Detail of GM0112
Summary
The genetically modified enzybiotic, named D195A/Q199A , constructed by Mutagenesis strategy, decrease the binding activity.With D195A/Q199A
Sequence Length: 78 AA.
Mass: 8595.7 Da.
Isoelectric Point: 8.91
Function: decrease the binding activity
Construction
GM0112, constructed by Mutagenesis strategy. No schema construted on GM0112
Details:
GM0112[1-78]: derive from protein Q8LTE6 sequence 156-233
Q8LTE6, 233 AA., the N-acetylmuramoyl-L-alanine amidase from Bacillus phage Gamma
Source: Bacillus phage Gamma
189 - 232: IPR021976, the N-acetylmuramoyl-l-alanine amidase
Molecular Function: 0008745, the N-acetylmuramoyl-L-alanine amidase activity
Linking to UniprotKB
Linging to InterPro
Domains and repeats
3 - 156: IPR002502, the N-acetylmuramoyl-L-alanine amidase domain189 - 232: IPR021976, the N-acetylmuramoyl-l-alanine amidase
GO term prediction
Biological Process: 0009253, the peptidoglycan catabolic processMolecular Function: 0008745, the N-acetylmuramoyl-L-alanine amidase activity
Linking to UniprotKB
Linging to InterPro
Annotation
1-78
1-78
: CBD, Cell wall-targeting domain, derived from B. anthracis ??Phage lysin PlyG (PlyGB (PlyG binding domain; residues 156?C233));195
: MUT, mutation with D195A ;199
: MUT, mutation with Q199A ;Domain and repeats:
1-78
: IPR021976,N-acetylmuramoyl-l-alanine amidase; 1-78
: IPR002502,N-acetylmuramoyl-L-alanine amidase domain; GO term prediction:
0008745, the N-acetylmuramoyl-L-alanine amidase activity
0009253, the peptidoglycan catabolic process
NGNVATTSPTKQNIIQSGAFSPYETPDVMGALTSLKMTAAFILASDGLTYFISKPTSDAQLKAMKEYLDRKGWWYEVK