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ATPA_WHEAT
ID   ATPA_WHEAT              Reviewed;         504 AA.
AC   P12112;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   26-SEP-2001, sequence version 2.
DT   03-AUG-2022, entry version 151.
DE   RecName: Full=ATP synthase subunit alpha, chloroplastic {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   Triticum aestivum (Wheat).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   AGRICOLA=IND85057686; DOI=10.1007/BF02418255;
RA   Howe C.J., Fearnley I.M., Walker J.E., Dyer T.A., Gray J.C.;
RT   "Nucleotide sequences of the genes for the alpha, beta and epsilon subunits
RT   of wheat chloroplast ATP synthase.";
RL   Plant Mol. Biol. 4:333-345(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Chinese Spring;
RA   Ogihara Y., Isono K., Kojima T., Endo A., Hanaoka M., Shiina T.,
RA   Terachi T., Utsugi S., Murata M., Mori N., Takumi S., Ikeo K., Gojobori T.,
RA   Murai R., Murai K., Matsuoka Y., Ohnishi Y., Tajiri H., Tsunewaki K.;
RT   "Chinese spring wheat (Triticum aestivum L.) chloroplast genome: complete
RT   sequence and contig clones.";
RL   Plant Mol. Biol. Rep. 18:243-253(2000).
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, chloroplast thylakoid membrane
CC       {ECO:0000255|HAMAP-Rule:MF_01346}; Peripheral membrane protein
CC       {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; M16842; AAA84725.1; -; Genomic_DNA.
DR   EMBL; AB042240; BAB47031.1; -; Genomic_DNA.
DR   PIR; S09351; PWWTA.
DR   RefSeq; NP_114256.1; NC_002762.1.
DR   AlphaFoldDB; P12112; -.
DR   SMR; P12112; -.
DR   STRING; 4565.EPlTAEP00000010058; -.
DR   PRIDE; P12112; -.
DR   GeneID; 803205; -.
DR   KEGG; taes:803205; -.
DR   eggNOG; KOG1353; Eukaryota.
DR   HOGENOM; CLU_010091_2_1_1; -.
DR   Proteomes; UP000019116; Chloroplast.
DR   ExpressionAtlas; P12112; baseline.
DR   Genevisible; P12112; TA.
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); IBA:GO_Central.
DR   GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR   GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
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); Chloroplast; Hydrogen ion transport;
KW   Ion transport; Membrane; Nucleotide-binding; Plastid; Reference proteome;
KW   Thylakoid; Translocase; Transport.
FT   CHAIN           1..504
FT                   /note="ATP synthase subunit alpha, chloroplastic"
FT                   /id="PRO_0000144394"
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"
FT   CONFLICT        13
FT                   /note="L -> V (in Ref. 1; AAA84725)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        16
FT                   /note="R -> L (in Ref. 1; AAA84725)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        96
FT                   /note="A -> P (in Ref. 1; AAA84725)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   504 AA;  55296 MW;  6B3A5726BF0DC806 CRC64;
     MATLRVDEIH KILRERIEQY NRKVGIENIG RVVQVGDGIA RIIGLGEIMS GELVEFAEGT
     RGIALNLESK NVGIVLMGDG LMIQEGSFVK ATGRIAQIPV SEAYLGRVVN ALAKPIDGKG
     EIIASESRLI ESPAPSIISR RSVYEPLQTG LIAIDSMIPI GRGQRELIIG DRQTGKTAVA
     TDTILNQKGQ GVICVYVAIG QRASSVAQVV TTFHEEGAME YTIVVAEMAD SPATLQYLAP
     YTGAALAEYF MYRERHTLII YDDLSKQAQA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE
     RAAKLNSLLG EGSMTALPIV ETQSGDVSAY IPTNVISITD GQIFLSADLF NAGIRPAINV
     GISVSRVGSA AQIKAMKQVA GKSKLELAQF AELQAFAQFA SALDKTSQNQ LARGRRLREL
     LKQSQANPLP VEEQIATIYT GTRGYLDSLE IEQVNKFLDE LRKHLKDTKP QFQEIISSSK
     TFTEQAEILL KEAIQEQLER FSLQ
 
 
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