Reviewed, UniProtKB/Swiss-Prot P07251 (ATPA_YEAST)

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 (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

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. Ref.8
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
Gene Ontology (GO)
Biological process	ATP synthesis coupled proton transport Ref.1 Inferred from mutant phenotype. Source: SGD
Cellular component	mitochondrial nucleoid Inferred from direct assay. Source: SGD mitochondrial proton-transporting ATP synthase, catalytic core Ref.1 Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW hydrogen ion transporting ATP synthase activity, rotational mechanism Ref.1 Inferred from electronic annotation. Source: InterPro 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

383

1

T → I in ATP1-2; growth-defect.

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.2

Sequence conflict

340

1

S → P in CAA84924. Ref.2

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

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545

Helix Strand Turn

Details...

Beta strand

63 – 72

10

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 – 131

8

Beta strand

133 – 137

5

Helix

138 – 140

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

Helix

212 – 222

11

Helix

224 – 227

4

Beta strand

237 – 244

8

Helix

247 – 259

13

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

Turn

351 – 354

4

Beta strand

357 – 365

9

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 – 436

19

Helix

438 – 441

4

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 – 543

16

Sequences

	Sequence		Length	Mass (Da)
	P07251-1 [UniParc]. Last modified October 25, 2004. Version 3. 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: 2876995] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	Mabuchi T., Ichimura Y., Takeda M. Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTANT ATP1-2. Strain: XJY12.
[3]	Mabuchi T., Ichimura Y., Takeda M., Douglas M.G. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 64665 / S288c / DC5.
[4]	"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: 7502586] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[5]	"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: 7813418] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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: 17322287] [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: 11502169] [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: 14562106] [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: 17761666] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-178, MASS SPECTROMETRY.
[10]	"Molecular architecture of the rotary motor in ATP synthase." Stock D., Leslie A.G., Walker J.E. Science 286:1700-1705(1999) [PubMed: 10576729] [Abstract] Cited for: 3D-STRUCTURE MODELING.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

J02603 Genomic DNA. Translation: AAA66888.1.
X79489 Genomic DNA. Translation: CAA56001.1.
D88458 Genomic DNA. Translation: BAA13613.1.
D37948 Genomic DNA. Translation: BAA22508.1.
Z35861 Genomic DNA. Translation: CAA84924.1.
AY692969 Genomic DNA. Translation: AAT92988.1.

PIR

PWBYA. S45401.

RefSeq

NP_009453.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2HLD	X-ray	2.80	A/B/C/J/K/L/S/T/U	36-545	[»]
3FKS	X-ray	3.59	A/B/C/J/K/L/S/T/U	36-545	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:3025N.

IntAct

P07251. 22 interactions.

STRING

P07251.

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

PeptideAtlas

P07251.

PRIDE

P07251.

Genome annotation databases

Ensembl

YBL099W; YBL099W; YBL099W; Saccharomyces cerevisiae. [Genome view]

GeneID

852177.

KEGG

sce:YBL099W.

Organism-specific databases

CYGD

YBL099w.

SGD

S000000195. ATP1.

Phylogenomic databases

HOGENOM

P07251.

OrthoDB

EOG9RFN8R

Gene expression databases

ArrayExpress

P07251.

Genevestigator

P07251.

GermOnline

YBL099W. Saccharomyces cerevisiae.

Family and domain databases

InterPro

IPR005294. ATPase_F1-cplx_asu.
IPR017458. ATPase_F1-cplx_asu_C.
IPR018118. ATPase_F1/A1-cplx_a/bsu_N.
IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C.
IPR004100. ATPase_F1/V1/A1-cplx_a/bsu_N.
IPR020003. ATPase_F1/V1/A1_a/bsu_AS.
IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd.
[Graphical view]

PANTHER

PTHR15184:SF3. ATPase_F1_a. 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]

TIGRFAMs

TIGR00962. atpA. 1 hit.

PROSITE

PS00152. ATPASE_ALPHA_BETA. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ATPA_YEAST

Accession

Primary (citable) accession number: P07251
Secondary accession number(s): Q92449

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	October 25, 2004
Last modified:	November 24, 2009
This is version 109 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)