Penicillin-binding proteins
| Penicillin-binding protein, transpeptidase | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | PCN-bd_Tpept | ||||||
| Pfam | PF00905 | ||||||
| InterPro | IPR001460 | ||||||
| OPM superfamily | 195 | ||||||
| OPM protein | 5hlb | ||||||
| Membranome | 541 | ||||||
| |||||||
| Penicillin-binding protein, dimerisation domain | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | PBP_dimer | ||||||
| Pfam | PF03717 | ||||||
| InterPro | IPR005311 | ||||||
| |||||||
Penicillin-binding proteins (PBPs) are a group of proteins that are characterized by their affinity for and binding of penicillin. They are a normal constituent of many bacteria; the name just reflects the way by which the protein was discovered. All β-lactam antibiotics (except for tabtoxinine-β-lactam, which inhibits glutamine synthetase) bind to PBPs, which are essential for bacterial cell wall synthesis. PBPs are members of a subgroup of transpeptidase enzymes called DD-transpeptidases.