Detail of GM0122
Summary
The genetically modified enzybiotic, named phill 194 , constructed by Truncation strategy, decrease the lytic activity.With phill 194
Sequence Length: 194 AA.
Mass: 22022 Da.
Isoelectric Point: 6.54
Function: decrease the lytic activity
Construction
GM0122, constructed by Truncation strategy. No schema construted on GM0122
Details:
GM0122[1-194]: derive from protein Q2FX77 sequence 1-194
Q2FX77, 481 AA., the Autolysin from Staphylococcus aureus (strain NCTC 8325)
Source: Staphylococcus aureus (strain NCTC 8325)
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
1-194
1-194
: EAD, CHAP domain, derived from S. aureus bacteriophage phi11 endolysin;Domain and repeats:
1-194
: IPR003646,SH3-like domain, bacterial-type; 1-194
: IPR007921,CHAP domain; 1-194
: IPR002502,N-acetylmuramoyl-L-alanine amidase domain; GO term prediction:
0008745, the N-acetylmuramoyl-L-alanine amidase activity
0009253, the peptidoglycan catabolic process
MQAKLTKNEFIEWLKTSEGKQFNVDLWYGFQCFDYANAGWKVLFGLLLKGLGAKDIPFANNFDGLATVYQNTPDFLAQPGDMVVFGSNYGAGYGHVAWVIEATLDYIIVYEQNWLGGGWTDGIEQPGWGWEKVTRRQHAYDFPMWFIRPNFKSETAPRSVQSPTQAPKKETAKPQPKAVELKIIKDVVKGYDLP