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3.A.2.1.3
H+-translocating F-type ATPase. Evidence of the proximity of ATP synthase subunit 6 is in proximity to the membrane in the supramolecular form (Velours et al., 2011).  The structure of the intact monomeric ATP synthase from the fungus, Pichia angusta, has been solved by electron cryo-microscopy (Vinothkumar et al. 2016). The Mg2+ and Ca2+-dependent enzymes are both active, but exhibit quite different behaviors (Nesci et al. 2017). Dimerization is necessary to create the inner membrane folds (cristae) characteristic of mitochondria.  Using cryo-electron microscopy, Guo et al. 2017 determined the structure of the dimeric FO complex from Saccharomyces cerevisiae at a resolution of 3.6 angstroms. The structure clarifies how the protons travel through the complex, how the complex dimerizes, and how the dimers bend the membrane to produce cristae. The crystal structure of the c-subunit ring with bound oligomycin revealed the inhibitor docked on the outer face of the proton-binding sites, deep in the transmembrane region (Zhou and Faraldo-Gómez 2018). A high resolution (3.7 Å) structure of the entire monomeric ATPase has been solved by cryo EM, suggesting how it is inhibited by oligomycin (Srivastava et al. 2018).  Absence of the e and g subunits decreases conductance of the F-ATP synthase channel about tenfold. Ablation of the first TMS of subunit b, which creates a distinct lateral domain with e and g, further affected channel activity. Thus, F-ATP synthase e, g and b subunits create a domain within the membrane that is critical for the generation of the high-conductance channel that is a prime candidate for formation of the permeability transition pore (PTP). Subunits e and g are only present in eukaryotes and may have evolved to confer this novel function to F-ATP synthases (Carraro et al. 2018). The translation rate of all yeast mitochondrial mRNAs, including all F-type ATPase subunits has been studied (Chicherin et al. 2021). Attenuated ADP-inhibition of F0F1 ATPase mitigates manifestations of mitochondrial dysfunction in yeast (Lapashina et al. 2022).

Accession Number:P00854
Protein Name:ATP6 aka OLI2 aka OLI4 aka PHO1 aka Q0085
Length:259
Molecular Weight:29099.00
Species:Saccharomyces cerevisiae (Baker's yeast) [4932]
Number of TMSs:7
Location1 / Topology2 / Orientation3: Mitochondrion inner membrane1 / Multi-pass membrane protein2
Substrate hydron

Cross database links:

DIP: DIP-3038N
RefSeq: NP_009313.1   
Entrez Gene ID: 854601   
Pfam: PF00119   
KEGG: sce:Q0085   

Gene Ontology

GO:0016021 C:integral to membrane
GO:0000276 C:mitochondrial proton-transporting ATP synth...
GO:0015078 F:hydrogen ion transmembrane transporter acti...
GO:0015986 P:ATP synthesis coupled proton transport

References (4)

[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.et.al.   6446405
[2] “Sequence of the mitochondrial oli2 gene coding for subunit 6 of the mitochondrial ATPase complex in different strains of Saccharomyces.”  John U.P.et.al.   2950378
[3] “The complete sequence of the mitochondrial genome of Saccharomyces cerevisiae.”  Foury F.et.al.   9872396
[4] “NH2-terminal sequence of the isolated yeast ATP synthase subunit 6 reveals post-translational cleavage.”  Michon T.et.al.   2894987
Structure:
6B2Z   6B8H   6CP3   6CP5   6CP6   6CP7   6WTD     

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MFNLLNTYIT SPLDQFEIRT LFGLQSSFID LSCLNLTTFS LYTIIVLLVI TSLYTLTNNN 
61:	NKIIGSRWLI SQEAIYDTIM NMTKGQIGGK NWGLYFPMIF TLFMFIFIAN LISMIPYSFA 
121:	LSAHLVFIIS LSIVIWLGNT ILGLYKHGWV FFSLFVPAGT PLPLVPLLVI IETLSYFARA 
181:	ISLGLRLGSN ILAGHLLMVI LAGLTFNFML INLFTLVFGF VPLAMILAIM MLEFAIGIIQ 
241:	GYVWAILTAS YLKDAVYLH