SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P00830

- ATPB_YEAST

UniProt

P00830 - ATPB_YEAST

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

ATP synthase subunit beta, mitochondrial

Gene
ATP2, YJR121W, J2041
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.UniRule annotation

Catalytic activityi

ATP + H2O + H+(In) = ADP + phosphate + H+(Out).UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi190 – 1978ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. proton-transporting ATPase activity, rotational mechanism Source: SGD
  3. proton-transporting ATP synthase activity, rotational mechanism Source: InterPro

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. ATP hydrolysis coupled proton transport Source: InterPro
  3. ATP synthesis coupled proton transport Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-31742-MONOMER.
ReactomeiREACT_189012. Mitochondrial protein import.

Protein family/group databases

TCDBi3.A.2.1.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
ATP synthase subunit beta, mitochondrial (EC:3.6.3.14)
Gene namesi
Name:ATP2
Ordered Locus Names:YJR121W
ORF Names:J2041
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome X

Organism-specific databases

CYGDiYJR121w.
SGDiS000003882. ATP2.

Subcellular locationi

Mitochondrion. Mitochondrion inner membrane
Note: Peripheral membrane protein.UniRule annotation

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrial inner membrane Source: Reactome
  3. mitochondrial intermembrane space Source: Reactome
  4. mitochondrial proton-transporting ATP synthase, catalytic core Source: SGD
  5. mitochondrion Source: SGD
  6. proton-transporting ATP synthase complex, catalytic core F(1) Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

CF(1), Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333MitochondrionUniRule annotationAdd
BLAST
Chaini34 – 511478ATP synthase subunit beta, mitochondrialUniRule annotationPRO_0000002454Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei112 – 1121Phosphothreonine1 Publication
Modified residuei237 – 2371Phosphothreonine1 Publication
Modified residuei373 – 3731Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP00830.
PaxDbiP00830.
PeptideAtlasiP00830.
PRIDEiP00830.

2D gel databases

SWISS-2DPAGEP00830.

Expressioni

Gene expression databases

GenevestigatoriP00830.

Interactioni

Subunit structurei

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.

Protein-protein interaction databases

BioGridi33877. 73 interactions.
DIPiDIP-3028N.
IntActiP00830. 66 interactions.
MINTiMINT-534087.
STRINGi4932.YJR121W.

Structurei

Secondary structure

1
511
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi43 – 508
Beta strandi53 – 586
Beta strandi59 – 613
Beta strandi69 – 724
Beta strandi75 – 773
Beta strandi79 – 8810
Beta strandi91 – 988
Beta strandi108 – 1114
Beta strandi113 – 1153
Beta strandi117 – 1193
Helixi122 – 1243
Beta strandi128 – 1303
Beta strandi131 – 1333
Beta strandi137 – 1393
Beta strandi147 – 1504
Helixi157 – 1593
Helixi172 – 1776
Beta strandi180 – 1834
Beta strandi184 – 1907
Beta strandi192 – 1954
Helixi196 – 20712
Turni208 – 2103
Beta strandi211 – 2133
Beta strandi215 – 2228
Helixi224 – 23512
Turni236 – 2383
Beta strandi242 – 2443
Beta strandi247 – 2537
Helixi259 – 27820
Beta strandi283 – 2897
Helixi292 – 30211
Helixi303 – 3053
Helixi311 – 3133
Helixi318 – 3269
Beta strandi332 – 3343
Beta strandi335 – 34410
Helixi346 – 3483
Helixi353 – 3586
Helixi359 – 3613
Beta strandi363 – 3686
Helixi370 – 3745
Turni383 – 3853
Helixi393 – 3964
Helixi398 – 42326
Helixi426 – 4283
Helixi431 – 44616
Helixi455 – 4584
Helixi467 – 47913
Turni480 – 4845
Helixi487 – 4893
Turni490 – 4923
Helixi496 – 50712

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP00830.
SMRiP00830. Positions 39-508.

Miscellaneous databases

EvolutionaryTraceiP00830.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0055.
GeneTreeiENSGT00550000074800.
HOGENOMiHOG000009605.
KOiK02133.
OMAiVVRGIHQ.
OrthoDBiEOG7F7WJV.

Family and domain databases

Gene3Di1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01347. ATP_synth_beta_bact.
InterProiIPR003593. 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]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01039. atpD. 1 hit.
PROSITEiPS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00830-1 [UniParc]FASTAAdd to Basket

