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P00830 (ATPB_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 155. 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 beta, mitochondrial

EC=3.6.3.14
Gene names
Name:ATP2
Ordered Locus Names:YJR121W
ORF Names:J2041
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length511 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. HAMAP-Rule MF_01347

Catalytic activity

ATP + H2O + H+(In) = ADP + phosphate + H+(Out). HAMAP-Rule MF_01347

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. Mitochondrion inner membrane. Note: Peripheral membrane protein. HAMAP-Rule MF_01347

Miscellaneous

Present with 164000 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
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
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 inner membrane

Traceable author statement. Source: Reactome

mitochondrial intermembrane space

Traceable author statement. Source: Reactome

mitochondrial proton-transporting ATP synthase, catalytic core

Inferred from direct assay PubMed 17082766. Source: SGD

mitochondrion

Inferred from physical interaction PubMed 16962558. 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 electronic annotation. Source: InterPro

proton-transporting ATPase activity, rotational mechanism

Inferred from mutant phenotype PubMed 2529856. Source: SGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3333Mitochondrion HAMAP-Rule MF_01347
Chain34 – 511478ATP synthase subunit beta, mitochondrial HAMAP-Rule MF_01347
PRO_0000002454

Regions

Nucleotide binding190 – 1978ATP By similarity

Amino acid modifications

Modified residue1121Phosphothreonine Ref.11
Modified residue2371Phosphothreonine Ref.11
Modified residue3731Phosphoserine Ref.11

Experimental info

Sequence conflict2011Q → M in AAA34443. Ref.8
Sequence conflict2181T → A in AAA34444. Ref.1
Sequence conflict2181T → A in AAA34443. Ref.8
Sequence conflict232 – 2376REMKET → HEMEDS in AAA34443. Ref.8
Sequence conflict2601G → E in AAA34443. Ref.8
Sequence conflict287 – 2882FI → Y in AAA34443. Ref.8
Sequence conflict354 – 3585APATT → SPSTS in AAA34444. Ref.1
Sequence conflict365 – 3662TT → SS in AAA34444. Ref.1
Sequence conflict365 – 3662TT → SS in AAA34443. Ref.8
Sequence conflict469 – 4735DTVAS → RTRCL in AAA34443. Ref.8
Sequence conflict4891A → R in AAA34443. Ref.8
Sequence conflict5011A → R in AAA34444. Ref.1
Sequence conflict5081A → R in AAA34444. Ref.1

Secondary structure

............................................................................................. 511
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00830 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: EDFF256826F68F0C

FASTA51154,794
        10         20         30         40         50         60 
MVLPRLYTAT SRAAFKAAKQ SAPLLSTSWK RCMASAAQST PITGKVTAVI GAIVDVHFEQ 

        70         80         90        100        110        120 
SELPAILNAL EIKTPQGKLV LEVAQHLGEN TVRTIAMDGT EGLVRGEKVL DTGGPISVPV 

       130        140        150        160        170        180 
GRETLGRIIN VIGEPIDERG PIKSKLRKPI HADPPSFAEQ STSAEILETG IKVVDLLAPY 

       190        200        210        220        230        240 
ARGGKIGLFG GAGVGKTVFI QELINNIAKA HGGFSVFTGV GERTREGNDL YREMKETGVI 

       250        260        270        280        290        300 
NLEGESKVAL VFGQMNEPPG ARARVALTGL TIAEYFRDEE GQDVLLFIDN IFRFTQAGSE 

       310        320        330        340        350        360 
VSALLGRIPS AVGYQPTLAT DMGLLQERIT TTKKGSVTSV QAVYVPADDL TDPAPATTFA 

       370        380        390        400        410        420 
HLDATTVLSR GISELGIYPA VDPLDSKSRL LDAAVVGQEH YDVASKVQET LQTYKSLQDI 

       430        440        450        460        470        480 
IAILGMDELS EQDKLTVERA RKIQRFLSQP FAVAEVFTGI PGKLVRLKDT VASFKAVLEG 

