Detail of GM0143


Summary

The genetically modified enzybiotic, named D5 , constructed by Truncation strategy, decrease the lytic activity.
With  D5
  Sequence Length:  203 AA.
  Mass:  21977.9 Da.
  Isoelectric Point:  10.73
  Function:  decrease the lytic activity

Construction

GM0143, constructed by Truncation strategy.
    No schema construted on GM0143
Details:
GM0143[1-203]: derive from protein P11187 sequence 46-248

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

1-203

1-203
: EAD, Endopeptidase domain, derived from Bacillus amyloliquefaciens phage endolysin;
: EAD, LysM domain, derived from Bacillus amyloliquefaciens phage endolysin;
Domain and repeats:
1-203
: IPR018392,LysM domain ;
1-203
: IPR023346,Lysozyme-like domain;
1-203
: IPR018392,LysM domain;
GO term prediction:
QVITAKQAEDMLRDDVQAFVDGVNKALKVSVTQNQFDALVSFAYNVGLGAFRSSSLLEYLNEGRTALAAAEFPKWNKSGGKVYQGLINRRAQEQALFNSGTPKNVSRGTSSTKTTPKYKVKSGDNLTKIAKKHNTTVATLLKLNPSIKDPNMIRVGQTINVTGSGGKTHKVKSGDTLSKIAVDNKTTVSRLMSLNPEITNPNH
  BlastP to GMEnzy

Production

  1.  Expressed by pET24d(+) in E. coli JM109(DE3),  Purified by HiTrap(Amersham Pharmacia Biotech)

Activity

    No activity data found on GM0143

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 GM0143


CAPTCHA Image   Reload Image
Enter Code*: