Family C82

Family

Summary Holotypes Alignment Tree Genomes Structure Literature H-seq M-seq

M20A

Summary Holotypes Alignment Tree Genomes Literature

M20B

Summary Holotypes Alignment Tree Genomes Literature

M20C

Summary Holotypes Alignment Tree Genomes Literature

M20D

Summary Holotypes Alignment Tree Genomes Literature

M20F

Summary Holotypes Alignment Tree Genomes Literature

Summary for family C82

Family type peptidaseC82.001 - L,D-transpeptidase (Enterococcus-type) (Enterococcus faecium), MEROPS Accession MER0076166 (peptidase unit: 217-466)
Content of familyFamily C82 contains enzymes that hydrolase (and transfer) bacterial cell wall peptides.
History Identifier created: MEROPS 7.9 (17 September 2007)
During the final stages of cell-wall synthesis in bacteria, D,D-transpeptidases catalyse the cross-linking of peptide chains from adjacent glycan strands of nascent peptidoglycan. The D,D-transpeptidases are inhibited by antibiotics like penicillin and ampicillin. An ampicillin-resistant mutant of Enterococcus faecium was found to express a beta-lactam-insensitive LD-transpeptidase, termed Ldt(fm) (Mainardi et al., 2000). Homologous enzymes occur widely in bacteria, and some of them can act as peptide hydrolases as well as transpeptidases.
Catalytic typeCysteine
Active siteActive site residues His421 and Cys442 (see the Alignment) were identified crystallographically by Biarrotte-Sorin et al. (2006).
Activities and specificitiesThe L,D-transpeptidase of Enterococcus faecalis (known as Ldt(fs)) was shown to hydrolyse the L-Lys(3)-D-Ala(4) bonds of bacterial cell wall components, including the tetrapeptide and pentapeptide stems; the protein also showed cell-wall cross-linking activity (Magnet et al., 2007).
Molecular structureThe structure of a fragment of the L,D-transpeptidase of Enterococcus faecium was determined by Biarrotte-Sorin et al. (2006). The active site residues were seen to occur in the so-called ErfK/YbiS/YhnG domain, as they do in the Escherichia coli protein ykuD and the sortases (family C60). As a result, family C82 is placed in clan CL.
ClanCL
Basis of clan assignmentActive site residues for members of this family and family C60 occur in the same order in the sequence: H, C.
Distribution of family Bacteria details  
Archaea -  
Protozoa -  
Fungi -  
Plants details  
Animals details  
Viruses -  
Biological functions
Statistics for family C82Sequences:9593
Identifiers:8
Identifiers with PDB entries:4
Downloadable files Sequence library (FastA format)
Sequence alignment (FastA format)
Phylogenetic tree (Newick format)
Subfamily C82A
Name Peptidase subfamily C82A
Subfamily type peptidase C82.001 - L,D-transpeptidase ({Enterococcus}-type) (Enterococcus faecium), MEROPS Accession MER0076166 (peptidase unit: 217-466)
Active site residues H421 C442 
Statistics Sequences: 8580
Identifiers: 7
Identifiers with PDB entries: 2
Other databases INTERPRO IPR038063
PFAM PF03734
SCOP 141524
Downloadable files Sequence library [FastA format]
Sequence alignment [FastA format]
Phylogenetic tree [Newick format]
Peptidases and Homologues MEROPS ID Structure
L,D-transpeptidase (Enterococcus-type)C82.001Yes
Ldt(fs) transpeptidaseC82.002-
LdtF protein (Escherichia coli)C82.A01-
ECBD_1659 protein (Escherichia coli)C82.A02-
YnhG protein (Escherichia coli)C82.A03-
YbiS protein (Escherichia coli)C82.A04-
YcfS protein (Escherichia coli)C82.A05-
Subfamily C82A non-peptidase homologuesnon-peptidase homologue-
Subfamily C82A unassigned peptidasesunassignedYes
Subfamily C82B
Name Peptidase subfamily C82B
Subfamily type peptidase C82.003 - ykuD transpeptidase (Bacillus subtilis), MEROPS Accession MER0094392 (peptidase unit: 52-164)
Active site residues H123 G124 C139 R141 
Statistics Sequences: 1014
Identifiers: 1
Identifiers with PDB entries: 2
Other databases INTERPRO IPR005490
PANTHER PTHR30582
PFAM PF03734
SCOP 54107
Downloadable files Sequence library [FastA format]
Sequence alignment [FastA format]
Phylogenetic tree [Newick format]
Peptidases and Homologues MEROPS ID Structure
ykuD transpeptidaseC82.003Yes
Subfamily C82B non-peptidase homologuesnon-peptidase homologue-
Subfamily C82B unassigned peptidasesunassignedYes
Peptidases not assigned to subfamily
Peptidases and Homologues MEROPS ID Structure
Family C82 non-peptidase homologuesnon-peptidase homologue-
Family C82 unassigned peptidasesunassigned-