ATPA_SPIOL
ID ATPA_SPIOL Reviewed; 507 AA.
AC P06450; Q9LD04;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 166.
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 Spinacia oleracea (Spinach).
OG Plastid; Chloroplast.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2443718; DOI=10.1016/0022-2836(87)90690-5;
RA Hudson G.S., Mason J.G., Holton T.A., Koller B., Cox G.B., Whitfeld P.R.,
RA Bottomley W.;
RT "A gene cluster in the spinach and pea chloroplast genomes encoding one CF1
RT and three CF0 subunits of the H+-ATP synthase complex and the ribosomal
RT protein S2.";
RL J. Mol. Biol. 196:283-298(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Geant d'hiver, and cv. Monatol;
RX PubMed=11292076; DOI=10.1023/a:1006478403810;
RA Schmitz-Linneweber C., Maier R.M., Alcaraz J.-P., Cottet A., Herrmann R.G.,
RA Mache R.;
RT "The plastid chromosome of spinach (Spinacia oleracea): complete nucleotide
RT sequence and gene organization.";
RL Plant Mol. Biol. 45:307-315(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-83.
RA Hennig J., Herrmann R.G.;
RT "Chloroplast ATP synthase of spinach contains nine nonidentical subunit
RT species, six of which are encoded by plastid chromosomes in two operons in
RT a phylogenetically conserved arrangement.";
RL Mol. Gen. Genet. 203:117-128(1986).
RN [4]
RP PROTEIN SEQUENCE OF 158-177; 221-229 AND 252-261, AND CHARACTERIZATION.
RX PubMed=1832378; DOI=10.1111/j.1432-1033.1991.tb16203.x;
RA Horbach M., Meyer H.E., Bickel-Sandkoetter S.;
RT "Inactivation of chloroplast H(+)-ATPase by modification of Lys beta 359,
RT Lys alpha 176 and Lys alpha 266.";
RL Eur. J. Biochem. 200:449-456(1991).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF 25-501 IN COMPLEX WITH BETA CHAIN.
RX PubMed=11032839; DOI=10.1074/jbc.m008015200;
RA Groth G., Pohl E.;
RT "The structure of the chloroplast F1-ATPase at 3.2 A resolution.";
RL J. Biol. Chem. 276:1345-1352(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB88710.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X03775; CAA27403.1; -; Genomic_DNA.
DR EMBL; AJ400848; CAB88710.1; ALT_INIT; Genomic_DNA.
DR PIR; S00584; PWSPA.
DR RefSeq; NP_054917.2; NC_002202.1.
DR PDB; 1FX0; X-ray; 3.20 A; A=1-507.
DR PDB; 1KMH; X-ray; 3.40 A; A=1-507.
DR PDB; 6FKF; EM; 3.10 A; A/C/E=1-507.
DR PDB; 6FKH; EM; 4.20 A; A/C/E=1-507.
DR PDB; 6FKI; EM; 4.30 A; A/C/E=1-507.
DR PDB; 6VM1; EM; 7.90 A; A/B/C=1-507.
DR PDB; 6VM4; EM; 7.08 A; A/B/C=1-507.
DR PDB; 6VMB; EM; 5.23 A; A/B/C=1-507.
DR PDB; 6VMD; EM; 4.53 A; A/B/C=1-507.
DR PDB; 6VMG; EM; 6.46 A; A/B/C=1-507.
DR PDB; 6VOF; EM; 4.51 A; A/B/C=1-507.
DR PDB; 6VOG; EM; 4.35 A; A/B/C=1-507.
DR PDB; 6VOH; EM; 4.16 A; A/B/C=1-507.
DR PDB; 6VOI; EM; 4.03 A; A/B/C=1-507.
DR PDB; 6VOJ; EM; 4.34 A; A/B/C=1-507.
DR PDB; 6VOK; EM; 3.85 A; A/B/C=1-507.
DR PDB; 6VOL; EM; 4.06 A; A/B/C=1-507.
DR PDB; 6VOM; EM; 3.60 A; A/B/C=1-507.
DR PDB; 6VON; EM; 3.35 A; A/B/C=1-507.
