|Family type peptidase||C108.001 - Prp peptidase (Staphylococcus aureus) (Staphylococcus aureus), MEROPS Accession MER0003820 (peptidase unit: 1-106)|
|Content of family||Family C108 contains cysteine endopeptidases|
Identifier created: MEROPS 10.0 (14 Mar 2016)|
The Prp protein (C108.001) was discovered to be the peptidase responsible for post-translational trimming of ribosomal protein L27 from (Staphylococcus aureus), removing an N-terminal extension that is absent in most Gram-positive bacteria (Wall et al., 2014). The Prp peptidase is homologous to the orf13 protein from bacteriophage Cp-1 (C108.002), which processes the major capsid protein of the phage (Martin et al., 1998).
|Active site residues||H22 C34 |
|Active site||A His, Cys catalytic dyad has been proposed and mutagenesis of the cysteine prevents cleavage of ribosomal protein L27 by the Prp peptidase (Wall et al., 2014).|
|Activities and specificities||The Prp protein removes a nine-residue extension from the N-terminus of ribosomal protein L27 (Wall et al., 2014). The processing peptidase from bacteriophage Cp-1 removes a 48-residue N-terminal propeptide from the main coat protein (Martin et al., 1998). In both cleavages, Ala is in P1".|
|Molecular structure||The first tertiary structure to be solved was of the TM1457 protein from Thermotoga maritima. The fold comprises two helices contacting one side of a five-stranded beta sheet. The proposed active site lies in the large cleft between the first alpha helix and the second beta strand (Shin et al., 2005). Because this fold is unlike that of any other peptidase, family C108 is the representative structure of clan CR.|