Abstract:DegP, also known as HtrA, is a protein widely distributed in eukaryotic and prokaryotic cells. It has both protease activity and chaperone activity. On one hand, DegP forms a capsule-like structure to perform its chaperone function, called "Cage assembly". On the other hand, the protease activity of DegP depends on protease active site and PDZ1 domain, called "molecular ruler". In Gram-negative bacteria periplasm, DegP protects misfolded proteins or degrades denatured proteins. For example, DegP takes part in the transport of outer membrane proteins has been well-studied to prove its functions. Additionally, DegP can be secreted to extracellular and participates in the regulation of biofilm formation. In this way, DegP endows the ability to survive from the harsh environments on bacteria. In this review we summarized the structures and functions of DegP. It provides new insights into vitro activities of DegP and how DegP works as the final step in protein quality control system.