Literature summary for 7.4.2.8 extracted from

Gazi, A.D.; Bastaki, M.; Charova, S.N.; Gkougkoulia, E.A.; Kapellios, E.A.; Panopoulos, N.J.; Kokkinidis, M.
Evidence for a coiled-coil interaction mode of disordered proteins from bacterial type III secretion systems (2008), J. Biol. Chem., 283, 34062-34068.

Search for more literature for 7.4.2.8

Activating Compound

Activating Compound	Comment	Organism	Structure
FliH	the stimulation of the FliI ATPase activity by FliJ occurs either via a transient FliJ-FliI interaction or via interactions of FliJ with other flagellar components, e.g. the FliH protein, the flagellar counterpart of HrpE, with a predicted coiled-coil structure. FliH is a known regulator of FliI activity that binds to FliI and suppresses its oligomerization and ATPase activity	Pseudomonas syringae

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O	Pseudomonas syringae	FliH regulates the activity of the FliI ATPase and binds to FliI suppressing its oligomerization and ATPase activity. At the level of the export ATPase complex, two activities have been reported for FliJ, i.e. a T3SS chaperone escort activity and a stimulation of the FliI ATPase activity	ADP + phosphate	-	?

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas syringae	-	pv. phaseolicola	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O	-	Pseudomonas syringae	ADP + phosphate	-	?
ATP + H2O	FliH regulates the activity of the FliI ATPase and binds to FliI suppressing its oligomerization and ATPase activity. At the level of the export ATPase complex, two activities have been reported for FliJ, i.e. a T3SS chaperone escort activity and a stimulation of the FliI ATPase activity	Pseudomonas syringae	ADP + phosphate	-	?

Synonyms

Synonyms	Comment	Organism
FliI	-	Pseudomonas syringae

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)