ATPA_TRICV
ID ATPA_TRICV Reviewed; 503 AA.
AC Q00820;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=ATP synthase subunit alpha, chloroplastic {ECO:0000255|HAMAP-Rule:MF_01346};
DE EC=7.1.2.2 {ECO:0000255|HAMAP-Rule:MF_01346};
DE AltName: Full=ATP synthase F1 sector subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
DE AltName: Full=F-ATPase subunit alpha {ECO:0000255|HAMAP-Rule:MF_01346};
GN Name=atpA {ECO:0000255|HAMAP-Rule:MF_01346};
OS Trieres chinensis (Marine centric diatom) (Odontella sinensis).
OG Plastid; Chloroplast.
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; Bacillariophyta; Mediophyceae;
OC Biddulphiophycidae; Eupodiscales; Parodontellaceae; Trieres.
OX NCBI_TaxID=1514140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1532839; DOI=10.1016/0022-2836(92)91017-j;
RA Pancic P.G., Strotmann H., Kowallik K.V.;
RT "Chloroplast ATPase genes in the diatom Odontella sinensis reflect
RT cyanobacterial characters in structure and arrangement.";
RL J. Mol. Biol. 224:529-536(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Kowallik K.V., Stoebe B., Schaffran I., Kroth-Pancic P., Freier U.;
RT "The chloroplast genome of a chlorophyll a+c-containing alga, Odontella
RT sinensis.";
RL Plant Mol. Biol. Rep. 13:336-342(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39.
RX PubMed=1826484; DOI=10.1016/0014-5793(91)80338-4;
RA Pancic P.G., Strotmann H., Kowallik K.V.;
RT "The delta subunit of the chloroplast ATPase is plastid-encoded in the
RT diatom Odontella sinensis.";
RL FEBS Lett. 280:387-392(1991).
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 -!- 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:0000255|HAMAP-Rule:MF_01346};
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:0000255|HAMAP-Rule:MF_01346}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast thylakoid membrane
CC {ECO:0000255|HAMAP-Rule:MF_01346}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family.
CC {ECO:0000255|HAMAP-Rule:MF_01346}.
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DR EMBL; X60752; CAA43157.1; -; Genomic_DNA.
DR EMBL; Z67753; CAA91694.1; -; Genomic_DNA.
DR EMBL; X57701; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S78321; S78321.
DR AlphaFoldDB; Q00820; -.
DR SMR; Q00820; -.
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; 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; 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; ATP-binding; CF(1); Chloroplast; Hydrogen ion transport;
KW Ion transport; Membrane; Nucleotide-binding; Plastid; Thylakoid;
KW Translocase; Transport.
FT CHAIN 1..503
FT /note="ATP synthase subunit alpha, chloroplastic"
FT /id="PRO_0000144387"
FT BINDING 170..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
FT SITE 363
FT /note="Required for activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01346"
SQ SEQUENCE 503 AA; 54090 MW; 8636EA440225BDB5 CRC64;
MINIRPDEIS SIIREQIEQY DQDVKVDNIG TVLQVGDGIA RVYGLDQVMS GELLEFEDKT
IGIALNLEND NVGVVLMGNG RQILEGSTVK TTGQIAQIPT GEAFLGRVVN PLGAPIDGKG
DIANTETRLL EAMAPGIISR KSVCEPLQTG ITSIDAMIPI GRGQRELIIG DRQTGKTAIA
VDTIINQKTE DVVCVYVGVG QKASTVAQVV NVLEEKEAMA YTIIVCASAN DPATLQYIAP
YAGAALAEYF MYNGKATLVI YDDLTKQAMA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE
RAAKLSDALG GGSMTALPVI ETQASDVSAY IPTNVISITD GQIFLSNDLF NSGIRPAINV
GISVSRVGSA AQTKAMKQVA GKLKLELAQF AELEAFSQFA SDLDEATQKQ LARGTRLREV
LKQPQNSPLS VAEQVALIYT GINGFLDELE VASVKKYCAS LLSFLNTSNN SYIGIVSSTN
QFTAEAETAL KEAISESKAV FMK
