ID A0A097KP09_9CHLO Unreviewed; 506 AA. AC A0A097KP09; DT 07-JAN-2015, integrated into UniProtKB/TrEMBL. DT 07-JAN-2015, sequence version 1. DT 22-FEB-2023, entry version 32. DE RecName: Full=ATP synthase subunit alpha, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01346, ECO:0000256|RuleBase:RU004286}; DE EC=7.1.2.2 {ECO:0000256|HAMAP-Rule:MF_01346, ECO:0000256|RuleBase:RU004286}; DE AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346}; DE AltName: Full=F-ATPase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01346}; GN Name=atpA {ECO:0000256|HAMAP-Rule:MF_01346, GN ECO:0000256|RuleBase:RU004286, ECO:0000313|EMBL:AIT94897.1}; OS Paradoxia multiseta. OG Plastid; Chloroplast {ECO:0000313|EMBL:AIT94897.1}. OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae; OC Trebouxiophyceae incertae sedis; Coccomyxaceae; Paradoxia. OX NCBI_TaxID=249350 {ECO:0000313|EMBL:AIT94897.1}; RN [1] {ECO:0000313|EMBL:AIT94897.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25270575; DOI=10.1186/s12862-014-0211-2; RA Lemieux C., Otis C., Turmel M.; RT "Chloroplast phylogenomic analysis resolves deep-level relationships within RT the green algal class Trebouxiophyceae."; RL BMC Evol. Biol. 14:211-211(2014). 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:0000256|HAMAP-Rule:MF_01346, ECO:0000256|RuleBase:RU004286}. 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:0000256|HAMAP-Rule:MF_01346, CC ECO:0000256|RuleBase:RU004286}; 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:0000256|HAMAP-Rule:MF_01346, CC ECO:0000256|RuleBase:RU004286}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane CC {ECO:0000256|HAMAP-Rule:MF_01346, ECO:0000256|RuleBase:RU000341}; CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01346, CC ECO:0000256|RuleBase:RU000341}. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_01346, CC ECO:0000256|RuleBase:RU000339}. 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; KM462879; AIT94897.1; -; Genomic_DNA. DR RefSeq; YP_009106133.1; NC_025540.1. DR AlphaFoldDB; A0A097KP09; -. DR GeneID; 22160264; -. 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; cd18116; ATP-synt_F1_alpha_N; 1. DR CDD; cd01132; F1_ATPase_alpha; 1. DR Gene3D; 2.40.30.20; -; 1. DR Gene3D; 1.20.150.20; ATP synthase alpha/beta chain, C-terminal domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR48082; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1. DR PANTHER; PTHR48082:SF2; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 1. 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; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 1. DR SUPFAM; SSF50615; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR TIGRFAMs; TIGR00962; atpA; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. PE 3: Inferred from homology; KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP- KW Rule:MF_01346}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01346}; KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_01346}; KW Chloroplast {ECO:0000256|RuleBase:RU000341, ECO:0000313|EMBL:AIT94897.1}; KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP- KW Rule:MF_01346}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP- KW Rule:MF_01346}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01346}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01346}; KW Plastid {ECO:0000256|RuleBase:RU004286, ECO:0000313|EMBL:AIT94897.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01346, ECO:0000256|RuleBase:RU000341}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01346, KW ECO:0000256|RuleBase:RU004286}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01346}. FT DOMAIN 28..93 FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N- FT terminal" FT /evidence="ECO:0000259|Pfam:PF02874" FT DOMAIN 150..365 FT /note="ATPase F1/V1/A1 complex alpha/beta subunit FT nucleotide-binding" FT /evidence="ECO:0000259|Pfam:PF00006" FT DOMAIN 372..496 FT /note="ATP synthase alpha subunit C-terminal" FT /evidence="ECO:0000259|Pfam:PF00306" FT BINDING 170..177 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01346" FT SITE 363 FT /note="Required for activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01346" SQ SEQUENCE 506 AA; 54704 MW; C0673D9C79657233 CRC64; MVKIRPDEIS SIIRQQIEQY NLEVKVVNVG TVFQVGDGIA RIYGLEKVMA GELLEFEDGT VGIALNLESK NVGAVLMGEG LTVQEGTSVR GTGKIAQIPV GEGYLGRVVN ALARPIDGKG EIPSSETRLI ESGAPGIISR RSVYEPLQTG LLAIDAMIPI GRGQRELIIG DRQTGKTAVA VDTILNQKGK GVVCVYVAIG QRASSIAQVL NTLQERGAME YTVIVAAPAD SPATLQYLAP YTGAAIAEYF MYNGRHTLAI YDDLSKQAQA YREMSLLLRR PPGREAYPGD VFYLHSRLLE RAAKLSDKLG GGSMTALPIV ETQEGDVSAY IPTNVISITD GQIFLSGDIF NAGVRPAINV GISVSRVGSA AQPKAMKKVA GKLKLELAQF AELEAFSQFA SDLDQATQNQ LARGQRLREL LKQAQASPLS VEDQVASIYA GTNGYLDKFQ VEQVRPFLIG LRQFLAARKA EYGEIIRSTN TFDDKAEKLL VEAIKEYSEE FLASAK //