Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P07251 (ATPA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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, mitochondrial
Gene names
Name:ATP1
Ordered Locus Names:YBL099W
ORF Names:YBL0827
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length545 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F1. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites By similarity. HAMAP-Rule 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 three main subunits: a, b and c.

Subcellular location

Mitochondrion inner membrane. Note: Peripheral membrane protein. Ref.7

Miscellaneous

Present with 41500 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the ATPase alpha/beta chains family.

Ontologies

Keywords
   Biological processATP synthesis
Hydrogen ion transport
Ion transport
Transport
   Cellular componentCF(1)
Membrane
Mitochondrion
Mitochondrion inner membrane
   DomainTransit peptide
   LigandATP-binding
Nucleotide-binding
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay PubMed 15294286PubMed 18722382. Source: GOC

ATP hydrolysis coupled proton transport

Inferred from electronic annotation. Source: InterPro

ATP synthesis coupled proton transport

Inferred from direct assay PubMed 20691145. Source: SGD

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

mitochondrial intermembrane space

Traceable author statement. Source: Reactome

mitochondrial nucleoid

Inferred from direct assay PubMed 10869431. Source: SGD

mitochondrial proton-transporting ATP synthase, catalytic core

Inferred from direct assay PubMed 17082766. Source: SGD

mitochondrion

Inferred from direct assay Ref.7. Source: SGD

proton-transporting ATP synthase complex, catalytic core F(1)

Inferred from direct assay PubMed 15294286. Source: SGD

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

proton-transporting ATP synthase activity, rotational mechanism

Inferred from sequence or structural similarity Ref.1. Source: SGD

proton-transporting ATPase activity, rotational mechanism

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3535Mitochondrion HAMAP-Rule MF_01346
Chain36 – 545510ATP synthase subunit alpha, mitochondrial HAMAP-Rule MF_01346
PRO_0000002433

Regions

Nucleotide binding206 – 2138ATP By similarity

Sites

Site4071Required for activity By similarity

Amino acid modifications

Modified residue571Phosphoserine Ref.9
Modified residue1781Phosphoserine Ref.9

Experimental info

Mutagenesis2911G → D in ATP1-2; growth-defect. Ref.2
Mutagenesis3831T → I in ATP1-1; growth-defect. Ref.2
Sequence conflict311 – 3133QAV → ASL in AAA66888. Ref.1
Sequence conflict3211L → M in AAA66888. Ref.1
Sequence conflict3401S → P in CAA56001. Ref.3
Sequence conflict3401S → P in CAA84924. Ref.4
Sequence conflict3851G → A in AAA66888. Ref.1
Sequence conflict4591E → Q in AAA66888. Ref.1
Sequence conflict479 – 4835VPLIY → SMII in AAA66888. Ref.1
Sequence conflict490 – 4934LDGI → SGWY in AAA66888. Ref.1

Secondary structure

......................................................................................... 545
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07251 [UniParc].

Last modified July 27, 2011. Version 5.
Checksum: E8041D289B924696

FASTA54558,608
        10         20         30         40         50         60 
MLARTAAIRS LSRTLINSTK AARPAAAALA STRRLASTKA QPTEVSSILE ERIKGVSDEA 

        70         80         90        100        110        120 
NLNETGRVLA VGDGIARVFG LNNIQAEELV EFSSGVKGMA LNLEPGQVGI VLFGSDRLVK 

       130        140        150        160        170        180 
EGELVKRTGN IVDVPVGPGL LGRVVDALGN PIDGKGPIDA AGRSRAQVKA PGILPRRSVH 

       190        200        210        220        230        240 
EPVQTGLKAV DALVPIGRGQ RELIIGDRQT GKTAVALDTI LNQKRWNNGS DESKKLYCVY 

       250        260        270        280        290        300 
VAVGQKRSTV AQLVQTLEQH DAMKYSIIVA ATASEAAPLQ YLAPFTAASI GEWFRDNGKH 

       310        320        330        340        350        360 
ALIVYDDLSK QAVAYRQLSL LLRRPPGREA YPGDVFYLHS RLLERAAKLS EKEGSGSLTA 

       370        380        390        400        410        420 
LPVIETQGGD VSAYIPTNVI SITDGQIFLE AELFYKGIRP AINVGLSVSR VGSAAQVKAL 

       430        440        450        460        470        480 
KQVAGSLKLF LAQYREVAAF AQFGSDLDAS TKQTLVRGER LTQLLKQNQY SPLATEEQVP 

       490        500        510        520        530        540 
LIYAGVNGHL DGIELSRIGE FESSFLSYLK SNHNELLTEI REKGELSKEL LASLKSATES 


