ID A0A088CI87_9CHLO Unreviewed; 507 AA. AC A0A088CI87; DT 26-NOV-2014, integrated into UniProtKB/TrEMBL. DT 26-NOV-2014, sequence version 1. DT 05-DEC-2018, entry version 22. 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; Chlorophyta; Palmophyllophyceae; OC Prasinococcales; Prasinococcaceae; 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 RT and the diversity of streamlined genome architecture in picoplanktonic RT species."; RL BMC Genomics 15:857-857(2014). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The alpha chain is a regulatory CC subunit. {ECO:0000256|HAMAP-Rule:MF_01346, CC 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; CC EC=7.1.2.2; Evidence={ECO:0000256|HAMAP-Rule:MF_01346, CC ECO:0000256|RuleBase:RU004286}; CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic CC core - and CF(0) - the membrane proton channel. CF(1) has five CC subunits: alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) CC has four main subunits: a, b, b' and c. {ECO:0000256|HAMAP- CC Rule:MF_01346, 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|HAMAP-Rule:MF_01346, 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 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: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:0015986; P:ATP synthesis coupled proton transport; IEA:UniProtKB-UniRule. DR CDD; cd01132; F1_ATPase_alpha; 1. DR Gene3D; 1.20.150.20; -; 1. DR Gene3D; 2.40.30.20; -; 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 {ECO:0000256|HAMAP-Rule:MF_01346, KW ECO:0000256|RuleBase:RU004286}; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01346, KW ECO:0000256|RuleBase:RU004286}; KW CF(1) {ECO:0000256|HAMAP-Rule:MF_01346, KW ECO:0000256|RuleBase:RU004286}; KW Chloroplast {ECO:0000256|RuleBase:RU000341, KW ECO:0000313|EMBL:AID67503.1}; KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01346, KW ECO:0000256|RuleBase:RU000339}; KW Ion transport {ECO:0000256|HAMAP-Rule:MF_01346, KW ECO:0000256|RuleBase:RU000339}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01346, KW ECO:0000256|RuleBase:RU004286}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01346, KW ECO:0000256|RuleBase:RU004286}; KW Plastid {ECO:0000256|RuleBase:RU004286, ECO:0000313|EMBL:AID67503.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01346, KW ECO:0000256|RuleBase:RU000341}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01346, KW ECO:0000256|RuleBase:RU004286}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01346, KW ECO:0000256|RuleBase:RU000339}. FT DOMAIN 28 93 ATP-synt_ab_N. {ECO:0000259|Pfam: FT PF02874}. FT DOMAIN 150 365 ATP-synt_ab. {ECO:0000259|Pfam:PF00006}. FT DOMAIN 372 495 ATP-synt_ab_C. {ECO:0000259|Pfam: FT PF00306}. FT NP_BIND 170 177 ATP. {ECO:0000256|HAMAP-Rule:MF_01346}. FT SITE 363 363 Required for activity. FT {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 //