ID A0A0G2QXH7_SALBI Unreviewed; 507 AA. AC A0A0G2QXH7; DT 16-SEP-2015, integrated into UniProtKB/TrEMBL. DT 16-SEP-2015, sequence version 1. DT 27-SEP-2017, entry version 15. DE RecName: Full=ATP synthase subunit alpha, chloroplastic {ECO:0000256|HAMAP-Rule:MF_01346, ECO:0000256|RuleBase:RU004286}; DE EC=3.6.3.14 {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:0000313|EMBL:AIC37177.1}; OS Salicornia bigelovii (Dwarf glasswort). OG Plastid; Chloroplast {ECO:0000313|EMBL:AIC37177.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; Caryophyllales; Chenopodiaceae; Salicornioideae; OC Salicornia. OX NCBI_TaxID=46105 {ECO:0000313|EMBL:AIC37177.1}; RN [1] {ECO:0000313|EMBL:AIC37177.1} RP NUCLEOTIDE SEQUENCE. RA Ho Y.S., Khan M.S., Salazar O.R., Otto T.D., Ali S., Pain A., RA Fedoroff N.V.; RT "Complete chloroplast genomes of halophyte genus Salicornia and RT phylogenetic relationship with other plants."; RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases. 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 -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). {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; KJ629117; AIC37177.1; -; Genomic_DNA. DR RefSeq; YP_009143792.1; NC_027226.1. DR GeneID; 24571700; -. 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; 2.40.30.20; -; 1. DR HAMAP; MF_01346; ATP_synth_alpha_bact; 1. DR InterPro; IPR023366; ATP_synth_asu-like. DR InterPro; IPR000793; ATP_synth_asu_C. 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; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR42875; PTHR42875; 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; 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 ATP-binding {ECO:0000256|HAMAP-Rule:MF_01346}; KW CF(1) {ECO:0000256|HAMAP-Rule:MF_01346}; KW Chloroplast {ECO:0000256|RuleBase:RU000341, KW ECO:0000313|EMBL:AIC37177.1}; KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01346, KW ECO:0000256|RuleBase:RU000339}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01346}; KW Ion transport {ECO:0000256|HAMAP-Rule:MF_01346, KW ECO:0000256|RuleBase:RU000339}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01346}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01346}; KW Plastid {ECO:0000313|EMBL:AIC37177.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01346, KW ECO:0000256|RuleBase:RU000341}; 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 372 496 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 507 AA; 55557 MW; C588BC80418BB1EA CRC64; MATIRADEIG NIIRERIEQY SREVKVVNTG TVLQVGDGIA RIHGLDEVMA GELVEFEEGT IGIALNLESN NVGVVLMGDG LMIQEGSSVK ATGRIAQIPV SESYLGRVVN ALAKPIDGRG EISASEFRLI ESPAPGIISR RSVYEPLQTG LLAIDSMIPI GRGQRELIIG DRQTGKTAVS TDTILNQQGQ NVICVYVAIG QKASSVAQVV NNFQERGAME YTIVVAETAD SPATLQYLAP YTGAALAEYF MYRERHTLII YDDLSKQAQA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE RAAKSSSRLG EGSMTALPIV ETQAGDVSAY IPTNVISITD GQIFLSADLF NAGIRPAINV GISVSRVGSA AQIKAMKKVA GKLKLELAQF AELEAFAQFA SDLDKATQNQ LARGQRLREL LKQPQSAPLT VEEQVMTIYT GTNGYLDSLE LEQVRKYLVE LRTYVKTNKP EFQEILSSTK TFTEEAEALL KDAIQEQMER FLLQEQA //