Detail of GM0031

Summary

The genetically modified enzybiotic, named C165 , constructed by Truncation strategy, improve the lytic activity.
With  C165
  Sequence Length:  165 AA.
  Mass:  18586.8 Da.
  Isoelectric Point:  9.11
  Function:  activity of C165 was approximately twofold higher than LysK

Construction

GM0031, constructed by Truncation strategy.
No schema construted on GM0031

Details:

GM0031[1-165]: derive from protein I6X5A8 sequence 1-165

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

1-165

35-160

: EAD, CHAP domain, derived from phage endolysin LysK;
Domain and repeats:

29-160

: IPR007921,CHAP domain;
GO term prediction:

MAKTQAEINKRLDAYAKGTVDSPYRVKKATSYDPSFGVMEAGAIDADGYYHAQCQDLITDYVLWLTDNKVRTWGNAKDQIKQSYGTGFKIHENKPSTVPKKGWIAVFTSGSYEQWGHIGIVYDGGNTSTFTILEQNWNGYANKKPTKRVDNYYGLTHFIEIPVKA

BlastP to GMEnzy

Production

1. Expressed by pQE60 in E. coli XL1-Blue, Purified by ion-exchange and size exclusion chromatography

Activity

No activity data found on GM0031

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 GM0031

GMEnzy : A Genetically Modified Enzybiotic Database