Family S11
Summary for family S11
| Name | Peptidase family S11 (D-Ala-D-Ala carboxypeptidase A family) |
|---|
| Family type peptidase | S11.001 - D-Ala-D-Ala carboxypeptidase A (Geobacillus stearothermophilus), MEROPS Accession MER0000448 (peptidase unit: 31-452) |
| Content of family | Peptidase family S11 contains serine-type D-Ala-D-Ala carboxypeptidases. |
| History |
Identifier created: Biochem.J. 290:205-218 (1993)
|
| Catalytic type | Serine |
| Active site residues | S66 K69 S130 |
| Active site | The active site residues Ser and Lys form the catalytic dyad and are found in the motif Ser-Xaa-Thr-Lys. There is a further catalytic Ser residue further toward the C-terminus in a conserved Ser-Xaa-Asn motif. |
| Activities and specificities | Two main types of enzymatic activity are found in family S11. These are DD-carboxypeptidase activity in which there is transfer of the C-terminal D-Ala to water, and DD-transpeptidase activity in which the peptidoglycan monomer is transferred to an exogenous receptor after removal of the C-terminal D-Ala. There are peptidases that have both activities. |
| Inhibitors | Antibiotics of the beta-lactam family inactivate some members of family S11 through acylation of the active site serine. |
| Molecular structure | Family S11 is included in clan SE as the protein fold of the peptidase unit for members of this family resembles that of the type example of family S12, D-Ala-D-Ala-carboxypeptidase B (S12.001). The peptidases of family S11 contain two domains - one of alpha helices and one containing an alpha-beta sandwich. The active site residues reside on a helix that crosses the cleft between the two lobes. The all-alpha helix domain, containing the third catalytic residue in the motif Ser-Xaa-Asn, forms one side of the cavity whereas the other side is formed by the third strand of the beta sheet containing a Lys-Thr-Gly motif. |
| Clan | SE |
| Basis of clan assignment | Protein fold of the peptidase unit for members of this family resembles that of D-Ala-D-Ala-carboxypeptidase B, the type example for clan SE. |
| Peptidases and Homologues |
MEROPS ID |
Structure |
| D-Ala-D-Ala carboxypeptidase A | S11.001 | - |
| murein-DD-endopeptidase | S11.002 | - |
| penicillin-binding protein 6 | S11.003 | Yes |
| K15-type DD-transpeptidase | S11.004 | Yes |
| D-Ala-D-Ala carboxypeptidase DacF | S11.005 | - |
| D,D-carboxypeptidase PBP3 (Streptococcus-type) | S11.006 | Yes |
| penicillin-binding protein 4 (Neisseria-type) peptidase | S11.007 | - |
| penicillin-binding protein 5-type peptidase | S11.008 | Yes |
| penicillin-binding protein 6b-type peptidase | S11.009 | Yes |
| penicillin-binding protein 4 (Staphylococcus-type) peptidase | S11.010 | Yes |
| D-alanyl-D-alanine carboxypeptidase (Mycobacterium smegmatis) | S11.011 | - |
| penP g.p. (Bacillus subtilis) | S11.A01 | Yes |
| Family S11 non-peptidase homologues | non-peptidase homologue | Yes |
| Family S11 unassigned peptidases | unassigned | Yes |
