{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Reinhardt L"],"funding":["Deutsche Forschungsgemeinschaft"],"pagination":["e0141322"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9765437"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(6)"],"pubmed_abstract":["Clp proteases consist of a proteolytic, tetradecameric ClpP core and AAA+ Clp-ATPases. Streptomycetes, producers of a plethora of secondary metabolites, encode up to five different ClpP homologs, and the composition of their unusually complex Clp protease machinery has remained unsolved. Here, we report on the composition of the housekeeping Clp protease in <i>Streptomyces</i>, consisting of a heterotetradecameric core built of ClpP1, ClpP2, and the cognate Clp-ATPases ClpX, ClpC1, or ClpC2, all interacting with ClpP2 only. Antibiotic acyldepsipeptides (ADEP) dysregulate the Clp protease for unregulated proteolysis. We observed that ADEP binds <i>Streptomyces</i> ClpP1, but not ClpP2, thereby not only triggering the degradation of nonnative protein substrates but also accelerating Clp-ATPa"],"journal":["mBio"],"pubmed_title":["Antibiotic Acyldepsipeptides Stimulate the <i>Streptomyces</i> Clp-ATPase/ClpP Complex for Accelerated Proteolysis."],"pmcid":["PMC9765437"],"funding_grant_id":["Project-ID 398967434","Project-ID 390838134","Project-ID 174858087"],"pubmed_authors":["Sieber SA","Sass P","Brotz-Oesterhelt H","Westermann LM","Thomy D","Reinhardt L","Ortega J","Lakemeyer M"],"additional_accession":[]},"is_claimable":false,"name":"Antibiotic Acyldepsipeptides Stimulate the <i>Streptomyces</i> Clp-ATPase/ClpP Complex for Accelerated Proteolysis.","description":"Clp proteases consist of a proteolytic, tetradecameric ClpP core and AAA+ Clp-ATPases. Streptomycetes, producers of a plethora of secondary metabolites, encode up to five different ClpP homologs, and the composition of their unusually complex Clp protease machinery has remained unsolved. Here, we report on the composition of the housekeeping Clp protease in <i>Streptomyces</i>, consisting of a heterotetradecameric core built of ClpP1, ClpP2, and the cognate Clp-ATPases ClpX, ClpC1, or ClpC2, all interacting with ClpP2 only. Antibiotic acyldepsipeptides (ADEP) dysregulate the Clp protease for unregulated proteolysis. We observed that ADEP binds <i>Streptomyces</i> ClpP1, but not ClpP2, thereby not only triggering the degradation of nonnative protein substrates but also accelerating Clp-ATPa","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2026-06-15T06:14:40.511Z","creation":"2026-06-15T03:08:26.863Z"},"accession":"S-EPMC9765437","cross_references":{"pubmed":["36286522"],"doi":["10.1128/mbio.01413-22"]}}