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Protein

ATP synthase subunit a

Gene

ATP6

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: 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. Key component of the proton channel; it may play a direct role in the translocation of protons across the membrane.

GO - Molecular functioni

GO - Biological processi

  • ATP synthesis coupled proton transport Source: SGD
Complete GO annotation...

Keywords - Biological processi

ATP synthesis, Hydrogen ion transport, Ion transport, Transport

Enzyme and pathway databases

BioCyciYEAST:G3O-34379-MONOMER.

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 a
Alternative name(s):
F-ATPase protein 6
Gene namesi
Name:ATP6
Synonyms:OLI2, OLI4, PHO1
Ordered Locus Names:Q0085
Encoded oniMitochondrion
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Mitochondrion

Organism-specific databases

EuPathDBiFungiDB:Q0085.
SGDiS000007268. ATP6.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei36 – 5621HelicalSequence analysisAdd
BLAST
Transmembranei92 – 11221HelicalSequence analysisAdd
BLAST
Transmembranei125 – 14521HelicalSequence analysisAdd
BLAST
Transmembranei150 – 17021HelicalSequence analysisAdd
BLAST
Transmembranei191 – 21121HelicalSequence analysisAdd
BLAST
Transmembranei216 – 23621HelicalSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

CF(0), Membrane, Mitochondrion, Mitochondrion inner membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 1010Removed in mature form1 PublicationPRO_0000002626
Chaini11 – 259249ATP synthase subunit aPRO_0000002627Add
BLAST

Interactioni

Subunit structurei

F-type ATPases have 2 components, CF1 - the catalytic core - and CF0 - the membrane proton channel. In yeast, the dimeric form of ATP synthase consists of 17 polypeptides: alpha, beta, gamma, delta, epsilon, 4 (B), 5 (OSCP), 6 (A), 8, 9 (C), d, E (Tim11), f, g, h, i/j and k.

Protein-protein interaction databases

BioGridi34793. 21 interactions.
DIPiDIP-3038N.
IntActiP00854. 1 interaction.
MINTiMINT-4981504.

Structurei

3D structure databases

ProteinModelPortaliP00854.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ATPase A chain family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

GeneTreeiENSGT00390000005568.
HOGENOMiHOG000253874.
InParanoidiP00854.
KOiK02126.
OMAiIYDTIMN.
OrthoDBiEOG7WDNFH.

Family and domain databases

Gene3Di1.20.120.220. 1 hit.
HAMAPiMF_01393. ATP_synth_a_bact.
InterProiIPR000568. ATPase_F0-cplx_asu.
IPR023011. ATPase_F0-cplx_asu_AS.
[Graphical view]
PANTHERiPTHR11410. PTHR11410. 1 hit.
PfamiPF00119. ATP-synt_A. 1 hit.
[Graphical view]
PRINTSiPR00123. ATPASEA.
SUPFAMiSSF81336. SSF81336. 1 hit.
TIGRFAMsiTIGR01131. ATP_synt_6_or_A. 1 hit.
PROSITEiPS00449. ATPASE_A. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P00854-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFNLLNTYIT SPLDQFEIRT LFGLQSSFID LSCLNLTTFS LYTIIVLLVI
60 70 80 90 100
TSLYTLTNNN NKIIGSRWLI SQEAIYDTIM NMTKGQIGGK NWGLYFPMIF
110 120 130 140 150
TLFMFIFIAN LISMIPYSFA LSAHLVFIIS LSIVIWLGNT ILGLYKHGWV
160 170 180 190 200
FFSLFVPAGT PLPLVPLLVI IETLSYFARA ISLGLRLGSN ILAGHLLMVI
210 220 230 240 250
LAGLTFNFML INLFTLVFGF VPLAMILAIM MLEFAIGIIQ GYVWAILTAS

