Detail of GM0099
Summary
The genetically modified enzybiotic, named ami , constructed by Truncation strategy, lose the lytic activity.With ami
Sequence Length: 190 AA.
Mass: 21060.8 Da.
Isoelectric Point: 9.69
Function: showed significantly reduced lytic activity on SDS cell walls in the absence of the cell wall binding domain
Construction
GM0099, constructed by Truncation strategy. No schema construted on GM0099
Details:
GM0099[1-190]: derive from protein Q8SDS7 sequence 181-370
Q8SDS7, 481 AA., the Amidase from Staphylococcus phage phi11 (Bacteriophage phi-11)
Source: Staphylococcus phage phi11 (Bacteriophage phi-11)
188-338: IPR002502, the N-acetylmuramoyl-L-alanine amidase domain
395-466: IPR003646, the SH3-like domain, bacterial-type
Molecular Function: 0008745, the N-acetylmuramoyl-L-alanine amidase activity?
Linking to UniprotKB
Linging to InterPro
Domains and repeats
7-148: IPR007921, the CHAP domain188-338: IPR002502, the N-acetylmuramoyl-L-alanine amidase domain
395-466: IPR003646, the SH3-like domain, bacterial-type
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
1-190
1-190
: EAD, Amidase domain, derived from S. aureus NCTC8325 bacteriophages ??16;Domain and repeats:
8-158
: IPR002502,N-acetylmuramoyl-L-alanine amidase domain; GO term prediction:
0008745, the N-acetylmuramoyl-L-alanine amidase activity
0009253, the peptidoglycan catabolic process
LKIIKDVVKGYDLPKRGSNPKGIVIHNDAGSKGATAEAYRNGLVNAPLSRLEAGIAHSYVSGNTVWQALDESQVGWHTANQIGNKYYYGIEVCQSMGADNATFLKNEQATFQECARLLKKWGLPANRNTIRLHNEFTSTSCPHRSSVLHTGFDPVTRGLLPEDKRLQLKDYFIKQIRAYMDGKIPVATVS