ID   ATPA_ANEMR              Reviewed;         507 AA.
AC   B0YPM5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=ATP synthase subunit alpha, plastid {ECO:0000255|HAMAP-Rule:MF_01346};
DE            EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01346};
DE   AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE   AltName: Full=F-ATPase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
GN   Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346};
OS   Aneura mirabilis (Parasitic liverwort) (Cryptothallus mirabilis).
OG   Plastid; Non-photosynthetic plastid.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Jungermanniopsida; Metzgeriidae; Metzgeriales; Aneuraceae; Aneura.
OX   NCBI_TaxID=280810;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=18056074; DOI=10.1093/molbev/msm267;
RA   Wickett N.J., Zhang Y., Hansen S.K., Roper J.M., Kuehl J.V., Plock S.A.,
RA   Wolf P.G., dePamphilis C.W., Boore J.L., Goffinet B.;
RT   "Functional gene losses occur with minimal size reduction in the plastid
RT   genome of the parasitic liverwort Aneura mirabilis.";
RL   Mol. Biol. Evol. 25:393-401(2008).
CC   -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC       across the membrane. The alpha chain is a regulatory subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_01346}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate;
CC         Xref=Rhea:RHEA:57720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.1.2.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01346};
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 four main
CC       subunits: a, b, b' and c. {ECO:0000255|HAMAP-Rule:MF_01346}.
CC   -!- SUBCELLULAR LOCATION: Plastid membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000255|HAMAP-Rule:MF_01346}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000255|HAMAP-Rule:MF_01346}.
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DR   EMBL; EU043314; ABS54472.1; -; Genomic_DNA.
DR   RefSeq; YP_001687211.1; NC_010359.1.
DR   AlphaFoldDB; B0YPM5; -.
DR   SMR; B0YPM5; -.
DR   PRIDE; B0YPM5; -.
DR   GeneID; 5952151; -.
DR   GO; GO:0042170; C:plastid 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:UniProtKB-EC.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
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; Nucleotide-binding; Plastid; Translocase; Transport.
FT   CHAIN           1..507
FT                   /note="ATP synthase subunit alpha, plastid"
FT                   /id="PRO_0000339069"
FT   BINDING         170..177
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT   SITE            363
FT                   /note="Required for activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ   SEQUENCE   507 AA;  55169 MW;  22475A752E3C6F11 CRC64;
     MVNIRPDEIS NVIRTRIEQY NQEVKVVNTG TVPQVGDGIA RIYGLDKVMA GELVKFEDGT
     VGIAPNSESD NVGVVLMGDG LTIQEGSSVK ATGQIAQIPV SEAYLGRVVN ALAQPIDGKG
     KIPASESRLI ESPAPGIISR RSVYEPMQTG LIAIDSMIPI GRGQRELIIG DRQTGKTAVA
     TDTILNQKGQ DVICIYVAIG QKASSVAQVV NTFEERGALK YTIVVTENAN SPATLQYLAP
     YTGAALAEYF MYRKQHTLIV YDDLSKQAQA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE
     RAAKSNSQLG EGSMTAPPII ETQAGDVSAY IPTNVISITD GQIFLSADLF NAGIRPAINV
     GISVSRVGSA AQIRAMKQVA GKLKLELAQF AELEAFAQFA SDLDKATQNQ LARGQRLREL
     LKQSQSAPLG VEEQVATIHT GVNGYSDILE TGQVKKFLVQ LREYLPTNKP QFAEIIRSTK
     IFTEEAENIL KEAIREHSEL FSSRESK