Self-resistance mechanism to acyldepsipeptide antibiotics in the <i>Streptomyces</i> producer.

ABSTRACT: Clp proteases are ubiquitous in bacteria and play an important role in regulatory proteolysis and in maintaining protein homeostasis within the bacterial cell. They consist of a tetradecameric, proteolytic ClpP core and associated AAA+ Clp-ATPases. The Clp system of Streptomyces is unusually complex, comprising up to five ClpP homologs (ClpP1-ClpP5) and three Clp-ATPases (ClpX, ClpC1, and ClpC2). Streptomycetes produce a plethora of secondary metabolites, including potent acyldepsipeptide (ADEP) antibiotics, which target ClpP. We have previously reported on the operation mode of the Streptomyces ClpP1P2 protease and identified a novel clpP gene (named clpP_ADEP) as a resistance determinant encoded near the ADEP biosynthesis gene cluster. However, the m

SUBMITTER: Thomy D 

PROVIDER: S-EPMC12607617 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature