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Information on EC 7.1.2.2 - H+-transporting two-sector ATPase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P00830
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7.1.2.2 H+-transporting two-sector ATPaseIUBMB Comments
A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (Fo, Vo, Ao) and a cytoplasmic-compartment sector (F1, V1, A1). The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. Within this complex, the gamma- and epsilon-subunits, as well as the 9--12 c subunits rotate by consecutive 120_degree_ angles and perform parts of ATP synthesis. This movement is driven by the H+ electrochemical potential gradient. The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H+ rather than synthesize ATP.
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Word Map
- 7.1.2.2
-
acidification
- adp
- bafilomycin
- lysosomal
-
electrochemical
- triphosphate
- beta-subunits
- endosomes
- succinate
-
bioenergetics
- stalk
-
acidify
- osteoclast
- thylakoids
-
submitochondrial
- tubule
-
proteolipids
- resorption
- beef
-
dissipation
- vanadate
-
atp-driven
- mtdna
- acidosis
-
antiporter
-
subcomplexes
- photosystems
-
electrogenic
- mgatp
-
proteoliposomes
- cristae
-
intercalated
-
torque
-
oxphos
-
multisubunit
- presequence
-
chromaffin
-
endomembrane
-
membrane-embedded
-
proton-pumping
-
supercomplexes
-
gamma-subunits
-
ceroid
- valinomycin
-
b-subunits
- adenosinetriphosphatase
- nigericin
-
light-driven
- leigh
- prorenin
- drug development
- synthesis
- molecular biology
- medicine
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
atp synthase, v-atpase, f1-atpase, h+-atpase, mitochondrial atpase, vacuolar h(+)-atpase, vacuolar atpase, lipid-binding protein, vacuolar h+-atpase, f0f1-atpase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
15 kDa mediatophore protein
-
-
-
-
32 kDa accessory protein
-
-
-
-
59 kDa membrane-associated GTP-binding protein
-
-
-
-
A6L
-
-
-
-
ATP synthase
ATP synthase proteolipid P1
-
-
-
-
ATP synthase proteolipid P2
-
-
-
-
ATP synthase proteolipid P3
-
-
-
-
bacterial Ca2+/Mg2+ ATPase
-
-
-
-
BN59
-
-
-
-
C7-1 protein
-
-
-
-
CGI-11
-
-
-
-
chloroplast ATPase
-
-
-
-
coupling factors (F0,F1 and CF1)
-
-
-
-
Dicyclohexylcarbodiimide-binding protein
-
-
-
-
Ductin
-
-
-
-
DVA41
-
-
-
-
F0F1-ATPase
F1-ATPase
F1F0 ATPase
-
-
-
-
F1F0H+-ATPase
-
-
-
-
H+-ATP synthase
-
the multisubunit complex is built by two major functional domains: the membrane-embedded Fo-ATPase (a and 8c subunits) and the membrane extrinsic catalytic F1-ATPase (3alpha, 3beta, gamma, delta and epsilon subunits) domains
H+-ATPase
-
-
-
-
H+-translocating ATPase
-
-
-
-
H+-transporting ATPase
-
-
-
-
HATPL
-
-
-
-
HO57
-
-
-
-
Invasion protein invC
-
-
-
-
Isoform HO68
-
-
-
-
Isoform VA68
-
-
-
-
Lipid-binding protein
-
-
-
-
M40
-
-
-
-
mitochondrial ATPase
-
-
-
-
My032 protein
-
-
-
-
Oligomycin sensitivity conferral protein
-
-
-
-
OSCP
-
-
-
-
P31
-
-
-
-
P39
-
-
-
-
Physophilin
-
-
-
-
PKIWI505
-
-
-
-
Protein bellwether
-
-
-
-
Sul-ATPase alpha
-
-
-
-
Sul-ATPase beta
-
-
-
-
SUL-ATPase epsilon
-
-
-
-
Sul-ATPase gamma
-
-
-
-
UV-inducible PU4 protein
-
-
-
-
V-ATPase
-
-
V-ATPase 28 kDa accessory protein
-
-
-
-
V-ATPase 40 kDa accessory protein
-
-
-
-
V-ATPase 41 KDa accessory protein
-
-
-
-
V-ATPase 9.2 kDa membrane accessory protein
-
-
-
-
V-ATPase S1 accessory protein
-
-
-
-
VEG100
-
-
-
-
VEG31
-
-
-
-
Vegetative protein 100
-
-
-
-
Vegetative protein 31
-
-
-
-
VHA16K
-
-
-
-
YOPS secretion ATPase
-
-
-
-
ATP synthase
-
-
-
-
F0F1-ATPase
-
-
-
-
F1-ATPase
-
-
-
-
F1-ATPase
-
isolated extrinsic part of ATP synthase, extrinsic F1 domain alpha3beta3gammadeltaepsilon in mitochondria
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
transmembrane transport
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (H+-transporting)
A multisubunit non-phosphorylated ATPase that is involved in the transport of ions. Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (Fo, Vo, Ao) and a cytoplasmic-compartment sector (F1, V1, A1). The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases. All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits. Within this complex, the gamma- and epsilon-subunits, as well as the 9--12 c subunits rotate by consecutive 120_degree_ angles and perform parts of ATP synthesis. This movement is driven by the H+ electrochemical potential gradient. The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H+ rather than synthesize ATP.
