ATPA_OENGL
ID ATPA_OENGL Reviewed; 507 AA.
AC B0Z550;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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 Oenothera glazioviana (Large-flowered evening primrose) (Oenothera
OS erythrosepala).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Myrtales; Onagraceae; Onagroideae; Onagreae; Oenothera.
OX NCBI_TaxID=482428;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Rr-lamarckiana Sweden;
RX PubMed=18299283; DOI=10.1093/nar/gkn081;
RA Greiner S., Wang X., Rauwolf U., Silber M.V., Mayer K., Meurer J.,
RA Haberer G., Herrmann R.G.;
RT "The complete nucleotide sequences of the five genetically distinct plastid
RT genomes of Oenothera, subsection Oenothera: I. Sequence evaluation and
RT plastome evolution.";
RL Nucleic Acids Res. 36:2366-2378(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, 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; EU262890; ABX10043.1; -; Genomic_DNA.
DR RefSeq; YP_001687289.1; NC_010360.2.
DR AlphaFoldDB; B0Z550; -.
DR SMR; B0Z550; -.
DR GeneID; 5955316; -.
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; Thylakoid;
KW Translocase; Transport.
FT CHAIN 1..507
FT /note="ATP synthase subunit alpha, chloroplastic"
FT /id="PRO_0000339102"
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; 55473 MW; 4FF7AAFC2F35E7CA CRC64;
MATIRADEIS NIIRERIEQY NREVKIVNTG TVLQVGDGIA RIYGLDEVMA GELVEFEEGT
IGIALNLESK NVGVVLMGDG LLIQEGSSVK ATGRIAQIPV SEAYLGRVIN ALAKPIDGRG
EISSSESRLI ESPAPGIISR RSVYEPLQTG LIAIDAMIPI GRGQRELIIG DRQTGKTAVA
TDTILNQQGN NVICVYVAIG QKASSVAQVV NALQERGAME YTIVVAEAAD SPATLQYLAP
YTGAALAEYF MYRERHTLII YDDPSKQAQA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE
RAAKLSSRLG EGSMTALPIV ETQSGDVSAY IPTNVISITD GQIFLSADLF NAGIRPAINV
GISVSRVGSA AQIKAMKQVA GKLKLELAQF AELEAFAQFS SDLDKATQNQ LARGQRLREL
LKQSQAKPLT VAEQILTIYT GTNGYLDSFE IAQVRKFLDE LRDYVKTRKP QFEEIISSTK
IFTEEAQALL KDAIQEQKEL FLVQEKV