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P07251

- ATPA_YEAST

UniProt

P07251 - ATPA_YEAST

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Protein

ATP synthase subunit alpha, mitochondrial

Gene

ATP1

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. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei407 – 4071Required for activityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi206 – 2138ATPBy similarity

GO - Molecular functioni

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

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 - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-28984-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 alpha, mitochondrial
Gene namesi
Name:ATP1
Ordered Locus Names:YBL099W
ORF Names:YBL0827
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
ProteomesiUP000002311: Chromosome II

Organism-specific databases

SGDiS000000195. ATP1.

Subcellular locationi

Mitochondrion inner membrane 1 Publication
Note: Peripheral membrane protein.

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. mitochondrial intermembrane space Source: Reactome
  3. mitochondrial nucleoid Source: SGD
  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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi291 – 2911G → D in ATP1-2; growth-defect. 1 Publication
Mutagenesisi383 – 3831T → I in ATP1-1; growth-defect. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3535MitochondrionAdd
BLAST
Chaini36 – 545510ATP synthase subunit alpha, mitochondrialPRO_0000002433Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei57 – 571Phosphoserine1 Publication
Modified residuei178 – 1781Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP07251.
PaxDbiP07251.
PeptideAtlasiP07251.
PRIDEiP07251.

Expressioni

Gene expression databases

GenevestigatoriP07251.

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

BioGridi32606. 93 interactions.
DIPiDIP-3025N.
IntActiP07251. 18 interactions.
MINTiMINT-2786223.

Structurei

Secondary structure

1
545
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni62 – 643Combined sources
Beta strandi65 – 728Combined sources
Beta strandi75 – 806Combined sources
Beta strandi88 – 925Combined sources
Beta strandi97 – 1037Combined sources
Beta strandi108 – 1147Combined sources
Helixi116 – 1183Combined sources
Beta strandi124 – 13714Combined sources
Helixi138 – 1403Combined sources
Beta strandi144 – 1463Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi161 – 1677Combined sources
Beta strandi173 – 1764Combined sources
Beta strandi181 – 1833Combined sources
Helixi188 – 1936Combined sources
Beta strandi203 – 2075Combined sources
Beta strandi208 – 2114Combined sources
Helixi212 – 22110Combined sources
Helixi224 – 2274Combined sources
Beta strandi228 – 2303Combined sources
Turni232 – 2343Combined sources
Beta strandi237 – 2448Combined sources
Helixi247 – 25812Combined sources
Turni259 – 2613Combined sources
Helixi263 – 2653Combined sources
Beta strandi266 – 2716Combined sources
Helixi277 – 29620Combined sources
Beta strandi300 – 3067Combined sources
Helixi308 – 32114Combined sources
Helixi328 – 3303Combined sources
Helixi335 – 3439Combined sources
Beta strandi347 – 3493Combined sources
Turni351 – 3544Combined sources
Beta strandi357 – 3659Combined sources
Beta strandi367 – 3693Combined sources
Helixi374 – 3829Combined sources
Beta strandi383 – 3897Combined sources
Helixi391 – 3966Combined sources
Turni404 – 4063Combined sources
Beta strandi408 – 4114Combined sources
Helixi412 – 4154Combined sources
Helixi418 – 43720Combined sources
Helixi438 – 4469Combined sources
Helixi449 – 46517Combined sources
Helixi475 – 48713Combined sources
Turni488 – 4925Combined sources
Helixi495 – 4973Combined sources
Helixi498 – 51215Combined sources
Helixi514 – 52310Combined sources
Helixi528 – 54215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP07251.
SMRiP07251. Positions 61-544.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07251.

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase alpha/beta chains family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0056.
GeneTreeiENSGT00550000074846.
HOGENOMiHOG000130111.
InParanoidiP07251.
KOiK02132.
OMAiLHASNTC.
OrthoDBiEOG7FNCHF.

Family and domain databases

Gene3Di2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPiMF_01346. ATP_synth_alpha_bact.
InterProiIPR020003. 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]
PfamiPF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]
SUPFAMiSSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00962. atpA. 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.