CAS REGISTRY NUMBER
COMMENTARY
9000-83-3
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
r
additional information
?
-
Gly133 of beta subunit is important for structural stability, Glu222 and Arg293 are important for catalytic cooperativity
-
-
?
additional information
?
-
-
Gly133 of beta subunit is important for structural stability, Glu222 and Arg293 are important for catalytic cooperativity
-
-
?
additional information
?
-
-
other reactions catalyzed by ATPase and its components
-
-
?
additional information
?
-
-
bacterially expressed B subunit from the yeast Saccharomyces cerevisiae binds actin filaments. Actin-binding activity confers on the B subunit of yeast a function that is distinct from its role in the enzymatic activity of the proton pump
-
-
?
additional information
?
-
-
the enzyme B subunit binds purified polymerized actin from rabbit muscle
-
-
?
additional information
?
-
-
F1-ATP synthase beta-subunit binds specifically to the human pigment epithelium-derived factor and acts as a cell-surface receptor in retinal cells. PEDF is a ligand for endothelial cell-surface F1Fo-ATP synthase
-
-
?
additional information
?
-
electron density at the catalytic sites of F1 ATPase in the absence of nucleotides, overview
-
-
?
additional information
?
-
-
electron density at the catalytic sites of F1 ATPase in the absence of nucleotides, overview
-
-
?
additional information
?
-
-
subunit D plays an important role in coupling of proton transport and ATP hydrolysis
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O + H+[side 1]
ADP + phosphate + H+[side 2]
-
-
-
-
?
ATP + H2O + H+/in
ADP + phosphate + H+/out
-
-
-
-
?
additional information
?
-
-
bacterially expressed B subunit from the yeast Saccharomyces cerevisiae binds actin filaments. Actin-binding activity confers on the B subunit of yeast a function that is distinct from its role in the enzymatic activity of the proton pump
-
-
?
additional information
?
