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P27179 (ATPA_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ATP synthase subunit alpha

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:sll1326
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesSynechocystis

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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: a1, b1, b'1 and c(9-12) By similarity.

Subcellular location

Cellular 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 – 503503ATP synthase subunit alpha HAMAP MF_01346
PRO_0000144362

Regions

Nucleotide binding170 – 1778ATP By similarity

Sites

Site3631Required for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P27179 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 98738E1339E0ABE5

FASTA50353,966
        10         20         30         40         50         60 
MVSIRPDEIS SIIRQQIESY DQSVQVSNVG TVLQVGDGTA RIYGLEQVMS QELLEFEDGT 

        70         80         90        100        110        120 
IGIALNLEED NVGAVLMGDG FGIQEGSTVK TTGQIAQIPI GDAMVGRVVD SLGRPIDGKG 

       130        140        150        160        170        180 
PISSTATRLL ESPAPGIIER KSVCEPMQTG ITAIDAMIPI GRGQRELIIG DRKTGKTAIA 

       190        200        210        220        230        240 
IDTIINQKSE DVICVYVAIG QKASTVAQII DTLTEKGAMA YTIVVAANAN DPATLQYLAP 

       250        260        270        280        290        300 
YTGATLAEHF MYQGKSTLVI YDDLSKQAQA YRQMSLLMRR PPGREAYPGD VFYIHSRLLE 

       310        320        330        340        350        360 
RAAKLSDALG GGSMTALPVI ETQAGDVSAY IPTNVISITD GQIFLSTDLF NAGFRPAINA 

       370        380        390        400        410        420 
GISVSRVGSA AQTKAMKKVA GKLKLELAQF AELEAFSQFA SDLDAATQAQ LARGQRLRQL 

       430        440        450        460        470        480 
LKQPENSPLS VWEQVAISYA GLNGYIDTIP VDKVTEFAQG LRDYLKANKA KYVEIINSSK 

       490        500 
ALTDEAETLL KEGIKEFTQG FAA 

« Hide

References

« Hide 'large scale' references
[1]"The atp1 and atp2 operons of the cyanobacterium Synechocystis sp. PCC 6803."
Lill H., Nelson N.
Plant Mol. Biol. 17:641-652(1991) [PubMed: 1832989] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27184 / PCC 6803 / N-1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58128 Genomic DNA. Translation: CAA41135.1.
BA000022 Genomic DNA. Translation: BAA16735.1.
PIRPWYBA. S17751.
RefSeqNP_440055.1. NC_000911.1.

3D structure databases

ProteinModelPortalP27179.
SMRP27179. Positions 25-501.
ModBaseSearch...

Protein-protein interaction databases

IntActP27179. 7 interactions.
STRINGP27179.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID953354.
GenomeReviewsGene locus sll1326 in contig BA000022_GR.
KEGGsyn:sll1326.
NMPDRfig|1148.1.peg.156.
PATRIC23837190. VBISynSp132158_0170.

Phylogenomic databases

eggNOGCOG0056.
HOGENOMHBG565875.
OMAGSDRDIK.
PhylomeDBP27179.
ProtClustDBPRK09281.

Enzyme and pathway databases

BioCycSSP1148:SLL1326-MONOMER.

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_SYNY3
AccessionPrimary (citable) accession number: P27179
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: January 25, 2012
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

SIMILARITY comments

Index of protein domains and families