ClpP: a distinctive family of cylindrical energy-dependent serine proteases

FEBS Lett. 2007 Jul 31;581(19):3749-57. doi: 10.1016/j.febslet.2007.04.076. Epub 2007 May 8.


Processes maintaining protein homeostasis in the cell are governed by the activities of molecular chaperones that mainly assist in the folding of polypeptide chains and by a large class of proteases that regulate protein levels through degradation. ClpP proteases define a distinctive family of cylindrical, energy-dependent serine proteases that are highly conserved throughout bacteria and eukaryota. They typically interact with ATP-dependent AAA+ chaperones that bind and unfold target substrates and then translocate them into ClpP for degradation. Structural and functional studies have provided a detailed view of the mechanism of function of this class of proteases.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adenosine Triphosphate / chemistry
  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Endopeptidase Clp / chemistry*
  • Endopeptidase Clp / metabolism
  • Humans
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / metabolism
  • Molecular Sequence Data
  • Plant Proteins / chemistry
  • Plant Proteins / metabolism
  • Protein Conformation
  • Serine Endopeptidases / chemistry*
  • Serine Endopeptidases / metabolism


  • Bacterial Proteins
  • Molecular Chaperones
  • Plant Proteins
  • Adenosine Triphosphate
  • Serine Endopeptidases
  • Endopeptidase Clp