Detail of GM0037

Summary

The genetically modified enzybiotic, named LysK325-495 , constructed by Truncation strategy, decrease the lytic activity.
With  LysK325-495
  Sequence Length:  167 AA.
  Mass:  18161.7 Da.
  Isoelectric Point:  10.13
  Function:  show faint activity in both the zymogram and turbidity reduction assays, but no detectable activity in either plate lysis or MIC assays

Construction

GM0037, constructed by Truncation strategy.
No schema construted on GM0037

Details:

GM0037[1-171]: derive from protein I6X5A8 sequence 325-495

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

1-171

84-150

: CBD, SH3b domain, derived from staphylococcal bacteriophage endolysin LysK;
Domain and repeats:

85-157

: IPR003646,SH3-like domain, bacterial-type?;
GO term prediction:

PTACPHRSMVLHTGFNPVTQGRPSQAIMNKLKDYFIKQIKNYMDKGTSSSTVVKDGKTSSASTPATRPVTGSWKKNQYGTWYKPENATFVNGNQPIVTRIGSPFLNAPVGGNLPAGATIVYDEVCIQAGHIWIGYNAYNGNRVYCPVRTCQGVPPNQIPGVAWGVFK

BlastP to GMEnzy

Production

1. Expressed by pET21a in E. coli BL21 (DE3), Purified by nickel chromatography purification

Activity

No activity data found on GM0037

Reference

1. Becker, S. C.Dong, S.Baker, J. R.Foster-Frey, J.Pritchard, D. G.Donovan, D. M.. (2009) LysK CHAP endopeptidase domain is required for lysis of live staphylococcal cells. FEMS microbiology letters. 01:52-60. [doi:10.1111/j.1574-6968.2009.01541.x] [PMID:19493008]

Comments

No comments found on GM0037

GMEnzy : A Genetically Modified Enzybiotic Database