Detail of GM0148


Summary

The genetically modified enzybiotic, named D10 , constructed by Truncation strategy, decrease the lytic activity.
With  D10
  Sequence Length:  49 AA.
  Mass:  5286.1 Da.
  Isoelectric Point:  11.08
  Function:  decrease the lytic activity

Construction

GM0148, constructed by Truncation strategy.
    No schema construted on GM0148
Details:
GM0148[1-49]: derive from protein P11187 sequence 210-258

P11187, 258 AA., the Lysozyme EC=3.2.1.17 from Bacillus phage phi29

Source: Bacillus phage phi29

Domains and repeats

1 - 147:  IPR023346, the Lysozyme-like domain
162 - 207:  IPR018392, the LysM domain
213 - 258:  IPR018392, the LysM domain

GO term prediction

Biological Process:  0009253, the peptidoglycan catabolic process
Biological Process:  0016998, the cell wall macromolecule catabolic process
Molecular Function:  0003796, the Lysozyme activity


Linking to UniprotKB
Linging to InterPro

Annotation

1-49

1-49
: EAD, LysM domain, derived from Bacillus amyloliquefaciens phage endolysin;
Domain and repeats:
1-49
: IPR023346,Lysozyme-like domain;
1-49
: IPR018392,LysM domain;
1-49
: IPR018392,LysM domain ;
GO term prediction:
GGKTHKVKSGDTLSKIAVDNKTTVSRLMSLNPEITNPNHIKVGQTIRLS
  BlastP to GMEnzy

Production

  1.  Expressed by pET29d(+) in E. coli JM109(DE3,  Purified by HiTrap(Amersham Pharmacia Biotech)

Activity

    No activity data found on GM0148

Reference

  1. Morita, M.Tanji, Y.Orito, Y.Mizoguchi, K.Soejima, A.Unno, H.. (2001) Functional analysis of antibacterial activity of Bacillus amyloliquefaciens phage endolysin against Gram-negative bacteria. FEBS letters. 00:56-59. [doi:10.1016/S0014-5793(01)02587-X] [PMID:11434926]

Comments

    No comments found on GM0148


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