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Literature summary for 7.1.2.1 extracted from

  • 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 (2010), PLoS Pathog., 6, e1000822.
    View publication on PubMedView publication on EuropePMC

Inhibitors

Inhibitors Comment Organism Structure
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 Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining
lysosome
-
Saccharomyces cerevisiae 5764
-
vacuole
-
Saccharomyces cerevisiae 5773
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + H+/in Saccharomyces cerevisiae
-
ADP + phosphate + H+/out
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
-
Saccharomyces cerevisiae ADP + phosphate + H+/out
-
?

Synonyms

Synonyms Comment Organism
V-ATPase
-
Saccharomyces cerevisiae
vacuolar H+-ATPase
-
Saccharomyces cerevisiae

General Information

General Information Comment Organism
physiological function v-ATPase is a multi-subunit machinery primarily responsible for organelle acidification in eukaryotic cells Saccharomyces cerevisiae