Summary for clan CL

Summary Alignment Structure Literature
Clan type peptidaseC60.002 - sortase B (Staphylococcus aureus), MEROPS Accession MER0020433 (peptidase unit: 5-242); PDB accession 1NG5_A
HistoryMEROPS 6.8 (20 August 2004)
DescriptionCysteine nucleophile; catalytic residues in the order His, Cys in sequence
Contents of clanClan CL contains bacterial peptidases that hydrolase (and transfer) bacterial cell wall peptides.
EvidenceStructures are known to be similar for members of both families in the clan.
Catalytic mechanismPeptidase (and transferase) activity is dependent upon a His, Cys catalytic dyad.
Peptidase activityPeptidases in the clan act on substrates associated with bacterial cell wall cross-linking peptides, either cleaving the peptide itself (family C82) or cleaving proteins and forming new amide bonds betweent he new C-terminus and the cross-linking peptide (family C60).
Protein foldTertiary structures have been determined for sortase A (C60.001; Zong et al., 2004), sortase B (C60.002; Zong et al., 2004) and for a fragment of the L,D-transpeptidase of Enterococcus faecium (C82.001; Biarrotte-Sorin et al. (2006)). The protein fold consists of a closed beta barrel decorated on the outside with helices. The active site residues are at the end of the barrel.
Homologous non-peptidase familiesThe C-terminal domain from the ykuD transpeptidase of Bacillus subtilis has a similar fold (Bielnicki et al. (2006)).
Activation mechanismSortase A is activated by Ca2+ (Naik et al., 2005).
Other databases SCOP63817


Family Family Type Peptidase Structure
C60 sortase A ({Staphylococcus}-type) (Staphylococcus aureus) Yes
C82 L,D-transpeptidase ({Enterococcus}-type) (Enterococcus faecium) Yes

Distribution of clan CL among Kingdoms of Organisms