ID   ATPA_ACACA              Reviewed;         522 AA.
AC   Q37380;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=ATP synthase subunit alpha, mitochondrial;
GN   Name=ATP1;
OS   Acanthamoeba castellanii (Amoeba).
OG   Mitochondrion.
OC   Eukaryota; Amoebozoa; Discosea; Longamoebia; Centramoebida;
OC   Acanthamoebidae; Acanthamoeba.
OX   NCBI_TaxID=5755;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 30010 / Neff;
RX   PubMed=7844823; DOI=10.1006/jmbi.1994.0043;
RA   Burger G., Plante I., Lonergan K.M., Gray M.W.;
RT   "The mitochondrial DNA of the amoeboid protozoon, Acanthamoeba castellanii:
RT   complete sequence, gene content and genome organization.";
RL   J. Mol. Biol. 245:522-537(1995).
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; U12386; AAD11834.1; -; Genomic_DNA.
DR   PIR; S53842; S53842.
DR   RefSeq; NP_042541.1; NC_001637.1.
DR   AlphaFoldDB; Q37380; -.
DR   SMR; Q37380; -.
DR   GeneID; 1734037; -.
DR   VEuPathDB; AmoebaDB:ACA1_367940; -.
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..522
FT                   /note="ATP synthase subunit alpha, mitochondrial"
FT                   /id="PRO_0000144411"
FT   BINDING         172..179
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   522 AA;  57612 MW;  A5FAFB48FECE8CA4 CRC64;
     MKKYQFLKSN LLQNQNINEL FLQYLKNDSN IGVIKSIVDG VVIIEGLSNV KAGEMLQFSN
     DIQGMALNLN SETVSAVLFG DETKIKPGEY VEGTGNIISV PVGMSLLGRV VNALGQPIDN
     KGDFPGSELK QVEVKAPGII TRQSVNEPMI TGVKAIDCLV PVGRGQRELV IGDRQTGKTS
     ICLDAVLNQK YENSKNKKNA LYCIYTAIGQ KRSSISKLVT LLEKTNSLEY SIIVAATASE
     AAPLQYLAPY TGCVIGEYFR DNGKHALIIY DDLSKQAVAY RQMSLLLRRP PGREAYPGDI
     FYLHSRLLER AAKLNKNFGG GSLTALPVVE TQAGDVSAYI PTNVISITDG QIFLETNLFY
     NGIRPAVNVG LSVSRVGSAA QILAIKKLAG SLKLELAQYR EALSFAQFGS DLDETTKNLL
     SRGNMLTELL NQNRFTPIPI ENQFVLMYSG IKGFLTNVNN KVIRSYENEL FNRISNYSVF
     NTNVILLSNN EYYKKKNNNN VVAFFISYFK FITTNIFGFS AK