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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
 
 
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