ID   ATPAM_PHAVU             Reviewed;         508 AA.
AC   P24459;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=ATP synthase subunit alpha, mitochondrial;
GN   Name=ATPA;
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1423717; DOI=10.1007/bf00351475;
RA   Chase C.D., Ortaga V.M.;
RT   "Organization of ATPA coding and 3' flanking sequences associated with
RT   cytoplasmic male sterility in Phaseolus vulgaris L.";
RL   Curr. Genet. 22:147-153(1992).
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 (By
CC       similarity). {ECO:0000250}.
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane.
CC       Note=Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; M64246; AAB01582.1; -; Genomic_DNA.
DR   PIR; S26979; S26979.
DR   AlphaFoldDB; P24459; -.
DR   SMR; P24459; -.
DR   PRIDE; P24459; -.
DR   ProMEX; P24459; -.
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; 1.
DR   Gene3D; 1.20.150.20; -; 1.
DR   Gene3D; 2.40.30.20; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_01346; ATP_synth_alpha_bact; 1.
DR   InterPro; IPR023366; ATP_synth_asu-like_sf.
DR   InterPro; IPR000793; ATP_synth_asu_C.
DR   InterPro; IPR038376; ATP_synth_asu_C_sf.
DR   InterPro; IPR033732; ATP_synth_F1_a.
DR   InterPro; IPR005294; ATP_synth_F1_asu.
DR   InterPro; IPR020003; ATPase_a/bsu_AS.
DR   InterPro; IPR004100; ATPase_F1/V1/A1_a/bsu_N.
DR   InterPro; IPR036121; ATPase_F1/V1/A1_a/bsu_N_sf.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF00306; ATP-synt_ab_C; 1.
DR   Pfam; PF02874; ATP-synt_ab_N; 1.
DR   PIRSF; PIRSF039088; F_ATPase_subunit_alpha; 1.
DR   SUPFAM; SSF50615; SSF50615; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00962; atpA; 1.
DR   PROSITE; PS00152; ATPASE_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; ATP-binding; CF(1); Hydrogen ion transport; Ion transport;
KW   Membrane; Mitochondrion; Mitochondrion inner membrane; Nucleotide-binding;
KW   Transport.
FT   CHAIN           1..508
FT                   /note="ATP synthase subunit alpha, mitochondrial"
FT                   /id="PRO_0000144405"
FT   BINDING         171..178
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            373
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   508 AA;  55345 MW;  2198F396EE8C0A79 CRC64;
     MEFSSRAAEL TTLLESRMTN FYTNFQVDEI GRVVSVGDGI ARVYGLNEIQ AGEMVEFASG
     VKGIALNLEN ENVGIVVFGS DTAIKEGDLV KRTGSIVDVP AGKAMLGRVV DALGVPIDGR
     GALSDHERRR VEVKAPGIIE RKSVHEPMQT GLKAVDSLVP IGRGQRELII GDRQTGKTAI
     AIDTILNQKQ MNSRATSESE TLYCVYVAIG QKRSTVAQLV QILSEANALE YSILVAATAS
     DPAPLQFLAP YSGCAMGEYF RDNGMHALII YDDLSKQAVA YRQMSLLLRR PPGREAFPGD
     VFYLHSRLLE RAAKRSDQTG AGSLTALPVI ETQAGDVSAY IPTNVISITD GQICLETELF
     YRGIRPAINV GLSVSRVGSA AQLKAMKQAC GSLKLELAQY REVAAFAQFG SDLDAATQAL
     LNRGARLTEV LKQPQYAPLP IEKQILVIYA AVNGFCDRMP LDKIPQYERD ILTTIKPELL
     QSLKGGLTSE RKIELEKFLK EKAKNYTL