ID A0A088CI87_9VIRI Unreviewed; 507 AA. AC A0A088CI87; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 02-OCT-2024, entry version 38. 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:AID67503.1}; OS Prasinoderma coloniale. OG Plastid; Chloroplast {ECO:0000313|EMBL:AID67503.1}. OC Eukaryota; Viridiplantae; Prasinodermophyta; Prasinodermophyceae; OC Prasinodermales; Prasinodermaceae; Prasinoderma. OX NCBI_TaxID=156133 {ECO:0000313|EMBL:AID67503.1}; RN [1] {ECO:0000313|EMBL:AID67503.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=25281016; DOI=10.1186/1471-2164-15-857; RA Lemieux C., Otis C., Turmel M.; RT "Six newly sequenced chloroplast genomes from prasinophyte green algae RT provide insights into the relationships among prasinophyte lineages and the RT diversity of streamlined genome architecture in picoplanktonic species."; RL BMC Genomics 15:857-857(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; KJ746598; AID67503.1; -; Genomic_DNA. DR RefSeq; YP_009057535.1; NC_024817.1. DR AlphaFoldDB; A0A088CI87; -. DR GeneID; 20357960; -. 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:0043531; F:ADP binding; IEA:TreeGrafter. 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_CD; 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_nt-bd_dom. 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 NCBIfam; TIGR00962; atpA; 1. DR PANTHER; PTHR48082:SF12; ATP SYNTHASE SUBUNIT ALPHA, CHLOROPLASTIC; 1. DR PANTHER; PTHR48082; 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 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:AID67503.1}; 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:AID67503.1}; 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..495 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 507 AA; 54127 MW; 3891B459E64BF32E CRC64; MVAIRPDEIS SIIRQQIEDY ASTVKVTNVG TVLQVGDGIA RVYGLNKVMA GELLEFEDGT VGIALNLEAD NVGVVLMGGG FEIQEGSSVK ATGKIAQVPV GEGFLGRVVN ALAIPVDGKG DITADETRLI ESPAPGIISR RSVYEPLQTG LVAIDAMIPI GRGQRELIIG DRQTGKTAVA IDTIINQKET GVICVYVAIG QKASSVAQIV TSLEEAGALE NTIIVAENAD SPAPLQYLAP YTGAALAEYF MYTNRHTLAI YDDLSKQAAA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE RAAKLSDALG EGSMTALPVV ETQAGDVSAY IPTNVISITD GQVFLSGDLF NSGIRPAINV GISVSRVGSA AQIKAMKQVA GTLKLELAQF AELEAFSQFA SDLDKATQNQ LARGQRLREL LKQAQGAPLS VPQQVVTIYT GINGYLDDVE VADVREFLSG LREYVGTSAS KIIDSINSSQ KFDDDAEAML LEAIATYKES FFASKKK //