaction to proton translocation (for
CC       every two electrons transferred, four hydrogen ions are translocated
CC       across the cytoplasmic membrane), and thus conserves the redox energy
CC       in a proton gradient. {ECO:0000255|HAMAP-Rule:MF_01394}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01394};
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits NuoA, H,
CC       J, K, L, M, N constitute the membrane sector of the complex.
CC       {ECO:0000255|HAMAP-Rule:MF_01394}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01394};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01394}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01394}.
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DR   EMBL; AE016877; AAP12165.1; -; Genomic_DNA.
DR   RefSeq; NP_834964.1; NC_004722.1.
DR   RefSeq; WP_000179273.1; NZ_CP034551.1.
DR   AlphaFoldDB; Q814W6; -.
DR   SMR; Q814W6; -.
DR   STRING; 226900.BC_5301; -.
DR   EnsemblBacteria; AAP12165; AAP12165; BC_5301.
DR   GeneID; 58159516; -.
DR   GeneID; 67509928; -.
DR   KEGG; bce:BC5301; -.
DR   PATRIC; fig|226900.8.peg.5472; -.
DR   HOGENOM; CLU_119549_1_1_9; -.
DR   OMA; RFPVKYY; -.
DR   Proteomes; UP000001417; Chromosome.
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:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.58.1610; -; 1.
DR   HAMAP; MF_01394; NDH1_NuoA; 1.
DR   InterPro; IPR023043; NAD(P)H_OxRDtase_bac/plastid.
DR   InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3.
DR   InterPro; IPR038430; NDAH_ubi_oxred_su3_sf.
DR   PANTHER; PTHR11058; PTHR11058; 1.
DR   Pfam; PF00507; Oxidored_q4; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; NAD; Quinone; Reference proteome; Translocase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..122
FT                   /note="NADH-quinone oxidoreductase subunit A"
FT                   /id="PRO_0000362621"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
FT   TRANSMEM        66..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01394"
SQ   SEQUENCE   122 AA;  14038 MW;  F467129802078B5D CRC64;
     MASVYENSYM IVLIFLLLGI LLPVVALTLG RMLRPNKPSA AKATTYESGI EPFHDANIRF
     HARYYIFALL FVIFDVETLF LYPWAVAYDK LGLFALIEML IFVVMLLVGL AYAWKKKVLQ
     WL