YLKDAVYLH
Length:259
Mass (Da):29,099
Last modified:May 27, 2002 - v2
Checksum:i1A3257747B5A7C57
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti171 – 1711I → M in strain: D273-10B/A1.
Natural varianti177 – 1771F → I in strain: D273-10B/A1.
Natural varianti231 – 2311M → I in strain: D273-10B/A1.
Natural varianti241 – 2411G → S in strain: D273-10B/A1.
Natural varianti245 – 2451A → T in strain: D273-10B/A1.
Natural varianti255 – 2562AV → TL in strain: D273-10B/A1.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01464 Genomic DNA. Translation: AAA32145.2.
V00683 Genomic DNA. Translation: CAA24054.1.
X05056 Genomic DNA. Translation: CAA28727.1.
KP263414 Genomic DNA. Translation: AIZ98889.1.
PIRiA25869. PWBYJ6.
RefSeqiNP_009313.1. NC_001224.1.

Genome annotation databases

EnsemblFungiiQ0085; Q0085; Q0085.
GeneIDi854601.
KEGGisce:Q0085.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01464 Genomic DNA. Translation: AAA32145.2.
V00683 Genomic DNA. Translation: CAA24054.1.
X05056 Genomic DNA. Translation: CAA28727.1.
KP263414 Genomic DNA. Translation: AIZ98889.1.
PIRiA25869. PWBYJ6.
RefSeqiNP_009313.1. NC_001224.1.

3D structure databases

ProteinModelPortaliP00854.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34793. 21 interactions.
DIPiDIP-3038N.
IntActiP00854. 1 interaction.
MINTiMINT-4981504.

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.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiQ0085; Q0085; Q0085.
GeneIDi854601.
KEGGisce:Q0085.

Organism-specific databases

EuPathDBiFungiDB:Q0085.
SGDiS000007268. ATP6.

Phylogenomic databases

GeneTreeiENSGT00390000005568.
HOGENOMiHOG000253874.
InParanoidiP00854.
KOiK02126.
OMAiIYDTIMN.
OrthoDBiEOG7WDNFH.

Enzyme and pathway databases

BioCyciYEAST:G3O-34379-MONOMER.

Miscellaneous databases

PROiP00854.

Family and domain databases

Gene3Di1.20.120.220. 1 hit.
HAMAPiMF_01393. ATP_synth_a_bact.
InterProiIPR000568. ATPase_F0-cplx_asu.
IPR023011. ATPase_F0-cplx_asu_AS.
[Graphical view]
PANTHERiPTHR11410. PTHR11410. 1 hit.
PfamiPF00119. ATP-synt_A. 1 hit.
[Graphical view]
PRINTSiPR00123. ATPASEA.
SUPFAMiSSF81336. SSF81336. 1 hit.
TIGRFAMsiTIGR01131. ATP_synt_6_or_A. 1 hit.
PROSITEiPS00449. ATPASE_A. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Assembly of the mitochondrial membrane system: sequence analysis of a yeast mitochondrial ATPase gene containing the oli-2 and oli-4 loci."
    Macino G., Tzagoloff A.
    Cell 20:507-517(1980) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: D273-10B/A1.
  2. "Sequence of the mitochondrial oli2 gene coding for subunit 6 of the mitochondrial ATPase complex in different strains of Saccharomyces."
    John U.P., Nagley P.
    Nucleic Acids Res. 15:366-366(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: JM6.
  3. "The complete sequence of the mitochondrial genome of Saccharomyces cerevisiae."
    Foury F., Roganti T., Lecrenier N., Purnelle B.
    FEBS Lett. 440:325-331(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 96604 / S288c / FY1679.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 96604 / S288c / FY1679.
  5. "NH2-terminal sequence of the isolated yeast ATP synthase subunit 6 reveals post-translational cleavage."
    Michon T., Galante M., Velours J.
    Eur. J. Biochem. 172:621-625(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 11-32.

Entry informationi

Entry nameiATP6_YEAST
AccessioniPrimary (citable) accession number: P00854
Secondary accession number(s): A0A0A7P052, Q95A27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 27, 2002
Last modified: July 6, 2016
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.