« Hide

MVLPRLYTAT SRAAFKAAKQ SAPLLSTSWK RCMASAAQST PITGKVTAVI    50
GAIVDVHFEQ SELPAILNAL EIKTPQGKLV LEVAQHLGEN TVRTIAMDGT 100
EGLVRGEKVL DTGGPISVPV GRETLGRIIN VIGEPIDERG PIKSKLRKPI 150
HADPPSFAEQ STSAEILETG IKVVDLLAPY ARGGKIGLFG GAGVGKTVFI 200
QELINNIAKA HGGFSVFTGV GERTREGNDL YREMKETGVI NLEGESKVAL 250
VFGQMNEPPG ARARVALTGL TIAEYFRDEE GQDVLLFIDN IFRFTQAGSE 300
VSALLGRIPS AVGYQPTLAT DMGLLQERIT TTKKGSVTSV QAVYVPADDL 350
TDPAPATTFA HLDATTVLSR GISELGIYPA VDPLDSKSRL LDAAVVGQEH 400
YDVASKVQET LQTYKSLQDI IAILGMDELS EQDKLTVERA RKIQRFLSQP 450
FAVAEVFTGI PGKLVRLKDT VASFKAVLEG KYDNIPEHAF YMVGGIEDVV 500
AKAEKLAAEA N 511
Length:511
Mass (Da):54,794
Last modified:December 20, 2005 - v2
Checksum:iEDFF256826F68F0C
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti201 – 2011Q → M in AAA34443. 1 Publication
Sequence conflicti218 – 2181T → A in AAA34444. 1 Publication
Sequence conflicti218 – 2181T → A in AAA34443. 1 Publication
Sequence conflicti232 – 2376REMKET → HEMEDS in AAA34443. 1 Publication
Sequence conflicti260 – 2601G → E in AAA34443. 1 Publication
Sequence conflicti287 – 2882FI → Y in AAA34443. 1 Publication
Sequence conflicti354 – 3585APATT → SPSTS in AAA34444. 1 Publication
Sequence conflicti365 – 3662TT → SS in AAA34444. 1 Publication
Sequence conflicti365 – 3662TT → SS in AAA34443. 1 Publication
Sequence conflicti469 – 4735DTVAS → RTRCL in AAA34443. 1 Publication
Sequence conflicti489 – 4891A → R in AAA34443. 1 Publication
Sequence conflicti501 – 5011A → R in AAA34444. 1 Publication
Sequence conflicti508 – 5081A → R in AAA34444. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS57144. PWBYB.
RefSeqiNP_012655.3. NM_001181779.3.

Genome annotation databases

EnsemblFungiiYJR121W; YJR121W; YJR121W.
GeneIDi853585.
KEGGisce:YJR121W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S57144. PWBYB.
RefSeqi NP_012655.3. NM_001181779.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HLD X-ray 2.80 D/E/F/M/N/O/V/W/X 34-511 [» ]
2WPD X-ray 3.43 D/E/F 34-511 [» ]
2XOK X-ray 3.01 D/E/F 1-507 [» ]
3FKS X-ray 3.59 D/E/F/M/N/O/V/W/X 36-511 [» ]
3OE7 X-ray 3.19 D/E/F/M/N/O/V/W/X 36-511 [» ]
3OEE X-ray 2.74 D/E/F/M/N/O/V/W/X 36-511 [» ]
3OEH X-ray 3.00 D/E/F/M/N/O/V/W/X 36-511 [» ]
3OFN X-ray 3.20 D/E/F/M/N/O/V/W/X 36-511 [» ]
3ZIA X-ray 2.50 D/E/F/N/O/P 34-511 [» ]
3ZRY X-ray 6.50 D/E/F 34-511 [» ]
4B2Q electron microscopy 37.00 D/d 39-508 [» ]
E/F/e/f 39-511 [» ]
ProteinModelPortali P00830.
SMRi P00830. Positions 39-508.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 33877. 73 interactions.
DIPi DIP-3028N.
IntActi P00830. 66 interactions.
MINTi MINT-534087.
STRINGi 4932.YJR121W.

Chemistry

BindingDBi P00830.
ChEMBLi CHEMBL1075103.

Protein family/group databases

TCDBi 3.A.2.1.3. the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.

2D gel databases

SWISS-2DPAGE P00830.

Proteomic databases

MaxQBi P00830.
PaxDbi P00830.
PeptideAtlasi P00830.
PRIDEi P00830.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YJR121W ; YJR121W ; YJR121W .
GeneIDi 853585.
KEGGi sce:YJR121W.

Organism-specific databases

CYGDi YJR121w.
SGDi S000003882. ATP2.

Phylogenomic databases

eggNOGi COG0055.
GeneTreei ENSGT00550000074800.
HOGENOMi HOG000009605.
KOi K02133.
OMAi VVRGIHQ.
OrthoDBi EOG7F7WJV.

Enzyme and pathway databases

BioCyci YEAST:G3O-31742-MONOMER.
Reactomei REACT_189012. Mitochondrial protein import.

Miscellaneous databases

EvolutionaryTracei P00830.
NextBioi 974382.
PROi P00830.

Gene expression databases

Genevestigatori P00830.

Family and domain databases

Gene3Di 1.10.1140.10. 1 hit.
3.40.50.300. 1 hit.
HAMAPi MF_01347. ATP_synth_beta_bact.
InterProi IPR003593. 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 ]
Pfami PF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR01039. atpD. 1 hit.
PROSITEi PS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiATPB_YEAST
AccessioniPrimary (citable) accession number: P00830
Secondary accession number(s): D6VWU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 20, 2005
Last modified: September 3, 2014
This is version 158 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 164000 molecules/cell in log phase SD medium.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

External Data

Dasty 3

Similar proteinsi