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P56757 (ATPA_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
ATP synthase subunit alpha, chloroplastic

EC=3.6.3.14
Alternative name(s):
ATP synthase F1 sector subunit alpha
F-ATPase subunit alpha
Gene names
Name:atpA
Ordered Locus Names:AtCg00120
Encoded onPlastid; Chloroplast
OrganismArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length507 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. HAMAP MF_01346

Catalytic activity

ATP + H2O + H+(In) = ADP + phosphate + H+(Out). HAMAP MF_01346

Subunit structure

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. CF1 has five subunits: alpha3, beta3, gamma1, delta1, epsilon1. CF0 has four main subunits: a, b, b' and c By similarity.

Subcellular location

Plastidchloroplast thylakoid membrane; Peripheral membrane protein By similarity HAMAP MF_01346.

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 507507ATP synthase subunit alpha, chloroplastic HAMAP MF_01346
PRO_0000144370

Regions

Nucleotide binding170 – 1778ATP By similarity

Sites

Site3631Required for activity By similarity

Amino acid modifications

Modified residue1251Phosphoserine Ref.2

Sequences

Sequence LengthMass (Da)Tools
P56757 [UniParc].

Last modified May 30, 2000. Version 1.
Checksum: 5D48A3CAD6D645C9

FASTA50755,328
        10         20         30         40         50         60 
MVTIRADEIS NIIRERIEQY NREVTIVNTG TVLQVGDGIA RIYGLDEVMA GELVEFEEGT 

        70         80         90        100        110        120 
IGIALNLESN NVGVVLMGDG LMIQEGSSVK ATGKIAQIPV SEAYLGRVIN ALANPIDGRG 

       130        140        150        160        170        180 
KISASESRLI ESPAPGIISR RSVYEPLQTG LIAIDSMIPI GRGQRELIIG DRQTGKTAVA 

       190        200        210        220        230        240 
TDTILNQQGQ NVICVYVAIG QKASSVAQVV TSLQERGAME YTIVVAETAD SPATLQYLAP 

       250        260        270        280        290        300 
YTGAALAEYF MYREQHTLII YDDLSKQAQA YRQMSLLLRR PPGREAYPGD VFYLHSRLLE 

       310        320        330        340        350        360 
RAAKLSSQLG EGSMTALPIV ETQSGDVSAY IPTNVISITD GQIFLSADLF NAGIRPAINV 

       370        380        390        400        410        420 
GISVSRVGSA AQIKAMKQVA GKLKLELAQF AELEAFSQFS SDLDKATQNQ LARGQRLREL 

       430        440        450        460        470        480 
LKQSQSAPLT VEEQIMTIYT GTNGYLDGLE IGQVRKFLVQ LRTYLKTNKP QFQEIIASTK 

       490        500 
TLTAEAESFL KEGIQEQLER FLLQEKV 

« Hide

References

[1]"Complete structure of the chloroplast genome of Arabidopsis thaliana."
Sato S., Nakamura Y., Kaneko T., Asamizu E., Tabata S.
DNA Res. 6:283-290(1999) [PubMed: 10574454] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]"Large-scale Arabidopsis phosphoproteome profiling reveals novel chloroplast kinase substrates and phosphorylation networks."
Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A., Grossmann J., Gruissem W., Baginsky S.
Plant Physiol. 150:889-903(2009) [PubMed: 19376835] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, MASS SPECTROMETRY.
Strain: cv. Columbia.
Tissue: Seedling.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP000423 Genomic DNA. Translation: BAA84370.1.
IPIIPI00540632.
RefSeqNP_051044.1. NC_000932.1.

3D structure databases

ProteinModelPortalP56757.
SMRP56757. Positions 26-501.
ModBaseSearch...

Protein-protein interaction databases

STRINGP56757.

2D gel databases

SWISS-2DPAGEP56757.

Proteomic databases

PRIDEP56757.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsATCG00120.1; ATCG00120.1; ATCG00120.
GeneID844790.
GenomeReviewsGene locus ATCG00120 in contig AP000423_GR.
KEGGath:ArthCp007.
NMPDRfig|3702.1.peg.6.

Organism-specific databases

TAIRAtCg00120.

Phylogenomic databases

eggNOGKOG1353.
HOGENOMHBG565875.
PhylomeDBP56757.
ProtClustDBCHL00059.

Gene expression databases

GenevestigatorP56757.
GermOnlineATCG00120. Arabidopsis thaliana.

Family and domain databases

HAMAPMF_01346. ATP_synth_alpha_bact.
[Tree]
InterProIPR020003. ATPase_a/bsu_AS.
IPR005294. ATPase_F1-cplx_asu.
IPR018118. ATPase_F1/A1-cplx_a/bsu_N.
IPR023366. ATPase_F1/A1-cplx_a_su_N.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR004100. ATPase_F1/V1/A1-cplx_a/bsu_N.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
[Graphical view]
Gene3DG3DSA:2.40.30.20. G3DSA:2.40.30.20. 1 hit.
KOK02111.
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SUPFAMSSF47917. ATPase_a/b_C. 1 hit.
SSF50615. ATPase_a/b_N. 1 hit.
TIGRFAMsTIGR00962. AtpA. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameATPA_ARATH
AccessionPrimary (citable) accession number: P56757
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: November 16, 2011
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families