Detail of GM0097

Summary

The genetically modified enzybiotic, named endo , constructed by Truncation strategy, lose the lytic activity.
With  endo
  Sequence Length:  180 AA.
  Mass:  20439.1 Da.
  Isoelectric Point:  5.78
  Function:  showed significantly reduced lytic activity on SDS cell walls in the absence of the cell wall binding domain

Construction

GM0097, constructed by Truncation strategy.
No schema construted on GM0097

Details:

GM0097[1-180]: derive from protein Q8SDS7 sequence 1-180

Q8SDS7, 481 AA., the Amidase from Staphylococcus phage phi11 (Bacteriophage phi-11)

Source: Staphylococcus phage phi11 (Bacteriophage phi-11)

Domains and repeats

7-148:  IPR007921, the CHAP domain
188-338:  IPR002502, the N-acetylmuramoyl-L-alanine amidase domain
395-466:  IPR003646, the SH3-like domain, bacterial-type

GO term prediction

Biological Process: 0009253, the peptidoglycan catabolic process
Molecular Function: 0008745, the N-acetylmuramoyl-L-alanine amidase activity?

Linking to UniprotKB
Linging to InterPro

Annotation

1-180

: EAD, Endopeptidase domain, derived from S. aureus NCTC8325 bacteriophages ??13;
Domain and repeats:

7-148

: IPR007921,CHAP domain;
GO term prediction:

MQAKLTKNEFIEWLKTSEGKQFNVDLWYGFQCFDYANAGWKVLFGLLLKGLGAKDIPFANNFDGLATVYQNTPDFLAQPGDMVVFGSNYGAGYGHVAWVIEATLDYIIVYEQNWLGGGWTDGIEQPGWGWEKVTRRQHAYDFPMWFIRPNFKSETAPRSVQSPTQAPKKETAKPQPKAVE

BlastP to GMEnzy

Production

1. Expressed by pET22b in E. coli BL21(DE3), Purified by nickel-nitrilotriacetic acid affinity chromatography

Activity

No activity data found on GM0097

Reference

1. Sass, P.Bierbaum, G.. (2007) Lytic activity of recombinant bacteriophage phi11 and phi12 endolysins on whole cells and biofilms of Staphylococcus aureus. Applied and environmental microbiology. 01:347-352. [doi:10.1128/AEM.01616-06] [PMID:17085695] [FULL TEXT]

Comments

No comments found on GM0097

GMEnzy : A Genetically Modified Enzybiotic Database