ATPA_TUPAK
ID ATPA_TUPAK Reviewed; 502 AA.
AC Q3ZJ00;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 83.
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 Tupiella akineta (Green alga) (Pseudendoclonium akinetum).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Chlorophyta; Ulvophyceae; OUU clade;
OC Ulotrichales; Tupiellaceae; Tupiella.
OX NCBI_TaxID=160070;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 1912;
RX PubMed=15930151; DOI=10.1093/molbev/msi182;
RA Pombert J.-F., Otis C., Lemieux C., Turmel M.;
RT "The chloroplast genome sequence of the green alga Pseudendoclonium
RT akinetum (Ulvophyceae) reveals unusual structural features and new insights
RT into the branching order of chlorophyte lineages.";
RL Mol. Biol. Evol. 22:1903-1918(2005).
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; AY835431; AAV80689.1; -; Genomic_DNA.
DR RefSeq; YP_636267.1; NC_008114.1.
DR AlphaFoldDB; Q3ZJ00; -.
DR SMR; Q3ZJ00; -.
DR PRIDE; Q3ZJ00; -.
DR GeneID; 4108761; -.
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..502
FT /note="ATP synthase subunit alpha, chloroplastic"
FT /id="PRO_0000238437"
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 502 AA; 54081 MW; 79C9601C792308C4 CRC64;
MVKIQPDEIS SIIRQQIAQY SEEVKVVNVG TVFQVGDGIA RIYGLEKVMA GELLEFEDGT
IGIALNLETK NVGAVLMGDG LAIQEGSSVR ATGKIAQIPV SESYLGRVVN SLALPIDGKG
AINSSETRLI ESLAPGIISR RSVHEPLQTG LVAVDAMIPI GRGQRELIIG DRQTGKTAIA
VDTIINQKGK DVICVYVAIG QKASSIAQVV NSLEERGCLS YTIIVAATAD TPATLQYLAP
YTGATLAEYF MYKGRHTLVI YDDLSKQAQA YREMSLLLRR PPGREAFPGD VFYLHSRLLE
RAAKLSDQLG GGSMTALPIV ETQEGDVSAY IPTNVISITD GQIFLSGDIF NSGIRPAINV
GISVSRVGSA AQPKAMKKVA GKLKLELAQF AELEAFSQFA SDLDQATQKQ LSRGSRLREL
LKQAQSSPLA LEDQVSTIYA GINGYLDGIP VENVRAFLVE LRQYLASSKP KYGQILRDTE
AFTEEAESIL KEALVELTGS KN