Peptidase C56, PfpI (IPR006286)

Short name: Peptidase_C56

Family relationships



This group of cysteine peptidases form part of the MEROPS peptidase family C56 (Pfp1 endopeptidase, clan PC(C)).

The best characterised protein in this entry, Pyrococcus furiosus protease I (PfpI), is an intracellular cysteine peptidase characterised by its stability and proposed to represent the predominant proteolytic activity of this thermophilic archaebacterium. Pfpi-like proteins have been found in bacteria, archaea, in some plants and in amoebae. The structure of P. horikoshii PfpI shows an alpha/beta sandwich fold, which consists of a central beta sheet flanked by two helices and two strands on one side, and by six helices and two strands on the other side. The fold resembles that of glutamine amidotransferases (GATase) of class I, which are characterised by a conserved Cys-His-Glu active site. The catalytically essential cysteine is located at a nucleophile elbow. PfpI forms a hexameric structure and the active sites are formed at the interfaces between three pairs of monomers. Cys and His form a triad with a glutamate residue from an adjacent monomer [PMID: 11114201].

Other proteins in this group:

  • Pyrococcus horikoshii intracellular protease 1 (PfpI/PH1704).
  • Bacillus subtilis general stress protein 18 (GSP18/yfkM) [PMID: 19170879].
  • E. coli protein yhbO. It is involved in protection against environmental stresses. It has deglycase activity, and can repair glyoxal- and methylglyoxal-glycated proteins [PMID: 26774339].

Peptidase C56 family proteins not found in this entry are structurally and functionally different [PMID: 15070401], e.g. human DJ-1 creates a hydrophobic patch at the molecular interface instead of completing the catalytic triad, while Escherichia coli chaperone HSP31 forms a Cys-His-Asp triad.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE profiles