Kress W Maglica Z Weber-Ban E 2009 Clp proteases are the most widespread energy-dependent proteases in bacteria. Their two-component architecture of protease core and ATPase rings results in an inventory of several Clp protease complexes that often coexist. Here, we present insights into Clp protease function, from their assembly to substrate recruitment and processing, and how this is coupled to the expense of energy. https://sonar.ch/global/documents/164324 eng info:eu-repo/semantics/altIdentifier/doi/10.1016/j.resmic.2009.08.006 info:eu-repo/semantics/altIdentifier/pmid/19732826 Research in microbiology. - 2009 Bacteria Endopeptidase Clp Models, Molecular Molecular Chaperones Substrate Specificity Clp chaperone-proteases: structure and function. http://purl.org/coar/resource_type/c_6501