-
-
F1-ATP synthase beta-subunit binds specifically to the human pigment epithelium-derived factor and acts as a cell-surface receptor in retinal cells. PEDF is a ligand for endothelial cell-surface F1Fo-ATP synthase
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
intrinsic inhibitory peptide IF1
-
from Saccharomyces cerevisiae, the N-terminal part of the inhibitory peptide IF1 interacts with the central gamma subunit of mitochondrial isolated extrinsic part of ATP synthase in the inhibited complex. Kinetics of inhibition of the isolated and membrane-bound enzymes with IF1 modified in N-terminal extremity, i.e. IF1-Nter, overview. IF1-Nter plays no role in the recognition step but contributes to stabilize the inhibited complex. Its binding to the enzyme is not affected by truncations or fusion with PsaE, a 8 kDa globular-like protein
-
pigment epithelium-derived factor
-
competes with angiostatin. Human PEDF significantly reduces the amount of extracellular ATP produced by endothelial cells, in agreement with direct interactions between cell-surface ATP synthase and PEDF, 53% inhibition at 10 nM
-
SidK
-
a protein of Legionella pneumophila, an intracellular pathogen, specifically targets host v-ATPase. SidK interacts via an N-terminal portion with VatA, a key component of the proton pump leading to the inhibition of ATP hydrolysis and proton translocation. SidK inhibits vacuole acidification and impairs the ability of the cells to digest non-pathogenic Escherichia coli
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
binding kinetics of pigment epithelium-derived factor to cell surface F1-ATP synthase, overview
-
additional information
additional information
-
kinetic model of the F1-ATPase, dependence of kinetic behaviour on the ATP concentration, overview
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
oligomerization of ATP synthase is critical for the morphology of the inner mitochondrial membrane because it supports the generation of tubular cristae membrane domains, overview. Association of individual F1Fo-ATP synthase complexes is mediated by the membrane-embedded Fo-part
-
the enzyme is found in monomeric, dimeric and higher oligomeric forms in the inner mitochondrial membrane. Two small proteins of the membrane-embedded Fo-domain subunits e and g are dimer-specific subunits of yeast ATP synthase and are required for stabilization of the dimers
-
mitochondrial translation of the Saccharomyces cerevisiae Atp6p subunit of F1-F0 ATP synthase is regulated by the F1 ATPase
-
V-ATPase consists of a cytoplasmic domain V1 and a transmembrane domain V0. Both domains contain several subunits. The V0 transmembrane domain consists of subunits a, c, c', c'' and d
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
-
the enzyme modulates signaling pathways that activate the mitohormetic response, namely ATP, reactive oxygen species, and target of rapamycin
physiological function
additional information
malfunction
-
deletion of the 3'-UTR in the ATP2 gene leads to deficient protein import and reduced ATP synthesis, mtDNA depletion and respiratory dysfunction
malfunction
-
expression of Atp6p in HeLa cells depleted of the F1 beta subunit. Instead of being translationally downregulated, HeLa cells lacking F1 degrade Atp6p, thereby preventing proton leakage across the inner membrane. Yeast mutants lacking beta subunit have stable aggregated F1 alpha subunit in the mitochondrial matrix
physiological function
-
F1Fo-ATP synthase is a key enzyme of oxidative phosphorylation that is localized in the inner membrane of mitochondria. It uses the energy stored in the proton gradient across the inner mitochondrial membrane to catalyze the synthesis of ATP from ADP and phosphate
physiological function
-
v-ATPase is a multi-subunit machinery primarily responsible for organelle acidification in eukaryotic cells
additional information
-
pigment epithelium-derived factor-mediated inhibition of ATP synthase may form part of the biochemical mechanisms by which PEDF exerts its antiangiogenic activity
additional information
-
ATP2 mRNA is no Puf3p target and belongs to the class of Puf3-independent mitochondria-localized mRNAs
additional information
-
F1-ATPase is the isolated extrinsic part of ATP synthase, the extrinsic F1 domain alpha3beta3gammadeltaepsilon in mitochondria
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
phylogenetic analysis of the homologous F0F1-ATPases of bacteria, chloroplasts and mitochondria
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
-
