ATPA_ANTAG
ID ATPA_ANTAG Reviewed; 507 AA.
AC Q85AU2;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 101.
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 Anthoceros angustus (Hornwort) (Anthoceros formosae).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Anthocerotophyta;
OC Anthocerotopsida; Anthocerotidae; Anthocerotales; Anthocerotaceae;
OC Anthoceros.
OX NCBI_TaxID=48387;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND RNA EDITING.
RX PubMed=12527781; DOI=10.1093/nar/gkg155;
RA Kugita M., Kaneko A., Yamamoto Y., Takeya Y., Matsumoto T., Yoshinaga K.;
RT "The complete nucleotide sequence of the hornwort (Anthoceros formosae)
RT chloroplast genome: insight into the earliest land plants.";
RL Nucleic Acids Res. 31:716-721(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND RNA EDITING.
RC TISSUE=Thallus;
RX PubMed=12711687; DOI=10.1093/nar/gkg327;
RA Kugita M., Yamamoto Y., Fujikawa T., Matsumoto T., Yoshinaga K.;
RT "RNA editing in hornwort chloroplasts makes more than half the genes
RT functional.";
RL Nucleic Acids Res. 31:2417-2423(2003).
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=22 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 41 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 56 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 76 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 105 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 107 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 109 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 135 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 146 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 160 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 162 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 246 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 250 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 258 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 267 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 269 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 331 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 350 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 378 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 383 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 425 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 446 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 453 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 494 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}, 502 {ECO:0000269|PubMed:12527781,
CC ECO:0000269|PubMed:12711687}; Note=The nonsense codons at positions 22,
CC 267, 269, 378, 425 and 453 are modified to sense codons.;
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
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DR EMBL; AB086179; BAC55333.1; -; Genomic_DNA.
DR EMBL; AB087425; BAC55424.1; -; mRNA.
DR RefSeq; NP_777397.1; NC_004543.1.
DR AlphaFoldDB; Q85AU2; -.
DR SMR; Q85AU2; -.
DR PRIDE; Q85AU2; -.
DR GeneID; 2553480; -.
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_0000144368"
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; 55543 MW; AFB6C6CCE1BAA42F CRC64;
MVNIRPDEIS NIIRKQIEQY NQEVKVINIG TVLQVGDGIA RIYGLDKVMA GELVEFEDGT
VGIALNLESD NVGVVLMGDG LSIQEGSSVE ATGKIAQIPV SDAYLGRVVN ALAQPIDGKG
QIPAYEFRLI ESPAPGIISR RSVYEPMQTG LIAIDSMIPI GRGQRELIIG DRQTGKTAVA
TDTILNQKGQ NVICVYVAIG QKASSVAQVV NTFEERGALE YTIVVAETAD SPATLQYLAP
YTGAALAEYF MYRKQHTLII YDDLSKQAQA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE
RAAKLSSQLG EGSMTALPIV ETQAGDVSAY IPTNVISITD GQIFLSADLF NAGIRPAINV
GISVSRVGSA AQIKAMKQVA GKLKLELAQF AELEAFAQFA SDLDKATQNQ LARGQRLREL
LKQSQSAPLA VEEQVATIYT GVNGYLDVLE VEQVKKFLVQ LREYLITNKP QFVEIIRSTK
VFTEQAEIIL KEAIKEHTEF FLLQEQK
