Detail of GM0015


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.


GM0015, constructed by Truncation strategy.
    No schema construted on GM0015
GM0015[1-134]: derive from protein I6X5A8 sequence 26-160

I6X5A8, 495 AA., the LysK from Staphylococcus phage Fi200W

Source: Staphylococcus phage Fi200W

Domains and repeats

29-160:  IPR007921, the CHAP domain
196-369:  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 activity

Linking to UniprotKB
Linging to InterPro



: EAD, CHAP domain, derived from anti-staphylococcal bacteriophage endolysin, LysK;
Domain and repeats:
: IPR007921,CHAP domain;
GO term prediction:
  BlastP to GMEnzy


  1.  Expressed by pQE60 in E. coli XL1-Blue,  Purified by cation exchange chromatography and then desalted and concentrated using an amicon ultra centrifugal filter(Milipore) with 10kDa cut-off


    No activity data found on GM0015


  1. Fenton, M. Keary, R. McAuliffe, O. Ross, R. P. O'Mahony, J. Coffey, A.. (2013) Bacteriophage-Derived Peptidase CHAP(K) Eliminates and Prevents Staphylococcal Biofilms. International journal of microbiology. 2013625341:1-8. [doi:10.1155/2013/625341] [PMID:23431312] [FULL TEXT]


    No comments found on GM0015

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