ID   ATPA_DICCI              Reviewed;         519 AA.
AC   Q2LCQ7;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=ATP synthase subunit alpha, mitochondrial;
GN   Name=atp1;
OS   Dictyostelium citrinum (Slime mold).
OG   Mitochondrion.
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=361072;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18413355; DOI=10.1093/molbev/msn088;
RA   Heidel A.J., Gloeckner G.;
RT   "Mitochondrial genome evolution in the social amoebae.";
RL   Mol. Biol. Evol. 25:1440-1450(2008).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
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DR   EMBL; DQ336395; ABC60386.1; -; Genomic_DNA.
DR   RefSeq; YP_492635.1; NC_007787.2.
DR   AlphaFoldDB; Q2LCQ7; -.
DR   SMR; Q2LCQ7; -.
DR   PRIDE; Q2LCQ7; -.
DR   GeneID; 3912628; -.
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   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..519
FT                   /note="ATP synthase subunit alpha, mitochondrial"
FT                   /id="PRO_0000312384"
FT   BINDING         188..195
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            382
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   519 AA;  57261 MW;  9FBA4213175AEB5B CRC64;
     MQLERILTET NIERSKFKQY KVLSKYINAV AKKYTLNNVS NKYGKVLFIK DGVVKVSGLS
     QIKIGEKVEF VGKNLFGMAL NLEATSVGIV IFGEDTAIYE GVIVKRCEQN FAIKVDKTML
     GRVVDVLGQP IDGLGELKDT KTTRVMSVER KAPGIVTRKS VHESMLTGVK MVDALLPIGR
     GQRELIIGDR QTGKSAIAVD AILNQQVNKD IVCIYVAVGQ KKSTVRRLVE MLNTKGALEY
     TIVVVSTASD AAPLQFLAPY TGCTIGEYFR DEGKHALIVY DDLSKHAVAY RQMSLLLRRP
     PGREAYPGDV FYIHSRLLER AAKLNEKYGC GSLTAFPIVE TQAGDVSAYI PTNIISITDG
     QIFLEKELFN KGIRPAVNVG LSVSRVGSAA QSAVMKKLAG ALKLELAQYR ELARFEQFSS
     NADAVTTQIL KKGKLTIELL KQVNNNPMAV GMEALMIFAM STSYFQNLDL SLVRAEEAKL
     LQYIHSVSSF KLYAACVDAV KAFNPKDTVF TEMCQSYVK