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Database: UniProt
Entry: A0A0D2ZQE9_BRAOL
LinkDB: A0A0D2ZQE9_BRAOL
Original site: A0A0D2ZQE9_BRAOL 
ID   A0A0D2ZQE9_BRAOL        Unreviewed;       359 AA.
AC   A0A0D2ZQE9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=ATP synthase subunit alpha, mitochondrial {ECO:0000256|ARBA:ARBA00016087};
GN   Name=11271709 {ECO:0000313|EnsemblPlants:Bo00673s020.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo00673s020.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo00673s020.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TO1000 {ECO:0000313|EnsemblPlants:Bo00673s020.1};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo00673s020.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (JUN-2015) to UniProtKB.
CC   -!- FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or
CC       Complex V) produces ATP from ADP in the presence of a proton gradient
CC       across the membrane which is generated by electron transport complexes
CC       of the respiratory chain. F-type ATPases consist of two structural
CC       domains, F(1) - containing the extramembraneous catalytic core, and
CC       F(0) - containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC       in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC       the central stalk subunits to proton translocation. Subunits alpha and
CC       beta form the catalytic core in F(1). Rotation of the central stalk
CC       against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of
CC       ATP in three separate catalytic sites on the beta subunits. Subunit
CC       alpha does not bear the catalytic high-affinity ATP-binding sites.
CC       {ECO:0000256|ARBA:ARBA00037296}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC       subunits: a, b and c. {ECO:0000256|ARBA:ARBA00011648}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC       Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000256|ARBA:ARBA00008936}.
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DR   RefSeq; XP_013613736.1; XM_013758282.1.
DR   AlphaFoldDB; A0A0D2ZQE9; -.
DR   STRING; 109376.A0A0D2ZQE9; -.
DR   EnsemblPlants; Bo00673s020.1; Bo00673s020.1; Bo00673s020.
DR   GeneID; 106319879; -.
DR   Gramene; Bo00673s020.1; Bo00673s020.1; Bo00673s020.
DR   KEGG; boe:106319879; -.
DR   eggNOG; KOG1353; Eukaryota.
DR   HOGENOM; CLU_010091_0_1_1; -.
DR   OMA; HACNTHL; -.
DR   OrthoDB; 458933at2759; -.
DR   Proteomes; UP000032141; Unassembled WGS sequence.
DR   ExpressionAtlas; A0A0D2ZQE9; baseline.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:InterPro.
DR   CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR   CDD; cd01132; F1-ATPase_alpha_CD; 1.
DR   Gene3D; 1.20.150.20; ATP synthase alpha/beta chain, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR000793; ATP_synth_asu_C.
DR   InterPro; IPR038376; ATP_synth_asu_C_sf.
DR   InterPro; IPR033732; ATP_synth_F1_a_nt-bd_dom.
DR   InterPro; IPR005294; ATP_synth_F1_asu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR00962; atpA; 1.
DR   PANTHER; PTHR48082; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR48082:SF2; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF00306; ATP-synt_ab_C; 1.
DR   SUPFAM; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   CF(1) {ECO:0000256|ARBA:ARBA00023196};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00022792};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032141};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          9..227
FT                   /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT                   nucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF00006"
FT   DOMAIN          234..331
FT                   /note="ATP synthase alpha subunit C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00306"
SQ   SEQUENCE   359 AA;  39284 MW;  15F7D65E5359EC30 CRC64;
     MRTQIKVASL VPIGRGQREL LIGDRQTGKT TIAIDTILNQ KQINSRATSE SETMYCVYVA
     IGQKRSTVGQ LIQTLEEANA LEYSILVAAT ASDPAPLQFL APYSGCAMGE YFRDNGMHAL
     IIYDDLSKQA VAYRQMSLLL RRPPGREAFP GDVFYLHSRL LERAAKRSDQ TGAGSLTALP
     VIETQAGDVS AYIPTNVISI TDGQICLETE LFYRGIRPAI NVGLSVSRVG SAAQLKAMKQ
     VCGSSKLELA QYREVAAFAQ FGSDLDAATQ ALLNRGARLT EVPKQPQYAP LPIEKQILVI
     YAAVNGFCDR MPLDRISQYE KAIPNSVKPE LLQALKGGLT NERKMEPDAF LKERALALI
//
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