ID   ATPA_POPEU              Reviewed;          98 AA.
AC   P84582;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=ATP synthase subunit alpha, chloroplastic;
DE            EC=7.1.2.2;
DE   AltName: Full=ATP synthase F1 sector subunit alpha;
DE   AltName: Full=F-ATPase subunit alpha;
DE   Flags: Fragments;
GN   Name=atpA;
OS   Populus euphratica (Euphrates poplar).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Salicaceae; Saliceae; Populus.
OX   NCBI_TaxID=75702;
RN   [1]
RP   PROTEIN SEQUENCE OF 1-67 AND 75-98.
RC   TISSUE=Leaf;
RA   Ferreira S.;
RT   "Molecular analysis of Populus euphratica Oliv. response to moderate heat
RT   stress.";
RL   Thesis (2006), ICAT-FCUL, Portugal.
RN   [2]
RP   PROTEIN SEQUENCE OF 17-53 AND 68-85.
RC   TISSUE=Leaf;
RX   PubMed=16740589; DOI=10.1093/aob/mcl106;
RA   Ferreira S., Hjernoe K., Larsen M., Wingsle G., Larsen P., Fey S.,
RA   Roepstorff P., Pais M.S.;
RT   "Proteome profiling of Populus euphratica Oliv. upon heat stress.";
RL   Ann. Bot. 98:361-377(2006).
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   -!- 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|PROSITE-ProRule:PRU10106};
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC       {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC       {ECO:0000305}.
CC   -!- CAUTION: The order of the peptides shown is unknown. {ECO:0000305}.
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DR   AlphaFoldDB; P84582; -.
DR   SMR; P84582; -.
DR   GO; GO:0009535; C:chloroplast thylakoid 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.
PE   1: Evidence at protein level;
KW   ATP synthesis; ATP-binding; CF(1); Chloroplast; Direct protein sequencing;
KW   Hydrogen ion transport; Ion transport; Membrane; Nucleotide-binding;
KW   Plastid; Thylakoid; Translocase; Transport.
FT   CHAIN           <1..>98
FT                   /note="ATP synthase subunit alpha, chloroplastic"
FT                   /id="PRO_0000144390"
FT   NON_CONS        16..17
FT                   /evidence="ECO:0000305"
FT   NON_CONS        29..30
FT                   /evidence="ECO:0000305"
FT   NON_CONS        41..42
FT                   /evidence="ECO:0000305"
FT   NON_CONS        53..54
FT                   /evidence="ECO:0000305"
FT   NON_CONS        67..68
FT                   /evidence="ECO:0000305"
FT   NON_CONS        74..75
FT                   /evidence="ECO:0000305"
FT   NON_CONS        85..86
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         98
SQ   SEQUENCE   98 AA;  10621 MW;  AB396290D59E0DB5 CRC64;
     IVNTGTVLQV GDGIARIAQI PVSEAYLGRV INALAKPIDG RLIESPAPGI ISRASSVAQV
     VNALQERKFL VELRTQFQEI ISSTKLRNQA DQTITLIR