DR PDB; 6VOO; EM; 3.05 A; A/B/C=1-507.
DR PDBsum; 1FX0; -.
DR PDBsum; 1KMH; -.
DR PDBsum; 6FKF; -.
DR PDBsum; 6FKH; -.
DR PDBsum; 6FKI; -.
DR PDBsum; 6VM1; -.
DR PDBsum; 6VM4; -.
DR PDBsum; 6VMB; -.
DR PDBsum; 6VMD; -.
DR PDBsum; 6VMG; -.
DR PDBsum; 6VOF; -.
DR PDBsum; 6VOG; -.
DR PDBsum; 6VOH; -.
DR PDBsum; 6VOI; -.
DR PDBsum; 6VOJ; -.
DR PDBsum; 6VOK; -.
DR PDBsum; 6VOL; -.
DR PDBsum; 6VOM; -.
DR PDBsum; 6VON; -.
DR PDBsum; 6VOO; -.
DR AlphaFoldDB; P06450; -.
DR SMR; P06450; -.
DR IntAct; P06450; 8.
DR MINT; P06450; -.
DR STRING; 3562.P06450; -.
DR ChEMBL; CHEMBL2366567; -.
DR GeneID; 2715575; -.
DR KEGG; soe:2715575; -.
DR OrthoDB; 470054at2759; -.
DR EvolutionaryTrace; P06450; -.
DR PRO; PR:P06450; -.
DR Proteomes; UP000054095; Chloroplast.
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); IBA:GO_Central.
DR GO; GO:0043531; F:ADP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
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 GO; GO:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; ATP-binding; CF(1); Chloroplast;
KW Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW Nucleotide-binding; Plastid; Reference proteome; Thylakoid; Translocase;
KW Transport.
FT CHAIN 1..507
FT /note="ATP synthase subunit alpha, chloroplastic"
FT /id="PRO_0000144392"
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"
FT HELIX 6..16
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 27..36
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:1FX0"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1FX0"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:1FX0"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 176..186
FT /evidence="ECO:0007829|PDB:6FKF"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:1FX0"
FT STRAND 193..201
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 203..215
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 239..252
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 291..299
FT /evidence="ECO:0007829|PDB:6FKF"
FT TURN 307..310
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 313..321
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 330..338
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 339..345
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:6FKF"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:6FKF"
FT TURN 360..362
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 374..392
FT /evidence="ECO:0007829|PDB:6FKF"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:1FX0"
FT HELIX 397..399
FT /evidence="ECO:0007829|PDB:6FKF"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 405..420
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 431..442
FT /evidence="ECO:0007829|PDB:6FKF"
FT TURN 443..448
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 451..467
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 471..478
FT /evidence="ECO:0007829|PDB:6FKF"
FT HELIX 484..503
FT /evidence="ECO:0007829|PDB:6FKF"
SQ SEQUENCE 507 AA; 55451 MW; 97F0C73CE8B18417 CRC64;
MATIRADEIS KIIRERIEGY NREVKVVNTG TVLQVGDGIA RIHGLDEVMA GELVEFEEGT
IGIALNLESN NVGVVLMGDG LMIQEGSSVK ATGRIAQIPV SEAYLGRVIN ALAKPIDGRG
EITASESRLI ESPAPGIMSR RSVYEPLQTG LIAIDAMIPV GRGQRELIIG DRQTGKTAVA
TDTILNQQGQ NVICVYVAIG QKASSVAQVV TNFQERGAME YTIVVAETAD SPATLQYLAP
YTGAALAEYF MYRERHTLII YDDLSKQAQA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE
RAAKLSSLLG EGSMTALPIV ETQAGDVSAY IPTNVISITD GQIFLSADLF NAGIRPAINV
GISVSRVGSA AQIKAMKKVA GKLKLELAQF AELEAFAQFA SDLDKATQNQ LARGQRLREL
LKQPQSAPLT VEEQVMTIYT GTNGYLDSLE LDQVRKYLVE LRTYVKTNKP EFQEIISSTK
TFTEEAEALL KEAIQEQMER FLLQEQA
