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ATPA_THAPS
ID   ATPA_THAPS              Reviewed;         503 AA.
AC   A0T0P4;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
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   Thalassiosira pseudonana (Marine diatom) (Cyclotella nana).
OG   Plastid; Chloroplast.
OC   Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta;
OC   Coscinodiscophyceae; Thalassiosirophycidae; Thalassiosirales;
OC   Thalassiosiraceae; Thalassiosira.
OX   NCBI_TaxID=35128;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1335 / NEPCC58 / CCAP 1085/12;
RX   PubMed=17252281; DOI=10.1007/s00438-006-0199-4;
RA   Oudot-Le Secq M.-P., Grimwood J., Shapiro H., Armbrust E.V., Bowler C.,
RA   Green B.R.;
RT   "Chloroplast genomes of the diatoms Phaeodactylum tricornutum and
RT   Thalassiosira pseudonana: comparison with other plastid genomes of the red
RT   lineage.";
RL   Mol. Genet. Genomics 277:427-439(2007).
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; EF067921; ABK20729.1; -; Genomic_DNA.
DR   RefSeq; YP_874506.1; NC_008589.1.
DR   AlphaFoldDB; A0T0P4; -.
DR   SMR; A0T0P4; -.
DR   STRING; 35128.Thapsdraft1287; -.
DR   PRIDE; A0T0P4; -.
DR   GeneID; 4524801; -.
DR   eggNOG; KOG1353; Eukaryota.
DR   InParanoid; A0T0P4; -.
DR   OMA; MEYTIVY; -.
DR   Proteomes; UP000001449; Chloroplast.
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-UniRule.
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   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..503
FT                   /note="ATP synthase subunit alpha, chloroplastic"
FT                   /id="PRO_0000275176"
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   503 AA;  53989 MW;  4C965B0EEE5BEE96 CRC64;
     MINIRPDEIS SIIREQIEQY DQDVKIDNIG TVLQVGDGIA RVYGLDQVMS GELLEFEDKT
     IGIALNLEND NVGVVLMGNG RQILEGGSVK STGQIAQIPV GEAFLGRVVN PLGAPIDGKG
     DIASTETRLV ESMAPGIISR KSVCEPLQTG ITSIDAMIPI GRGQRELIIG DRQTGKTSIA
     VDTIINQKTE DVVCVYVGIG QKASTIAQVV NVLDEKEAMA YTIIVSASAN DPATLQYIAP
     YSGAALAEYF MYNGKATLIV YDDLTKQAMA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE
     RAAKLSDALG GGSMTALPII ETQASDVSAY IPTNVISITD GQIFLSNDLF NSGIRPAINV
     GISVSRVGSA AQTKAMKQVA GKLKLELAQF AELEAFSQFA SDLDEATQKQ LARGTRLREI
     LKQPQNSPLS VAQQVALIYA GINGFLDNLA VSDVKKFSAS LIQTLASQKS YIDVVGKTNQ
     FTEEAETLLK EAIASTKTGF ATL
 
 
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