ID H2F4H3_9ASPA Unreviewed; 507 AA. AC H2F4H3; DT 21-MAR-2012, integrated into UniProtKB/TrEMBL. DT 21-MAR-2012, sequence version 1. DT 11-DEC-2019, 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:AEX93556.1}; OS Xanthorrhoea preissii. OG Plastid; Chloroplast {ECO:0000313|EMBL:AEX93556.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Asphodelaceae; OC Xanthorrhoeoideae; Xanthorrhoea. OX NCBI_TaxID=470286 {ECO:0000313|EMBL:AEX93556.1}; RN [1] {ECO:0000313|EMBL:AEX93556.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=22291168; DOI=10.3732/ajb.1100491; RA Steele P.R., Hertweck K.L., Mayfield D., McKain M.R., Leebens-Mack J., RA Pires J.C.; RT "Quality and quantity of data recovered from massively parallel sequencing: RT Examples in Asparagales and Poaceae."; RL Am. J. Bot. 99:330-348(2012). RN [2] {ECO:0000313|EMBL:ATB18628.1} RP NUCLEOTIDE SEQUENCE. RA Park H., Kim C., Kim J.-H.; RT "The comparative plastid genome analysis and its phylogenetic implication RT on Asparagaceae s.l."; RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases. 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:RU004286}; CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01346, CC ECO:0000256|RuleBase:RU004286}. 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; JQ273591; AEX93556.1; -; Genomic_DNA. DR EMBL; KX822774; ATB18628.1; -; Genomic_DNA. 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, ECO:0000256|RuleBase:RU004286}; KW Chloroplast {ECO:0000256|RuleBase:RU004286, ECO:0000313|EMBL:AEX93556.1}; KW Hydrogen ion transport {ECO:0000256|HAMAP-Rule:MF_01346, KW ECO:0000256|RuleBase:RU004286}; KW Ion transport {ECO:0000256|HAMAP-Rule:MF_01346, KW ECO:0000256|RuleBase:RU004286}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_01346, 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:AEX93556.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01346, ECO:0000256|RuleBase:RU004286}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01346, KW ECO:0000256|RuleBase:RU004286}; KW Transport {ECO:0000256|HAMAP-Rule:MF_01346, ECO:0000256|RuleBase:RU004286}. FT DOMAIN 29..93 FT /note="ATP-synt_ab_N" FT /evidence="ECO:0000259|Pfam:PF02874" FT DOMAIN 150..365 FT /note="ATP-synt_ab" FT /evidence="ECO:0000259|Pfam:PF00006" FT DOMAIN 372..496 FT /note="ATP-synt_ab_C" FT /evidence="ECO:0000259|Pfam:PF00306" FT NP_BIND 170..177 FT /note="ATP" 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; 55353 MW; 704ABCED02258312 CRC64; MATLRADEIS NIIRERIEQY NREVKIVNTG TVLQVGDGIA RIHGLDEVMA GELVEFEEGT IGIALNLESN NVGVVLMGDG LMIQEGSSVK ATGRIAQIPV SEAYLSRVIN ALAKPIDGRG EISASESRLI ESPAPGIISR RSVYEPLQTG LIAIDSMIPI GRGQRELIIG DRQTGKTAVA TDTILNQKGK NVICVYVAIG QKASSVAQVV TTFQERGAME YTIVVAETAD SPATLQYLAP YTGAALAEYF MYRERHTLII YDDLSKQAQA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE RAAKSSSSLG EGSMTALPIV ETQSGDVSAY IPTNVISITD GQIFLSADLF NAGIRPAINV GISVSRVGSA AQIKAMKQVA GKLKLELAQF AELEAFAQFA SDLDKATQNQ LARGQRLREL LKQSQSDPLT VEEQIATIYT GANGYLDSLE IGQVKKFLIQ LRTYLKKNKP QFQEIISSTK TFTEQAETLL KEAIQEQSEL FLLEEQA //