ID G9IIX7_MILPI Unreviewed; 510 AA. AC G9IIX7; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 05-DEC-2018, entry version 40. 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:AET11349.1}; GN ORFNames=MipiCp026 {ECO:0000313|EMBL:AET11349.1}; OS Millettia pinnata (Pongame oiltree) (Cytisus pinnatus). OG Plastid; Chloroplast {ECO:0000313|EMBL:AET11349.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC 50 kb inversion clade; NPAAA clade; indigoferoid/millettioid clade; OC Millettieae; Millettia. OX NCBI_TaxID=56065 {ECO:0000313|EMBL:AET11349.1}; RN [1] {ECO:0000313|EMBL:AET11349.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=23272141; DOI=10.1371/journal.pone.0051687; RA Kazakoff S.H., Imelfort M., Edwards D., Koehorst J., Biswas B., RA Batley J., Scott P.T., Gresshoff P.M.; RT "Capturing the Biofuel Wellhead and Powerhouse: The Chloroplast and RT Mitochondrial Genomes of the Leguminous Feedstock Tree Pongamia RT pinnata."; RL PLoS ONE 7:E51687-E51687(2012). 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; JN673818; AET11349.1; -; Genomic_DNA. DR RefSeq; YP_005088812.1; NC_016708.2. DR GeneID; 11548620; -. 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:AET11349.1}; 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:AET11349.1}; 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 29 93 ATP-synt_ab_N. {ECO:0000259|Pfam: FT PF02874}. FT DOMAIN 150 365 ATP-synt_ab. {ECO:0000259|Pfam:PF00006}. FT DOMAIN 372 496 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 510 AA; 55709 MW; F01A7400C5D57E11 CRC64; MVTIRADEIS KIIRERIEQY NTEVKIVNTG TVLQVGDGIA RVYGLDEVMA GELVEFEEGT IGIALNLESK NVGVVLMGDG SMIQEGSSVK ATGRIAQIPV SEAYLGRVIN ALAKPIDGRG EISASESRLI ESPAPGIISR RSVYEPLQTG LIAIDSMIPI GRGQRELIIG DRQTGKTAVA TDTILNQQGQ NVICVYVAIG QKASSVAQVV TTLQERGAME YTIIVAETAD SPATLQYLAP YTGAALAEYF MYRELHTLII YDDLSKQAQA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE RAAKLSPQLG EGSMTALPIV ETQSGDVSAY IPTNVISITD GQIFLSADLF NAGIRPAINV GISVSRVGSA AQIKAMKQVA GKLKLELAQF AELEAFAQFA SDLDKATQNQ LARGQRLREL LKQSQSAPLT VEEQIITIYT GTNGYLDSLE IVRVKKFLVE LRAYLKTNKP QFKEIISSTK TFTGEAEAIL REAIQEEMEL FLLQDQVEKN //