P07251-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLARTAAIRS LSRTLINSTK AARPAAAALA STRRLASTKA QPTEVSSILE
60 70 80 90 100
ERIKGVSDEA NLNETGRVLA VGDGIARVFG LNNIQAEELV EFSSGVKGMA
110 120 130 140 150
LNLEPGQVGI VLFGSDRLVK EGELVKRTGN IVDVPVGPGL LGRVVDALGN
160 170 180 190 200
PIDGKGPIDA AGRSRAQVKA PGILPRRSVH EPVQTGLKAV DALVPIGRGQ
210 220 230 240 250
RELIIGDRQT GKTAVALDTI LNQKRWNNGS DESKKLYCVY VAVGQKRSTV
260 270 280 290 300
AQLVQTLEQH DAMKYSIIVA ATASEAAPLQ YLAPFTAASI GEWFRDNGKH
310 320 330 340 350
ALIVYDDLSK QAVAYRQLSL LLRRPPGREA YPGDVFYLHS RLLERAAKLS
360 370 380 390 400
EKEGSGSLTA LPVIETQGGD VSAYIPTNVI SITDGQIFLE AELFYKGIRP
410 420 430 440 450
AINVGLSVSR VGSAAQVKAL KQVAGSLKLF LAQYREVAAF AQFGSDLDAS
460 470 480 490 500
TKQTLVRGER LTQLLKQNQY SPLATEEQVP LIYAGVNGHL DGIELSRIGE
510 520 530 540
FESSFLSYLK SNHNELLTEI REKGELSKEL LASLKSATES FVATF
Length:545
Mass (Da):58,608
Last modified:July 27, 2011 - v5
Checksum:iE8041D289B924696
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti311 – 3133QAV → ASL in AAA66888. (PubMed:2876995)Curated
Sequence conflicti321 – 3211L → M in AAA66888. (PubMed:2876995)Curated
Sequence conflicti340 – 3401S → P in CAA56001. (PubMed:7502586)Curated
Sequence conflicti340 – 3401S → P in CAA84924. (PubMed:7813418)Curated
Sequence conflicti385 – 3851G → A in AAA66888. (PubMed:2876995)Curated
Sequence conflicti459 – 4591E → Q in AAA66888. (PubMed:2876995)Curated
Sequence conflicti479 – 4835VPLIY → SMII in AAA66888. (PubMed:2876995)Curated
Sequence conflicti490 – 4934LDGI → SGWY in AAA66888. (PubMed:2876995)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiS45401. PWBYA.
RefSeqiNP_009453.2. NM_001178339.2.

Genome annotation databases

EnsemblFungiiYBL099W; YBL099W; YBL099W.
GeneIDi852177.
KEGGisce:YBL099W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi S45401. PWBYA.
RefSeqi NP_009453.2. NM_001178339.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HLD X-ray 2.80 A/B/C/J/K/L/S/T/U 36-545 [» ]
2WPD X-ray 3.43 A/B/C 36-545 [» ]
2XOK X-ray 3.01 A/B/C 1-545 [» ]
3FKS X-ray 3.59 A/B/C/J/K/L/S/T/U 36-545 [» ]
3OE7 X-ray 3.19 A/B/C/J/K/L/S/T/U 36-545 [» ]
3OEE X-ray 2.74 A/B/C/J/K/L/S/T/U 36-545 [» ]
3OEH X-ray 3.00 A/B/C/J/K/L/S/T/U 36-545 [» ]
3OFN X-ray 3.20 A/B/C/J/K/L/S/T/U 36-545 [» ]
3ZIA X-ray 2.50 A/B/C/K/L/M 36-545 [» ]
3ZRY X-ray 6.50 A/B/C 36-545 [» ]
4B2Q electron microscopy 37.00 A/C/a/c 61-545 [» ]
B/b 60-545 [» ]
ProteinModelPortali P07251.
SMRi P07251. Positions 61-544.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 32606. 93 interactions.
DIPi DIP-3025N.
IntActi P07251. 18 interactions.
MINTi MINT-2786223.

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.

Proteomic databases

MaxQBi P07251.
PaxDbi P07251.
PeptideAtlasi P07251.
PRIDEi P07251.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii YBL099W ; YBL099W ; YBL099W .
GeneIDi 852177.
KEGGi sce:YBL099W.

Organism-specific databases

SGDi S000000195. ATP1.

Phylogenomic databases

eggNOGi COG0056.
GeneTreei ENSGT00550000074846.
HOGENOMi HOG000130111.
InParanoidi P07251.
KOi K02132.
OMAi LHASNTC.
OrthoDBi EOG7FNCHF.

Enzyme and pathway databases

BioCyci YEAST:G3O-28984-MONOMER.
Reactomei REACT_189012. Mitochondrial protein import.

Miscellaneous databases

EvolutionaryTracei P07251.
NextBioi 970637.
PROi P07251.

Gene expression databases

Genevestigatori P07251.

Family and domain databases

Gene3Di 2.40.30.20. 1 hit.
3.40.50.300. 1 hit.
HAMAPi MF_01346. ATP_synth_alpha_bact.
InterProi IPR020003. 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 ]
Pfami PF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47917. SSF47917. 1 hit.
SSF50615. SSF50615. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00962. atpA. 1 hit.
PROSITEi PS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: GENOME REANNOTATION, SEQUENCE REVISION TO 340.
    Strain: ATCC 204508 / S288c.
  6. 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. 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.

Entry informationi

Entry nameiATPA_YEAST
AccessioniPrimary (citable) accession number: P07251
Secondary accession number(s): D6VPQ6, Q92449
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 157 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 41500 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, 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 II
    Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

External Data

Dasty 3