ID E3T2M4_9TRAC Unreviewed; 507 AA.
AC E3T2M4;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
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:ADE18093.1};
OS Isoetes flaccida.
OG Plastid; Chloroplast {ECO:0000313|EMBL:ADE18093.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Isoetales; Isoetaceae; Isoetes.
OX NCBI_TaxID=49763 {ECO:0000313|EMBL:ADE18093.1};
RN [1] {ECO:0000313|EMBL:ADE18093.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20969798; DOI=10.1186/1471-2148-10-321;
RA Karol K.G., Arumuganathan K., Boore J.L., Duffy A.M., Everett K.D.,
RA Hall J.D., Hansen S.K., Kuehl J.V., Mandoli D.F., Mishler B.D.,
RA Olmstead R.G., Renzaglia K.S., Wolf P.G.;
RT "Complete plastome sequences of Equisetum arvense and Isoetes flaccida:
RT implications for phylogeny and plastid genome evolution of early land plant
RT lineages.";
RL BMC Evol. Biol. 10:321-321(2010).
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|ARBA:ARBA00003784, 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; 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: Plastid membrane {ECO:0000256|ARBA:ARBA00037835};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00037835}. 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}.
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DR EMBL; GU191333; ADE18093.1; -; Genomic_DNA.
DR RefSeq; YP_004021267.1; NC_014675.1.
DR AlphaFoldDB; E3T2M4; -.
DR GeneID; 9978021; -.
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:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:UniProtKB-EC.
DR CDD; cd18113; ATP-synt_F1_alpha_C; 1.
DR CDD; cd18116; ATP-synt_F1_alpha_N; 1.
DR CDD; cd01132; F1-ATPase_alpha_CD; 1.
DR Gene3D; 2.40.30.20; -; 1.
DR Gene3D; 1.20.150.20; ATP synthase alpha/beta chain, C-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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_nt-bd_dom.
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 NCBIfam; TIGR00962; atpA; 1.
DR PANTHER; PTHR48082:SF12; ATP SYNTHASE SUBUNIT ALPHA, CHLOROPLASTIC; 1.
DR PANTHER; PTHR48082; ATP SYNTHASE SUBUNIT ALPHA, MITOCHONDRIAL; 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; SSF47917; C-terminal domain of alpha and beta subunits of F1 ATP synthase; 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 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:ADE18093.1};
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:ADE18093.1};
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 26..93
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02874"
FT DOMAIN 150..365
FT /note="ATPase F1/V1/A1 complex alpha/beta subunit
FT nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF00006"
FT DOMAIN 372..496
FT /note="ATP synthase alpha subunit C-terminal"
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; 55239 MW; E57C7E24C5A0763F CRC64;
MVNIRPDEIS SIILKQIEQY NQEVKVMNIG TVLQVGDGIA RAYGLDEVMA GELVEFEDGT
AGIALNLESD NVGVVLMGDG LAIQEGSSVK ATGKIAQIPV SDAYLGRVVN ALAQPIDGKG
QIPASEFRLI ESPAPGIISR RSVYEPMQTG LIAIDSMIPI GRGQRELIIG DRQTGKTAVA
TDTILNQKGQ NVICVYVAIG QKASSVAQVV NNFEERGAME YTIVVAETAN SPATLQYLAP
YAGAALAEYF MYRKQHTLII YDDLSKQAQA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE
RAAKLSSQLG EGSMTALPIV ETQAGDVSAY IPTNVISITD GQIFLSADLF NAGIRPAIDV
GISVSRVGSA AQIKAMKQVA GKLKLELAQF AELEAFAQFA SDLDKATQNQ LARGQRLREL
LKQSQAAPLA VEEQVATIYA GVNGYLDILE IGQVKRFLVQ LREYLITNKP QFAEIIRSTK
VFTEQAEILL KEAIKEHTEF FLLQEQK
//