FVATF 

« Hide

References

« Hide 'large scale' references
[1]"Nuclear genes encoding the yeast mitochondrial ATPase complex. Analysis of ATP1 coding the F1-ATPase alpha-subunit and its assembly."
Takeda M., Chen W.-J., Saltzgaber J., Douglas M.G.
J. Biol. Chem. 261:15126-15133(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"ASC1/RAS2 suppresses the growth-defect on glycerol caused by the atp1-2 mutation in the yeast Saccharomyces cerevisiae."
Mabuchi T., Ichimura Y., Takeda M., Douglas M.G.
J. Biol. Chem. 275:10492-10497(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF GLY-291 AND THR-383.
Strain: ATCC 64665 / S288c / DC5.
[3]"Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces cerevisiae chromosome II."
Obermaier B., Gassenhuber J., Piravandi E., Domdey H.
Yeast 11:1103-1112(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"Complete DNA sequence of yeast chromosome II."
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C. expand/collapse author list , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[5]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 340.
Strain: ATCC 204508 / S288c.
[6]"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae."
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. expand/collapse author list , Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.
Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[7]"Yeast mitochondrial dehydrogenases are associated in a supramolecular complex."
Grandier-Vazeille X., Bathany K., Chaignepain S., Camougrand N., Manon S., Schmitter J.-M.
Biochemistry 40:9758-9769(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[9]"Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase."
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B., van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.
Mol. Cell. Proteomics 6:1896-1906(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ATCC 76625 / YPH499.
[10]"Molecular architecture of the rotary motor in ATP synthase."
Stock D., Leslie A.G., Walker J.E.
Science 286:1700-1705(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J02603 Genomic DNA. Translation: AAA66888.1.
D88458 Genomic DNA. Translation: BAA13613.1.
D37948 Genomic DNA. Translation: BAA22508.1.
X79489 Genomic DNA. Translation: CAA56001.1.
Z35861 Genomic DNA. Translation: CAA84924.1.
AY692969 Genomic DNA. Translation: AAT92988.1.
BK006936 Genomic DNA. Translation: DAA07026.2.
PIRPWBYA. S45401.
RefSeqNP_009453.2. NM_001178339.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HLDX-ray2.80A/B/C/J/K/L/S/T/U36-545[»]
2WPDX-ray3.43A/B/C36-545[»]
2XOKX-ray3.01A/B/C1-545[»]
3FKSX-ray3.59A/B/C/J/K/L/S/T/U36-545[»]
3OE7X-ray3.19A/B/C/J/K/L/S/T/U36-545[»]
3OEEX-ray2.74A/B/C/J/K/L/S/T/U36-545[»]
3OEHX-ray3.00A/B/C/J/K/L/S/T/U36-545[»]
3OFNX-ray3.20A/B/C/J/K/L/S/T/U36-545[»]
3ZIAX-ray2.50A/B/C/K/L/M36-545[»]
3ZRYX-ray6.50A/B/C36-545[»]
4B2Qelectron microscopy37.00A/C/a/c61-545[»]
B/b60-545[»]
ProteinModelPortalP07251.
SMRP07251. Positions 61-544.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32606. 93 interactions.
DIPDIP-3025N.
IntActP07251. 18 interactions.
MINTMINT-2786223.

Protein family/group databases

TCDB3.A.2.1.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Proteomic databases

MaxQBP07251.
PaxDbP07251.
PeptideAtlasP07251.
PRIDEP07251.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBL099W; YBL099W; YBL099W.
GeneID852177.
KEGGsce:YBL099W.

Organism-specific databases

SGDS000000195. ATP1.

Phylogenomic databases

eggNOGCOG0056.
GeneTreeENSGT00550000074846.
HOGENOMHOG000130111.
KOK02132.
OMALHASNTC.
OrthoDBEOG7FNCHF.

Enzyme and pathway databases

BioCycYEAST:G3O-28984-MONOMER.
ReactomeREACT_118590. Mitochondrial Protein Import (yeast).

Gene expression databases

GenevestigatorP07251.

Family and domain databases

Gene3D2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPMF_01346. ATP_synth_alpha_bact.
InterProIPR020003. ATPase_a/bsu_AS.
IPR023366. ATPase_asu-like.
IPR005294. ATPase_F1-cplx_asu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SUPFAMSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00962. atpA. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07251.
NextBio970637.
PROP07251.

Entry information

Entry nameATPA_YEAST
AccessionPrimary (citable) accession number: P07251
Secondary accession number(s): D6VPQ6, Q92449
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: July 27, 2011
Last modified: June 11, 2014
This is version 153 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references