oligomerization of ATP synthase is critical for the morphology of the inner mitochondrial membrane because it supports the generation of tubular cristae membrane domains, overview. Association of individual F1Fo-ATP synthase complexes is mediated by the membrane-embedded Fo-part. Subunits e, g, k, and i are involved in the stepwise assembly of F1Fo-ATP synthase dimers and oligomers. Subunit i facilitates the incorporation of newly synthesized subunits into ATP synthase complexes, while subunit k stabilizes the dimer. Formation of one dimeric form of ATP synthase is inhibited in the absence of subunit. Detailed overview i
additional information
additional information
-
molecular weight of the subunits, biogenesis of the enzyme depends on a close cooperation of mitochondrial and cytoplasmic synthesis
additional information
-
subunits alpha, beta, gamma, delta and sigma of the purified chimeric enzyme, with the stoichiometry of 3:3:1:1:1, SDS-PAGE
additional information
-
V-ATPase consists of a cytoplasmic domain V1 and a transmembrane domain V0. Both domains contain several subunits. The V0 transmembrane domain consists of subunits a, c, c', c'' and d. Proton translocation takes place at the interface of subunit a and the rotating c, c', and c'' subunits. NMR structure determination, 3D structure of a peptide derived from the putative transmembrane segment 7 of subunit a from H+-V-ATPase determined by solution state NMR in SDS solution. A stable helix is formed from L736 up to and including Q745, the lumenal half of the putative TM7. The helical region extends well beyond A738. The secondary structure of the peptide depends on the pH and the type of detergent used, overview
additional information
-
the enzyme is found in monomeric, dimeric and higher oligomeric forms in the inner mitochondrial membrane. Dimerization of ATP synthase complexes is a prerequisite for the generation of larger oligomers that promote membrane bending and formation of tubular cristae membranes. Two small proteins of the membrane-embedded Fo-domain subunits e and g are dimer-specific subunits of yeast ATP synthase and are required for stabilization of the dimers. Subunits e and g sequentially assemble with monomeric ATP synthase to form a dimerization-competent primed monomer, overview
additional information
-
beta-F1-ATPase is the catalytic subunit of the mitochondrial H+-ATP synthase
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified native nucleotide-free F1 ATPase, enzyme in 0.25 M sucrose, 0.2 M NaCl, 0.05 M Tris-Cl, 1mM EDTA, 2 mM sodium diphosphate, pH 8.0, 0.5 mM phenylmethylsulfonyl fluoride, crystallization buffer with PEG 6000 concentration 6.25% and 2 mM Na diphosphate replacing the nucleotides, X-ray diffraction structure determination and analysis at 3.6 A resolution, molecular replacement
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E222K
modification of beta-subunit, mutation assembles an F1 of normal size that is catalytically inactive
G133D
modification of beta-subunit, mutation correlates with an assembly-defective phenotype that is characterized by the acumulation of the F1 alpha and beta subunits in large protein aggregates
G227D
modification of beta-subunit, mutation correlates with an assembly-defective phenotype that is characterized by the acumulation of the F1 alpha and beta subunits in large protein aggregates
P179L
modification of beta subunit, mutation correlates with an assembly-defective phenotype that is characterized by the acumulation of the F1 alpha and beta subunits in large protein aggregates
R293K
modification of beta-subunit, mutation assembles an F1 of normal size that is catalytically inactive
A49T/R60S/W83R/Q132H/V163I/H236N/L296M/T338A
-
the mutant is resistant towards zinc
D46E/F50L/S198R/D217V/Y238F/K298E/T345A/T405M/L418P
-
the mutant is resistant towards zinc
E127V/A168T/L314Q/H344Y/H351Q
-
the mutant is resistant towards zinc
E76V/A79P/N164D/E340D/Q341K/H344Y/I403V
-
the mutant is resistant towards zinc
G80D/E220V/M221V
-
the mutant shows 10% of wild type ATPase activity
G80D/K209E
-
the double mutant shows increased coupling efficiency of proton transport and ATPase activity
H88L/I193S/Q209H/V303A/D337Y/I417N
-
the mutant is resistant towards zinc
I188N/I173N/A232T
-
the mutant shows 20% of wild type ATPase activity
L149V/E182D/D249G
-
the mutant shows 35% of wild type ATPase activity
M221V
N56T/P110H/I176V/L307I/N372D/N415D
-
the mutant is resistant towards zinc
Q98H/K299R/K310N/H351R/K362N/Q379K
-
the mutant is resistant towards zinc
R735A
-
the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
R735C
-
the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
R735E
-
the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
R735K
-
the mutant, although completely inactive for proton transport, retains 24% of wild type ATPase activity
R735L
-
the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
R735N
-
the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
R735Q
-
the mutant is fully assembled but is totally devoid of proton transport and ATPase activity
R762A
-
