P07251 (ATPA_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP synthase subunit alpha, mitochondrial

Gene names

Name:	ATP1
Ordered Locus Names:	YBL099W
ORF Names:	YBL0827

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	545 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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 process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	CF(1) Membrane Mitochondrion Mitochondrion inner membrane
Domain	Transit peptide
Ligand	ATP-binding Nucleotide-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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_component	cytosol Traceable author statement. Source: Reactome integral to membrane Inferred from sequence model PubMed 12192589. Source: SGD 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
Molecular_function	ATP 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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 35

35

Mitochondrion

Chain

36 – 545

510

ATP synthase subunit alpha, mitochondrial

PRO_0000002433

Regions

Nucleotide binding

206 – 213

8

ATP By similarity

Sites

Site

407

1

Required for activity By similarity

Amino acid modifications

Modified residue

57

1

Phosphoserine Ref.9

Modified residue

178

1

Phosphoserine Ref.9

Experimental info

Mutagenesis

291

1

G → D in ATP1-2; growth-defect. Ref.2

Mutagenesis

383

1

T → I in ATP1-1; growth-defect. Ref.2

Sequence conflict

311 – 313

3

QAV → ASL in AAA66888. Ref.1

Sequence conflict

321

1

L → M in AAA66888. Ref.1

Sequence conflict

340

1

S → P in CAA56001. Ref.3

Sequence conflict

340

1

S → P in CAA84924. Ref.4

Sequence conflict

385

1

G → A in AAA66888. Ref.1

Sequence conflict

459

1

E → Q in AAA66888. Ref.1

Sequence conflict

479 – 483

5

VPLIY → SMII in AAA66888. Ref.1

Sequence conflict

490 – 493

4

LDGI → SGWY in AAA66888. Ref.1

Secondary structure

1

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545

Helix Strand Turn

Details...

Turn

62 – 64

3

Beta strand

65 – 72

8

Beta strand

75 – 80

6

Beta strand

88 – 92

5

Beta strand

97 – 103

7

Beta strand

108 – 114

7

Helix

116 – 118

3

Beta strand

124 – 137

14

Helix

138 – 140

3

Beta strand

144 – 146

3

Beta strand

153 – 155

3

Beta strand

161 – 167

7

Beta strand

173 – 176

4

Beta strand

181 – 183

3

Helix

188 – 193

6

Beta strand

203 – 207

5

Beta strand

208 – 211

4

Helix

212 – 221

10

Helix

224 – 227

4

Beta strand

228 – 230

3

Turn

232 – 234

3

Beta strand

237 – 244

8

Helix

247 – 258

12

Turn

259 – 261

3

Helix

263 – 265

3

Beta strand

266 – 271

6

Helix

277 – 296

20

Beta strand

300 – 306

7

Helix

308 – 321

14

Helix

328 – 330

3

Helix

335 – 343

9

Beta strand

347 – 349

3

Turn

351 – 354

4

Beta strand

357 – 365

9

Beta strand

367 – 369

3

Helix

374 – 382

9

Beta strand

383 – 389

7

Helix

391 – 396

6

Turn

404 – 406

3

Beta strand

408 – 411

4

Helix

412 – 415

4

Helix

418 – 437

20

Helix

438 – 446

9

Helix

449 – 465

17

Helix

475 – 487

13

Turn

488 – 492

5

Helix

495 – 497

3

Helix

498 – 512

15

Helix

514 – 523

10

Helix

528 – 542

15

Sequences

	Sequence		Length	Mass (Da)
	P07251 [UniParc]. Last modified July 27, 2011. Version 5. Checksum: E8041D289B924696	FASTA	545	58,608
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	Saccharomyces Genome Database Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases 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. , 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, MASS SPECTROMETRY. 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.

PIR

PWBYA. S45401.

RefSeq

NP_009453.2. NM_001178339.2.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P07251.

SMR

P07251. Positions 61-544.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-3025N.

IntAct

P07251. 4 interactions.

MINT

MINT-2786223.

Protein family/group databases

TCDB

3.A.2.1.3. H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) superfamily.

Proteomic databases

PaxDb

P07251.

PeptideAtlas

P07251.

PRIDE

P07251.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblFungi

YBL099W; YBL099W; YBL099W.

GeneID

852177.

KEGG

sce:YBL099W.

Organism-specific databases

SGD

S000000195. ATP1.

Phylogenomic databases

eggNOG

COG0056.

GeneTree

ENSGT00550000074846.

HOGENOM

HOG000130111.

KO

K02132.

OMA

GSDRDIK.

OrthoDB

EOG43NBMV.

Enzyme and pathway databases

Reactome

REACT_118590. Mitochondrial Protein Import (yeast).
REACT_85873. Metabolism of proteins.

Gene expression databases

ArrayExpress

P07251.

Genevestigator

P07251.

GermOnline

YBL099W. Saccharomyces cerevisiae.

Family and domain databases

Gene3D

2.40.30.20. 1 hit.

InterPro

IPR020003. ATPase_a/bsu_AS.
IPR004100. ATPase_a/bsu_N.
IPR005294. ATPase_F1-cplx_asu.
IPR023366. ATPase_F1/A1-cplx_a_su_N.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
[Graphical view]

PANTHER

PTHR15184:SF3. PTHR15184:SF3. 1 hit.

Pfam

PF00006. ATP-synt_ab. 1 hit.
PF00306. ATP-synt_ab_C. 1 hit.
PF02874. ATP-synt_ab_N. 1 hit.
[Graphical view]

SUPFAM

SSF47917. ATPase_a/b_C. 1 hit.
SSF50615. ATPase_a/b_N. 1 hit.

TIGRFAMs

TIGR00962. atpA. 1 hit.

PROSITE

PS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P07251.

NextBio

970637.

Entry information

Entry name

ATPA_YEAST

Accession

Primary (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:	May 1, 2013
This is version 143 of the entry and version 5 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program