ID   ATPAM_MARPO             Reviewed;         513 AA.
AC   P26854;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 2.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=ATP synthase subunit alpha, mitochondrial;
GN   Name=ATPA;
OS   Marchantia polymorpha (Liverwort) (Marchantia aquatica).
OG   Mitochondrion.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=3197;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1731062; DOI=10.1016/0022-2836(92)90708-r;
RA   Oda K., Yamato K., Ohta E., Nakamura Y., Takemura M., Nozato N., Akashi K.,
RA   Kanegae T., Ogura Y., Kohchi T., Ohyama K.;
RT   "Gene organization deduced from the complete sequence of liverwort
RT   Marchantia polymorpha mitochondrial DNA. A primitive form of plant
RT   mitochondrial genome.";
RL   J. Mol. Biol. 223:1-7(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; M68929; AAC09446.1; -; Genomic_DNA.
DR   PIR; S25955; S25955.
DR   RefSeq; NP_054447.1; NC_001660.1.
DR   AlphaFoldDB; P26854; -.
DR   SMR; P26854; -.
DR   PRIDE; P26854; -.
DR   GeneID; 2702482; -.
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..513
FT                   /note="ATP synthase subunit alpha, mitochondrial"
FT                   /id="PRO_0000144401"
FT   BINDING         170..177
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   SITE            372
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   513 AA;  55441 MW;  A7314EC1FDCC70FE CRC64;
     MNKLAGAELS TLLEQRITNY YTKLQVDEIG RVVSVGDGIA RVYGLNKIQA GEMVEFASGV
     KGMALNLENE NVGIVIFGSD TAIKEGDIVK RTGSIVDVPV GKGMLGRVVD ALGVPIDGKG
     ALSAVERRRV EVKAPGIIAR KSVHEPMQTG LKAVDSLVPI GRGQRELIIG DRQTGKTAIA
     IDTILNQKQI NAQGTSDSEK LYCVYVAIGQ KRSTVAQLVK ILSEAGALEY SIIVAATASD
     PAPLQFLAPY SGCAMGEYFR DNGMHALIIY DDLSKQSVAY RQMSLLLRRP PGREAFPGDV
     FYLHSRLLER AAKMSDQTGA GSLTALPVIE TQAGDVSAYI PTNVISITDG QIFLETELFY
     RGSRPAINVG LSVSRVGSAA QLKAMKQVCG SLKLELAQYR EVAAFAQFGS DLDAATQYLL
     NRGARLTEIL KQAQYSPIPI EKQIVVIYAA VKGYLDQIPV ALITHYEQEL LKSIDPGLLS
     AIVQQKNITE QISSQLATFC QKFTQSFLAT HQS