the mutant retains full wild type ATPase activity and about 90% of wild type proton transport activity
R762K
-
the mutant retains about 80% of wild type ATPase activity and about 80% of wild type proton transport activity
R762L
-
the mutant retains about 75% of wild type ATPase activity and about 85% of wild type proton transport activity
R799A
-
the mutant is almost totally devoid of proton transport and ATPase activity
R799K
-
the mutant, which is almost completely inactive for proton transport, retains about 10% of wild type ATPase activity
R799L
-
the mutant is totally devoid of proton transport and ATPase activity
V71D/E220V
additional information
M221V
-
the mutation leads to significant uncoupling of proton transport and ATPase activity
V71D/E220V
-
the mutations lead to significant uncoupling of proton transport and ATPase activity
additional information
-
hybrid vacuolar H+-ATPase containing the mouse testis-specific E1 isoform and yeast subunits shows a defective assembly, reversible defect of the hybrid V-ATPase. Glucose depletion, known to dissociate V1 from Vo in yeast, has only a slight effect on the hybrid at acidic pH. The domain between Lys26 and Val83 of E1, which contains eight residues not conserved between E1 and E2, is responsible for the unique properties of the hybrid, while the E2 domain in E2/VMA4-2 chimera corresponding to between Lys26 and Val83 of E1 has no effect on the assembly of the V-ATPase. The mutant shows a temperature-sensitive defect
additional information
-
mutations in the profilin-like region, actin-binding domain, of the B subunit reduced or eliminated the actin-binding activity. Mutants assemble properly with endogenous yeast subunits when expressed in B subunit-null yeast, and bafilomycin-sensitive ATPase activity is not significantly different from yeast transformed with wild-type B subunit. Yeast containing the mutant subunits grow as well at pH 7.5 as wild-type. Mutant B subunits are more sensitive to cycloheximide and wortmannin than those transformed with wild-type B subunits
additional information
-
human pigment epithelium-derived factor is immobilized on the surface of a CM5 sensor chip revealing binding response units for the yeast F1-ATPase showing specific, reversible and concentration-response binding of F1 to PEDF
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
the recombinant hybrid enzyme Vo subunit a epitope is exposed to the corresponding antibody at 37 °C, but becomes inaccessible at 30 °C, showing apparent uncoupling between ATPase and proton transport
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant V-ATPase B subunits as maltose-binding protein fusion proteins from Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ATP2 gene, coding for the beta subunit of the mitochondrial F1-ATPase
ATPase genetically modified to include a His6 Ni affinity tag on the amino end of the mature beta-subunit, imported into mitochondrion, expression of the the purified chimeric enzyme in Escherichia coli DMY301
-
expression of a hybrid enzyme, formed by a mouse E1 isozyme and yeast subunits, in DELTAvma4 cells
-
expression of Atp6p in HeLa cells depleted of the F1 beta subunit. Instead of being translationally downregulated, HeLa cells lacking F1 degrade Atp6p, thereby preventing proton leakage across the inner membrane
-
expression of wild-type and mutant V-ATPase B subunits as maltose-binding protein fusion proteins in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of the catalytic subunit beta-F1-ATPase is tightly regulated at post-transcriptional levels during mammalian development and in the cell cycle
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
-
the enzyme is a target for development of specific inhibitors
additional information
-
simple and inexpensive method to grow yeast to high density and purify the mitochondrial F1-ATPase quickly and efficiently
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Liang, Y.; Ackerman, S.H.
Characterization of mutation in the beta subunit of the mitochondrial F1-ATPase that produce defects in enzyme catalysis and assembly
J. Biol. Chem.
271
26522-26528
1996
Saccharomyces cerevisiae (P00830), Saccharomyces cerevisiae
Penefsky, H.S.
Mitochondrial and chloroplast ATPases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
10
375-429
1974
Bos taurus, Saccharomyces cerevisiae, Magnusiomyces magnusii, Euglena gracilis, Rattus norvegicus, Spinacia oleracea
-
Criddle, R.S.; Johnston, R.F.; Stack, R.J.
Mitochondrial ATPases
Curr. Top. Bioenerg.
9
89-145
1979
Bos taurus, Saccharomyces cerevisiae, Escherichia coli, Schizosaccharomyces pombe
-
Sebald, W.
Biogenesis of mitochondrial ATPase
Biochim. Biophys. Acta
463
1-27
1977
Bos taurus, Saccharomyces cerevisiae, Neurospora crassa, Rattus norvegicus, Schizosaccharomyces pombe
Futai, M.; Kanazawa, H.
