Detail of GM0030


Summary

The genetically modified enzybiotic, named C203 , constructed by Truncation strategy, decrease the lytic activity.
With  C203
  Sequence Length:  203 AA.
  Mass:  22728.6 Da.
  Isoelectric Point:  10.04
  Function:  the activity of C203 was approximately 14-fold lower than LysK

Construction

GM0030, constructed by Truncation strategy.
I6X5A8: LysK
UniProt

IPR007921:29-160
IPR002502:196-369
IPR003646:409-481
InterPro

GM0030:1-203
GMEnzy

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Details:
GM0030[1-203]: derive from protein I6X5A8 sequence 1-203

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

Annotation

1-203
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495

35-160
: EAD, CHAP domain, derived from phage endolysin LysK;
Domain and repeats:
29-160
: IPR007921,CHAP domain;
GO term prediction:
MAKTQAEINKRLDAYAKGTVDSPYRVKKATSYDPSFGVMEAGAIDADGYYHAQCQDLITDYVLWLTDNKVRTWGNAKDQIKQSYGTGFKIHENKPSTVPKKGWIAVFTSGSYEQWGHIGIVYDGGNTSTFTILEQNWNGYANKKPTKRVDNYYGLTHFIEIPVKAGTTVKKETAKKSASKTPAPKKKATLKVSKNHINYTMDK
  BlastP to GMEnzy

Production

  1.  Expressed by pQE60 in E. coli XL1-Blue,  Purified by nickel affinity chromatography

Activity

    No activity data found on GM0030

Reference

  1. Horgan, M. O'Flynn, G. Garry, J. Cooney, J. Coffey, A. Fitzgerald, G. F. Ross, R. P. McAuliffe, O.. (2009) Phage lysin LysK can be truncated to its CHAP domain and retain lytic activity against live antibiotic-resistant staphylococci. Applied and environmental microbiology. 752:872-874. [doi:10.1128/AEM.01831-08] [PMID:19047377] [FULL TEXT]

Comments

    No comments found on GM0030


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