ID A0A218LNM5_PSAJU Unreviewed; 504 AA. AC A0A218LNM5; DT 27-SEP-2017, integrated into UniProtKB/TrEMBL. DT 27-SEP-2017, sequence version 1. DT 05-DEC-2018, entry version 6. 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:ASD42870.1}; OS Psathyrostachys juncea (Russian wildrye). OG Plastid; Chloroplast {ECO:0000313|EMBL:ASD42870.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade; OC Pooideae; Triticodae; Triticeae; Hordeinae; Psathyrostachys. OX NCBI_TaxID=4586 {ECO:0000313|EMBL:ASD42870.1}; RN [1] {ECO:0000313|EMBL:ASD42870.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=28622761; DOI=.1186/s12862-017-0989-9; RA Bernhardt N., Brassac J., Kilian B., Blattner F.R.; RT "Dated tribe-wide whole chloroplast genome phylogeny indicates RT recurrent hybridizations within Triticeae."; RL BMC Evol. Biol. 17:141-141(2017). 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; KY636111; ASD42870.1; -; 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 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:ASD42870.1}; 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:ASD42870.1}; 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 27 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 504 AA; 55405 MW; 4C767590F516B808 CRC64; MATLRVDEIH KILRERIEQY NRKVGIENIG RVVQVGDGIA RIIGLGEIMS GELVEFAEGT RGIALNLESK NVGIVLMGDG LMIQEGSFVK ATGRIAQIPV SEAYLGRVVN ALAKPIDGKG EILASESRLI ESPAPSIISR RSVYEPLQTG LIAIDSMIPI GRGQRELIIG DRQTGKTAVA TDTILNQKGQ GVICVYVAIG QRASSVAQVV TTFHEEGAME YTIVVAEMAD SPATLQYLAP YTGAALAEYF MYRERHTLII YDDLSKQAQA YRQMSLLLRR PPGRXXXXGD VFYLHSRLLE RAAKLNSLLG EGSMTALPIV EXXXXXXXXX XXXXXISITD GQIFLSADLF NAGIRPAINV GISVSRVGSA AQIKAMKQVA GKSKLELAQF AELQAFAQFA SALDKTSQNQ LARGRRLREL LKQSQANPLP VEEQIATIYT GTRGYLDSLE IEQVNKFLDE LRKHLKDTKP QFQEIISSSK TFTEQAEILL KEAIQEQLER FSLQ //