Structure and function of proton-translocating adenosine triphosphatase (F0F1): Biochemical and molecular biological approaches
Microbiol. Rev.
47
285-312
1983
Bos taurus, Saccharomyces cerevisiae, Escherichia coli, Mus musculus, Spinacia oleracea, Bacillus sp. PS3, Zea mays
Blair, A.; Ngo, L.; Park, J.; Paulsen, I.T.; Saier, M.H.
Phylogenetic analyses of the homologous transmembrane channel-forming proteins of the F0F1-ATPases of bacteria, chloroplasts and mitochondria
Microbiology
142
17-32
1996
Anabaena sp., Apis mellifera, Ascaris suum, Aspergillus nidulans, Cytobacillus firmus, Priestia megaterium, Balaenoptera physalus, Beta vulgaris, Bos taurus, Brassica napus, Saccharomyces cerevisiae, Caenorhabditis elegans, Candida parapsilosis, Cyprinus carpio, Cricetulus griseus, Bipolaris maydis, Cricetulus sp., Drosophila melanogaster, Escherichia coli, Euglena gracilis, Homo sapiens, Locusta migratoria, Marchantia polymorpha, Mus musculus, Neurospora crassa, Nicotiana tabacum, Trieres chinensis, Oenothera berteroana, Oryza sativa, Paracentrotus lividus, Phoca vitulina, Pisaster ochraceus, Pisum sativum, Podospora anserina, Propionigenium modestum, Rattus norvegicus, Rhodospirillum rubrum, Schizosaccharomyces pombe, Spinacia oleracea, Synechococcus sp., Bacillus sp. PS3, Triticum aestivum, Trypanosoma brucei, Vibrio alginolyticus, Xenopus laevis, Zea mays
Mueller, D.M.; Puri, N.; Kabaleeswaran, V.; Terry, C.; Leslie, A.G.; Walker, J.E.
Ni-chelate-affinity purification and crystallization of the yeast mitochondrial F1-ATPase
Protein Expr. Purif.
37
479-485
2004
Saccharomyces cerevisiae, Saccharomyces cerevisiae DK8
Hayashi, K.; Sun-Wada, G.H.; Wada, Y.; Nakanishi-Matsui, M.; Futai, M.
Defective assembly of a hybrid vacuolar H(+)-ATPase containing the mouse testis-specific E1 isoform and yeast subunits
Biochim. Biophys. Acta
1777
1370-1377
2008
Saccharomyces cerevisiae, Mus musculus
Vermeer, L.S.; Reat, V.; Hemminga, M.A.; Milon, A.
Structural properties of a peptide derived from H+-V-ATPase subunit a
Biochim. Biophys. Acta
1788
1204-1212
2009
Saccharomyces cerevisiae
Zuo, J.; Vergara, S.; Kohno, S.; Holliday, L.S.
Biochemical and functional characterization of the actin-binding activity of the B subunit of yeast vacuolar H+-ATPase
J. Exp. Biol.
211
1102-1108
2008
Saccharomyces cerevisiae
Johnson, R.M.; Allen, C.; Melman, S.D.; Waller, A.; Young, S.M.; Sklar, L.A.; Parra, K.J.
Identification of inhibitors of vacuolar proton-translocating ATPase pumps in yeast by high-throughput screening flow cytometry
Anal. Biochem.
398
203-211
2010
Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741
Notari, L.; Arakaki, N.; Mueller, D.; Meier, S.; Amaral, J.; Becerra, S.P.
Pigment epithelium-derived factor binds to cell-surface F1-ATP synthase
FEBS J.
277
2192-2205
2010
Bos taurus, Saccharomyces cerevisiae
Kabaleeswaran, V.; Shen, H.; Symersky, J.; Walker, J.E.; Leslie, A.G.; Mueller, D.M.
Asymmetric structure of the yeast F1 ATPase in the absence of bound nucleotides
J. Biol. Chem.
284
10546-10551
2009
Saccharomyces cerevisiae (P07251), Saccharomyces cerevisiae
Billack, B.; Pietka-Ottlik, M.; Santoro, M.; Nicholson, S.; Mlochowski, J.; Lau-Cam, C.
