Detail of GM0015
Summary
The genetically modified enzybiotic, named CHAP K , constructed by Truncation strategy, improve the lytic activity.With CHAP K
Sequence Length: 133 AA.
Mass: 15040.7 Da.
Isoelectric Point: 8.39
Function: exhibits stronger activity than the original multidomain lysin (LysK) and displays rapid lytic activity against a variety of pathogenic staphylococcal species including Staphylococcus epidermidis and methicillin-resistant S. aureus (MRSA) strains. Purified CHAPK applied to biofilms of Staphylococcus aureus DPC5246 completely eliminated the staphylococcal biofilms within 4 h. In addition,CHAPK was able to prevent biofilm formation by this strain. The CHAPK lysin also reduced S. aureus in a skin decolonization model.
Construction
GM0015, constructed by Truncation strategy. No schema construted on GM0015
Details:
GM0015[1-134]: derive from protein I6X5A8 sequence 26-160
I6X5A8, 495 AA., the LysK from Staphylococcus phage Fi200W
Source: Staphylococcus phage Fi200W
196-369: IPR002502, the N-acetylmuramoyl-L-alanine amidase domain
409-481: IPR003646, the SH3-like domain, bacterial-type?
Linking to UniprotKB
Linging to InterPro
Domains and repeats
29-160: IPR007921, the CHAP domain196-369: IPR002502, the N-acetylmuramoyl-L-alanine amidase domain
409-481: IPR003646, the SH3-like domain, bacterial-type?
GO term prediction
Molecular Function: 0008745, the N-acetylmuramoyl-L-alanine amidase activityLinking to UniprotKB
Linging to InterPro
Annotation
1-134
1-126
: EAD, CHAP domain, derived from anti-staphylococcal bacteriophage endolysin, LysK;Domain and repeats:
4-134
: IPR007921,CHAP domain; GO term prediction:
KKATSYDPSFGVMEAGAIDADGYYHAQCQDLITDYVLWLTDNKVRTWGNAKDQIKQSYGTGFKIHENKPSTVPKKGWIAVFTSGSYEQWGHIGIVYDGGNTSTFTILEQNWNGYANKKPTKRVDNYYGLTHFI