ATPA_ADICA
ID ATPA_ADICA Reviewed; 507 AA.
AC Q85FN4;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 96.
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 Adiantum capillus-veneris (Maidenhair fern).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Polypodiopsida; Polypodiidae; Polypodiales; Pteridineae; Pteridaceae;
OC Vittarioideae; Adiantum.
OX NCBI_TaxID=13818;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12755170; DOI=10.1093/dnares/10.2.59;
RA Wolf P.G., Rowe C.A., Sinclair R.B., Hasebe M.;
RT "Complete nucleotide sequence of the chloroplast genome from a
RT leptosporangiate fern, Adiantum capillus-veneris L.";
RL DNA Res. 10:59-65(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND RNA EDITING.
RC TISSUE=Frond;
RX PubMed=15363849; DOI=10.1016/j.gene.2004.06.018;
RA Wolf P.G., Rowe C.A., Hasebe M.;
RT "High levels of RNA editing in a vascular plant chloroplast genome:
RT analysis of transcripts from the fern Adiantum capillus-veneris.";
RL Gene 339:89-97(2004).
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 -!- RNA EDITING: Modified_positions=57 {ECO:0000269|PubMed:15363849}, 66
CC {ECO:0000269|PubMed:15363849}, 68 {ECO:0000269|PubMed:15363849}, 78
CC {ECO:0000269|PubMed:15363849}, 130 {ECO:0000269|PubMed:15363849}, 186
CC {ECO:0000269|PubMed:15363849}, 294 {ECO:0000269|PubMed:15363849}, 343
CC {ECO:0000269|PubMed:15363849}, 391 {ECO:0000269|PubMed:15363849};
CC Note=The nonsense codon at position 343 is modified to a sense codon.;
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
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DR EMBL; AY178864; AAP29377.2; -; Genomic_DNA.
DR RefSeq; NP_848045.1; NC_004766.1.
DR AlphaFoldDB; Q85FN4; -.
DR SMR; Q85FN4; -.
DR GeneID; 807426; -.
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 2: Evidence at transcript level;
KW ATP synthesis; ATP-binding; CF(1); Chloroplast; Hydrogen ion transport;
KW Ion transport; Membrane; Nucleotide-binding; Plastid; RNA editing;
KW Thylakoid; Translocase; Transport.
FT CHAIN 1..507
FT /note="ATP synthase subunit alpha, chloroplastic"
FT /id="PRO_0000144367"
FT BINDING 170..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 364
FT /note="Required for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ SEQUENCE 507 AA; 55033 MW; 045EFE4A1A609477 CRC64;
MVINIQPDEI GSIIRKQIKG YVPEMKVVNI GTVLQVGDGI ARIHGLDEVM AGELVEFEDG
TVGIALNLES DNVGAVLMGD GLTIREGGSV RATGKIAQIP VSDSFLGRVV NALAQPIDGK
GQIPASEFRL IESSAPGIIS RRSVYEPLQT GLIAIDSMIP IGRGQRELII GDRQTGKTAV
ATDTILNQKG QNVICVYVAI GQKASSVAQV VDTFRERGAL EYTIVVSETA NSPATLQYLA
PYTGAALAEY FMYRKQHTLI IYDDLSKQAQ AYRQMSLLLK RPPGREAYPG DVFYLHSRLL
ERAAKLSTQL GEGSMTALPI VETQAGDVSA YIPTNVISIT DGQIFLSADL FNAGIRPAIN
VGISVSRVGS AAQIKAMKQV AGKLKLELAQ FAELEAFAQF ASDLDKTTQN QLARGQRLRE
LLKQSQSAPL AVEEQVATIY TGVNGYLDVL DVEQVKRFLV QLREYVATSK PSFGEIIRST
KVFTEQAEAL LKEAIKESTE LFLLQER
