ID G3XHF0_SCIVE Unreviewed; 507 AA.
AC G3XHF0;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
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:BAK86697.1};
OS Sciadopitys verticillata (Japanese umbrella-pine) (Taxus verticillata).
OG Plastid; Chloroplast {ECO:0000313|EMBL:BAK86697.1}.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers II; Cupressales;
OC Sciadopityaceae; Sciadopitys.
OX NCBI_TaxID=28979 {ECO:0000313|EMBL:BAK86697.1};
RN [1] {ECO:0000313|EMBL:BAK86697.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21933779; DOI=10.1093/gbe/evr095;
RA Wu C.-S., Wang Y.-N., Hsu C.-Y., Lin C.-P., Chaw S.-M.;
RT "Loss of different inverted repeat copies from the chloroplast genomes of
RT Pinaceae and cupressophytes and influence of heterotachy on the evaluation
RT of gymnosperm phylogeny.";
RL Genome Biol. Evol. 3:1284-1295(2011).
RN [2] {ECO:0000313|EMBL:BAK86697.1}
RP NUCLEOTIDE SEQUENCE.
RA Hsu CY., Chaw SM., Wu CS.;
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:BAW34619.1}
RP NUCLEOTIDE SEQUENCE.
RA Zhang Y., Guo Z.;
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:BAW34619.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=27269365; DOI=10.1093/gbe/evw109;
RA Hsu C.-Y., Wu C.-S., Chaw S.-M.;
RT "Birth of Four Chimeric Plastid Gene Clusters in Japanese Umbrella Pine.";
RL Genome Biol. Evol. 8:1776-1784(2016).
RN [5] {ECO:0000313|EMBL:AMO00698.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=26865528;
RA Li J., Gao L., Chen S., Tao K., Su Y., Wang T.;
RT "Evolution of short inverted repeat in cupressophytes, transfer of accD to
RT nucleus in Sciadopitys verticillata and phylogenetic position of
RT Sciadopityaceae.";
RL Sci. Rep. 6:20934-20934(2016).
RN [6] {ECO:0000313|EMBL:BCK60789.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Chaw 1497 {ECO:0000313|EMBL:BCK60789.1};
RA Wu C.S., Sudianto E., Chaw S.M.;
RT "Tight association of genome rearrangements with gene expression in conifer
RT plastomes.";
RL BMC Plant Biol. 0:0-0(2020).
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}.
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; KT601210; AMO00698.1; -; Genomic_DNA.
DR EMBL; AB645770; BAK86697.1; -; Genomic_DNA.
DR EMBL; AP017299; BAW34619.1; -; Genomic_DNA.
DR EMBL; LC572147; BCK60789.1; -; Genomic_DNA.
DR RefSeq; YP_009240200.1; NC_029734.1.
DR AlphaFoldDB; G3XHF0; -.
DR GeneID; 27109666; -.
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:BAK86697.1};
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:BAK86697.1};
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; 55384 MW; 1A2BE93B6EB38D62 CRC64;
MVTIRPDEIS SMIRKQIQQY NNEVEVANIG TVVQVGDGIA RIHGLDQVMA GELVEFLDGT
IGIALNLESD NVGAVLMGDG STIQEGSSVR ATGKIAQIPV SDAYLGRVVN ALARPIDGKG
KITASEFRLI ESPAPGIISR RSVYEPLQTG LIAIDSMIPI GRGQRELIIG DRQTGKTAVA
TDTIINQKDQ NVICVYVAIG QKASSVAQVV NTFRECGAME YTIVVVETAD SPATLQYLAP
YTGAALAEYF MYKEQHTLII YDDLSKQAQA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE
RAAKLSSQLG EGSLTALPIV ETQAGDVSAY IPTNVISITD GQIFLSADLF NAGIQPAINV
GLSVSRVGSA AQMKAMKQVA GKLKLELAQL AELEAFAQFA SDLDKTTQNQ LGRGQRLREL
LKQSQASPLT VEEQIAMIYT GTNGYLSVLN IPQVRKFLDQ LRDYLKKKTP QFGEIIRSTR
TFTEQAEVLL KEAIQENIEL FLLREKK
//
