ID   ATPAM_RAPSA             Reviewed;         507 AA.
AC   P68541; P23413;
DT   23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=ATP synthase subunit alpha, mitochondrial;
GN   Name=ATPA;
OS   Raphanus sativus (Radish) (Raphanus raphanistrum var. sativus).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Raphanus.
OX   NCBI_TaxID=3726;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=2151720; DOI=10.1007/bf00016123;
RA   Makaroff C.A., Apel I.J., Palmer J.D.;
RT   "Characterization of radish mitochondrial atpA: influence of nuclear
RT   background on transcription of atpA-associated sequences and relationship
RT   with male sterility.";
RL   Plant Mol. Biol. 15:735-746(1990).
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   PIR; S12309; S12309.
DR   RefSeq; YP_006665997.1; NC_018551.1.
DR   AlphaFoldDB; P68541; -.
DR   SMR; P68541; -.
DR   PRIDE; P68541; -.
DR   GeneID; 13630159; -.
DR   KEGG; rsz:13630159; -.
DR   OrthoDB; 470054at2759; -.
DR   Proteomes; UP000504610; Mitochondrion MT.
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   Reference proteome; Transport.
FT   CHAIN           1..507
FT                   /note="ATP synthase subunit alpha, mitochondrial"
FT                   /id="PRO_0000144407"
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   507 AA;  55057 MW;  3E06628F9ADBCBEA CRC64;
     MELSPRAAEL TNLFESRIRN FYANFQVDEI GRVVSVGDGI AQVYGLNEIQ AGEMVLFANG
     VKGMALNLEN ENVGIVVFGG DTAIKEGDLV KRTGSIVDVP AGKAMLGRVV DAMGVPIDGR
     GALSDHEQRR VEVKAPGILE RKSVHEPMQT GLKAVDSLVP IGRGQRELLI GDRQTGKTTI
     AIDTILNQKQ INSRATSESE TMYCVYVAIG QKRSTVGQLI QTLEEANALE YSILVAATAS
     DPAPLQFLAP YSGCAMGEYF RDNGMHALII YDDLSKQAVA YRQMSLLLRR PPGREAFPGD
     VFYLHSRLLE RAAKRSDQTG AGSLTALPVI ETQAGDVSAY IPTNVISITD GQICLETELF
     YRGIRPAINV GLSVSRVGSA AQLKAMKQVC GSSKLELAQY REVAAFAQFG SDLDAATQAL
     LNRGARLTEV PKQPQYAPLP IEKQILVIYA AVNGFCDRMP LDRISQYEKA IPNSVKPELL
     QALKGGLTNE RKMEPDAFLK ERALALI