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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: -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

Keywordsi

Biological processATP 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

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transmembranei36 – 56HelicalSequence analysisAdd BLAST21
Transmembranei92 – 112HelicalSequence analysisAdd BLAST21
Transmembranei125 – 145HelicalSequence analysisAdd BLAST21
Transmembranei150 – 170HelicalSequence analysisAdd BLAST21
Transmembranei191 – 211HelicalSequence analysisAdd BLAST21
Transmembranei216 – 236HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000026261 – 10Removed in mature form1 Publication10
ChainiPRO_000000262711 – 259ATP synthase subunit aAdd BLAST249

Proteomic databases

PaxDbiP00854
PRIDEiP00854

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, 24 interactors
DIPiDIP-3038N
IntActiP00854, 1 interactor
STRINGi4932.Q0085

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6B2Zelectron microscopy3.60M/a11-259[»]
6B8Helectron microscopy3.60a/p11-259[»]
6CP3electron microscopy3.80X11-259[»]
6CP5electron microscopy4.20X11-259[»]
6CP6electron microscopy3.60X11-259[»]
6CP7electron microscopy4.10X11-259[»]
ProteinModelPortaliP00854
SMRiP00854
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
OMAiTAGHLLM
OrthoDBiEOG092C5GI0

Family and domain databases

Gene3Di1.20.120.220, 1 hit
HAMAPiMF_01393 ATP_synth_a_bact, 1 hit
InterProiView protein in InterPro
IPR000568 ATP_synth_F0_asu
IPR023011 ATP_synth_F0_asu_AS
IPR035908 F0_ATP_A_sf
PfamiView protein in Pfam
PF00119 ATP-synt_A, 1 hit
PRINTSiPR00123 ATPASEA
SUPFAMiSSF81336 SSF81336, 1 hit
TIGRFAMsiTIGR01131 ATP_synt_6_or_A, 1 hit
PROSITEiView protein in PROSITE
PS00449 ATPASE_A, 1 hit

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)DescriptionActionsGraphical viewLength
Natural varianti171I → M in strain: D273-10B/A1. 1
Natural varianti177F → I in strain: D273-10B/A1. 1
Natural varianti231M → I in strain: D273-10B/A1. 1
Natural varianti241G → S in strain: D273-10B/A1. 1
Natural varianti245A → T in strain: D273-10B/A1. 1
Natural varianti255 – 256AV → TL in strain: D273-10B/A1. 2

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

Similar proteinsi

Entry informationi

Entry nameiATP6_YEAST
AccessioniPrimary (citable) accession number: P00854
Secondary accession number(s): A0A0A7P052, Q95A27
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: May 27, 2002
Last modified: May 23, 2018
This is version 159 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

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