Literature summary extracted from

Gersch, M.; Famulla, K.; Dahmen, M.; Goebl, C.; Malik, I.; Richter, K.; Korotkov, V.S.; Sass, P.; Ruebsamen-Schaeff, H.; Madl, T.; Broetz-Oesterhelt, H.; Sieber, S.A.
AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control (2015), Nat. Commun., 6, 6320.

Activating Compound

EC Number	Activating Compound	Comment	Organism	Structure
3.4.21.92	acyldepsipeptide	acyldepsipeptides in addition to opening the axial pore directly stimulate ClpP activity through cooperative binding	Staphylococcus aureus

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.4.21.92	Staphylococcus aureus	Q2G036	-	-
3.4.21.92	Staphylococcus aureus NCTC 8325	Q2G036	-	-

General Information

EC Number	General Information	Comment	Organism
3.4.21.92	physiological function	both protein and small-molecule activators of ClpP allosterically control the ClpP barrel conformation. Acyldepsipeptides in addition to opening the axial pore directly stimulate ClpP activity through cooperative binding. ClpP activation thus reaches beyond active site accessibility and also involves conformational control of the catalytic residues. Substoichiometric amounts of acyldepsipeptide potently prevent binding of ClpX to ClpP and, at the same time, partially inhibit ClpP through conformational perturbance. The hydrophobic binding pocket is a major conformational regulatory site with implications for both ClpXP proteolysis and acyldepsipeptide -based anti-bacterial activity	Staphylococcus aureus

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Release 2023.1 (January 2023)