Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Streptomyces coelicolor |
Protein Variants | Comment | Organism |
---|---|---|
L684P | about 50% of wild-type activity | Streptomyces coelicolor |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
penicillin | - |
Streptomyces coelicolor |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | protein harbors two protein domains separated by a putative hydrophobic transmembrane region | Streptomyces coelicolor | 16020 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces coelicolor | Q9KZY7 | - |
- |
Streptomyces coelicolor ATCC BAA-471 | Q9KZY7 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
D-Ala-D-Ala + H2O | - |
Streptomyces coelicolor | 2 D-Ala | - |
? | |
D-Ala-D-Ala + H2O | - |
Streptomyces coelicolor ATCC BAA-471 | 2 D-Ala | - |
? | |
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O | substrate mimics the terminal portions of the peptidoglycan pentapeptide precursors | Streptomyces coelicolor | Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala | - |
? | |
Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala-D-Ala + H2O | substrate mimics the terminal portions of the peptidoglycan pentapeptide precursors | Streptomyces coelicolor ATCC BAA-471 | Nalpha,Nepsilon-diacetyl-L-Lys-D-Ala + D-Ala | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DD-CPase | - |
Streptomyces coelicolor |
SCO4439 | - |
Streptomyces coelicolor |
IC50 Value | IC50 Value Maximum | Comment | Organism | Inhibitor | Structure |
---|---|---|---|---|---|
1 | - |
pH 7.2, 37°C | Streptomyces coelicolor | penicillin |
General Information | Comment | Organism |
---|---|---|
physiological function | in a gene disruption mutant, the spores are affected in their resistance to heat and acid and show a dramatic increase in swelling during germination. The mycelium of the mutant is more sensitive to glycopeptide antibiotics vancomycin and teicoplanin. Both the DD-CPase domain and the hydrophobic transmembrane region are essential for complementing the wild type phenotypes in the mutant. In a model for the biological mechanism, DD-CPase releases D-Ala from peptidoglycan precursors, thereby reducing the substrate pool for peptidoglycan crosslinking (transpeptidation) | Streptomyces coelicolor |