Abstract
MecA is a broadly conserved adaptor protein in Gram-positive bacteria, mediating the recognition and degradation of specific target proteins by ClpCP protease complexes. MecA binds target proteins, often through recognition of degradation tags or motifs, and delivers them to the ClpC ATPase, which unfolds and translocates the substrates into the ClpP protease barrel for degradation. MecA activity is tightly regulated through interactions with ClpC ATPase and other factors, ensuring precise control over protein degradation and cellular homeostasis. Beyond proteolysis, emerging evidence highlights a ClpP-independent role of MecA in modulating the function of its targets, including key enzymes and transcriptional factors involved in biosynthetic and metabolic pathways. However, the full scope and mechanisms of ClpP-independent MecA regulation remain unclear, warranting further investigation.