ID A0A7U1AU55_9FABA Unreviewed; 507 AA. AC A0A7U1AU55; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 14-DEC-2022, entry version 5. 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:QQY86981.1}; OS Piptanthus nepalensis. OG Plastid; Chloroplast {ECO:0000313|EMBL:QQY86981.1}. OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade; OC genistoids sensu lato; core genistoids; Sophoreae; Piptanthus. OX NCBI_TaxID=70606 {ECO:0000313|EMBL:QQY86981.1}; RN [1] {ECO:0000313|EMBL:QWW33658.1} RP NUCLEOTIDE SEQUENCE. RA Zha X.; RT "Complete chloroplast genome of Piptanthus nepalensis."; RL Submitted (DEC-2019) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:QQY86981.1} RP NUCLEOTIDE SEQUENCE. RA Yin X.; RT "Characterization of the complete chloroplast genome of Arisaema RT nepenthoides."; RL Submitted (DEC-2020) 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 -!- 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 three main CC subunits: a, b and c. {ECO:0000256|ARBA:ARBA00011648}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}. CC Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}. Plastid, CC chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_01346, CC ECO:0000256|RuleBase:RU000341}; Peripheral membrane protein CC {ECO:0000256|HAMAP-Rule:MF_01346, ECO:0000256|RuleBase:RU000341}. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {ECO:0000256|ARBA:ARBA00008936, ECO:0000256|HAMAP-Rule:MF_01346, CC 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; MW327541; QQY86981.1; -; Genomic_DNA. DR EMBL; MN841455; QWW33658.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7U1AU55; -. DR GO; GO:0009535; C:chloroplast thylakoid membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005743; C:mitochondrial inner 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 CDD; cd18113; ATP-synt_F1_alpha_C; 1. DR CDD; cd01132; F1_ATPase_alpha; 1. DR Gene3D; 1.20.150.20; -; 1. DR Gene3D; 2.40.30.20; -; 1. DR Gene3D; 3.40.50.300; -; 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; N-terminal domain of alpha and beta subunits of F1 ATP synthase; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR TIGRFAMs; TIGR00962; atpA; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. PE 3: Inferred from homology; KW ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP- KW Rule:MF_01346}; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_01346}; KW CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_01346}; KW Chloroplast {ECO:0000256|RuleBase:RU000341, ECO:0000313|EMBL:QQY86981.1}; KW Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP- KW Rule:MF_01346}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP- KW Rule:MF_01346}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01346}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_01346}; KW Plastid {ECO:0000256|RuleBase:RU004286, ECO:0000313|EMBL:QQY86981.1}; KW Thylakoid {ECO:0000256|HAMAP-Rule:MF_01346, ECO:0000256|RuleBase:RU000341}; KW Translocase {ECO:0000256|HAMAP-Rule:MF_01346, KW ECO:0000256|RuleBase:RU004286}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01346}. 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 BINDING 170..177 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" 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; 55278 MW; CF85F9766E77D232 CRC64; MVTIRADEIS KIIRERIEQY NTEVKIVNTG TVLQVGDGIA RIYGLDEVMA GELVEFEEGT IGIALNLESN NVGVVLMGDG LMIQEGSSVK ATGRIAQIPV SEAYLGRVIN ALAKPIDGRG EISASESRLI ESPAPGIISR RSVYEPLQTG LIAIDSMIPI GRGQRELIIG DRQTGKTAVA TDTILNQQGQ NVICVYVAIG QKASSVAQVV TNLQERGAME YTIVVAETAD SPATLQYLAP YTGAALAEYF MYRERHTLII YDDPSKQAQA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE RAAKSSSQLG EGSMTALPIV ETQSGDVSAY IPTNVISITD GQIFLSADLF NAGIRPAINV GISVSRVGSA AQIKAMKQVA GKLKLELAQF AELEAFAQFA SDLDKATQNQ LARGQRLREL LKQSQSAPLT VEEQIITIYT GTNGYLDSLE IGQVRKFLVE LRAYLKTNKP QFQEIISSTK TFTGEAEALL KEAIQEQIEL FLLQEQV //