Evaluation of the antifungal and plasma membrane H+-ATPase inhibitory action of ebselen and two ebselen analogs in S. cerevisiae cultures
J. Enzyme Inhib. Med. Chem.
25
312-317
2010
Saccharomyces cerevisiae, Saccharomyces cerevisiae AH109
Wagner, K.; Rehling, P.; Sanjuan Szklarz, L.K.; Taylor, R.D.; Pfanner, N.; van der Laan, M.
Mitochondrial F1Fo-ATP synthase: the small subunits e and g associate with monomeric complexes to trigger dimerization
J. Mol. Biol.
392
855-861
2009
Saccharomyces cerevisiae
Wagner, K.; Perschil, I.; Fichter, C.D.; van der Laan, M.
Stepwise assembly of dimeric F1Fo-ATP synthase in mitochondria involves the small Fo-subunits k and i
Mol. Biol. Cell
21
1494-1504
2010
Saccharomyces cerevisiae
Xu, L.; Shen, X.; Bryan, A.; Banga, S.; Swanson, M.S.; Luo, Z.Q.
Inhibition of host vacuolar H+-ATPase activity by a Legionella pneumophila effector
PLoS Pathog.
6
e1000822
2010
Saccharomyces cerevisiae
Andrianaivomananjaona, T.; Moune-Dimala, M.; Herga, S.; David, V.; Haraux, F.
How the N-terminal extremity of Saccharomyces cerevisiae IF1 interacts with ATP synthase: a kinetic approach
Biochim. Biophys. Acta
1807
197-204
2011
Saccharomyces cerevisiae
Willers, I.M.; Cuezva, J.M.
Post-transcriptional regulation of the mitochondrial H+-ATP synthase: a key regulator of the metabolic phenotype in cancer
Biochim. Biophys. Acta
1807
543-551
2011
Saccharomyces cerevisiae, Homo sapiens, Rattus norvegicus
Rak, M.; McStay, G.P.; Fujikawa, M.; Yoshida, M.; Manfredi, G.; Tzagoloff, A.
Turnover of ATP synthase subunits in F1-depleted HeLa and yeast cells
FEBS Lett.
585
2582-2586
2011
Saccharomyces cerevisiae, Homo sapiens
Esparza-Molto, P.B.; Nuevo-Tapioles, C.; Cuezva, J.M.
Regulation of the H+-ATP synthase by IF1 a role in mitohormesis
Cell. Mol. Life Sci.
74
2151-2166
2017
Saccharomyces cerevisiae
Xu, T.; Forgac, M.
Subunit D (Vma8p) of the yeast vacuolar H+-ATPase plays a role in coupling of proton transport and ATP hydrolysis
J. Biol. Chem.
275
22075-22081
2000
Saccharomyces cerevisiae, Saccharomyces cerevisiae KHY105
Finnigan, G.C.; Cronan, G.E.; Park, H.J.; Srinivasan, S.; Quiocho, F.A.; Stevens, T.H.
Sorting of the yeast vacuolar-type, proton-translocating ATPase enzyme complex (V-ATPase) identification of a necessary and sufficient Golgi/endosomal retention signal in Stv1p
J. Biol. Chem.
287
19487-19500
2012
Saccharomyces cerevisiae, Saccharomyces cerevisiae SF838-1Dalpha
EXTERNAL LINKS (specific for EC-Number 7.1.2.2)
Transporter Classification Database (TCDB): 3.A.2.2.7, 3.A.2.1.13, 3.A.6.2.1, 3.A.2.3.3, 3.A.2.1.1, 3.A.2.2.5, 3.A.2.2.1, 3.A.2.1.14, 3.A.2.1.15, 3.A.2.3.1, 3.A.2.2.6, 3.A.2.1.7, 3.A.2.1.3, 3.A.2.2.4, 3.A.2.2.3, 3.A.2.1.4, 3.A.2.2.8, 3.A.2.1.11, 9.B.94.2.1, 3.A.2.3.2, 3.A.2.1.6, 3.A.2.1.12
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