       490        500        510 
KYDNIPEHAF YMVGGIEDVV AKAEKLAAEA N 

« Hide

References

« Hide 'large scale' references
[1]"Nuclear genes coding the yeast mitochondrial adenosine triphosphatase complex. Primary sequence analysis of ATP2 encoding the F1-ATPase beta-subunit precursor."
Takeda M., Vassarotti A., Douglas M.G.
J. Biol. Chem. 260:15458-15465(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]Erratum
Takeda M., Vassarotti A., Douglas M.G.
J. Biol. Chem. 261:10466-10466(1986)
[3]Takeda M.
Submitted (JUL-1986) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]"Characterization of mutations in the beta subunit of the mitochondrial F1-ATPase that produce defects in enzyme catalysis and assembly."
Liang Y., Ackerman S.H.
J. Biol. Chem. 271:26522-26528(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 24657 / D273-10B.
[5]"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. expand/collapse author list , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[6]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[7]"Transport of the yeast ATP synthase beta-subunit into mitochondria. Effects of amino acid substitutions on targeting."
Walker M.E., Valentin E., Reid G.A.
Biochem. J. 266:227-234(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
[8]"Nuclear genes coding the yeast mitochondrial adenosine triphosphatase complex. Isolation of ATP2 coding the F1-ATPase beta subunit."
Saltzgaber-Muller J., Kunapuli S.P., Douglas M.G.
J. Biol. Chem. 258:11465-11470(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 195-507.
[9]"Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae."
Norbeck J., Blomberg A.
FEMS Microbiol. Lett. 137:1-8(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 371-379 AND 390-398.
Strain: ATCC 38531 / Y41.
[10]"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].
[11]"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 THR-112; THR-237 AND SER-373, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: ATCC 76625 / YPH499.
[12]"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
M12082 Genomic DNA. Translation: AAA34444.1.
U46215 Genomic DNA. Translation: AAC49475.1.
Z49621 Genomic DNA. Translation: CAA89652.1.
X52004 Genomic DNA. Translation: CAA36255.1.
K00560 Genomic DNA. Translation: AAA34443.1.
BK006943 Genomic DNA. Translation: DAA08906.1.
PIRPWBYB. S57144.
RefSeqNP_012655.3. NM_001181779.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HLDX-ray2.80D/E/F/M/N/O/V/W/X34-511[»]
2WPDX-ray3.43D/E/F34-511[»]
2XOKX-ray3.01D/E/F1-507[»]
3FKSX-ray3.59D/E/F/M/N/O/V/W/X36-511[»]
3OE7X-ray3.19D/E/F/M/N/O/V/W/X36-511[»]
3OEEX-ray2.74D/E/F/M/N/O/V/W/X36-511[»]
3OEHX-ray3.00D/E/F/M/N/O/V/W/X36-511[»]
3OFNX-ray3.20D/E/F/M/N/O/V/W/X36-511[»]
3ZIAX-ray2.50D/E/F/N/O/P34-511[»]
3ZRYX-ray6.50D/E/F34-511[»]
4B2Qelectron microscopy37.00D/d39-508[»]
E/F/e/f39-511[»]
ProteinModelPortalP00830.
SMRP00830. Positions 39-508.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid33877. 62 interactions.
DIPDIP-3028N.
IntActP00830. 66 interactions.
MINTMINT-534087.
STRING4932.YJR121W.

Chemistry

BindingDBP00830.
ChEMBLCHEMBL1075103.

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.

2D gel databases

SWISS-2DPAGEP00830.

Proteomic databases

PaxDbP00830.
PeptideAtlasP00830.
PRIDEP00830.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYJR121W; YJR121W; YJR121W.
GeneID853585.
KEGGsce:YJR121W.

Organism-specific databases

CYGDYJR121w.
SGDS000003882. ATP2.

Phylogenomic databases

eggNOGCOG0055.
GeneTreeENSGT00550000074800.
HOGENOMHOG000009605.
KOK02133.
OMAAVVPNVR.
OrthoDBEOG7F7WJV.

Enzyme and pathway databases

BioCycYEAST:G3O-31742-MONOMER.
ReactomeREACT_118590. Mitochondrial Protein Import (yeast).
REACT_85873. Metabolism of proteins.

Gene expression databases

GenevestigatorP00830.

Family and domain databases

Gene3D1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPMF_01347. ATP_synth_beta_bact.
InterProIPR003593. AAA+_ATPase.
IPR020003. ATPase_a/bsu_AS.
IPR005722. ATPase_F1-cplx_bsu.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
IPR004100. ATPase_F1_a/bsu_N.
IPR024034. ATPase_F1_bsu/V1_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR15184:SF8. PTHR15184:SF8. 1 hit.
PfamPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR01039. atpD. 1 hit.
PROSITEPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00830.
NextBio974382.
PROP00830.

Entry information

Entry nameATPB_YEAST
AccessionPrimary (citable) accession number: P00830
Secondary accession number(s): D6VWU0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 20, 2005
Last modified: April 16, 2014
This is version 155 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome X

Yeast (Saccharomyces cerevisiae) chromosome X: 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