Detail of GM0125


Summary

The genetically modified enzybiotic, named B30-90 , constructed by Truncation strategy, lose the lytic activity.
With  B30-90
  Sequence Length:  90 AA.
  Mass:  10208.1 Da.
  Isoelectric Point:  3.95
  Function:  lose the lytic activity

Construction

GM0125, constructed by Truncation strategy.
    No schema construted on GM0125
Details:
GM0125[1-90]: derive from protein Q5MY96 sequence 1-90

Q5MY96, 443 AA., the Lysin PlyGBS from Streptococcus phage NCTC11261

Source: Streptococcus phage NCTC11261

Domains and repeats

1 - 131:  IPR007921, the CHAP domain
152 - 339:  IPR017853, the Glycoside hydrolase, superfamily
390 - 437:  IPR003646, the SH3-like domain, bacterial-type

GO term prediction

Biological Process:  0005975, the carbohydrate metabolic process
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

1-90

1-90
: EAD, CHAP domain, derived from S. agalactiae bacteriophage endolysin B30;
Domain and repeats:
1-90
: IPR017853,Glycoside hydrolase, superfamily;
1-90
: IPR003646,SH3-like domain, bacterial-type;
1-90
: IPR007921,CHAP domain;
GO term prediction:
MATYQEYKSRSNGNAYDIDGSFGAQCWDGYADYCKYLGLPYANCTNTGYARDIWEQRHENGILNYFDEVEVMQAGDVAIFMVVDGVTPYS
  BlastP to GMEnzy

Production

  1.  Expressed by pET21a in E. coli BL21(DE3),  Purified by nickel-affinity chromatography(gravity-flow QIAGEN Ni-nitrilotriaceticacid (Ni-NTA) agarose)

Activity

    No activity data found on GM0125

Reference

  1. Donovan, D. M.Dong, S.Garrett, W.Rousseau, G. M.Moineau, S.Pritchard, D. G.. (2006) Peptidoglycan hydrolase fusions maintain their parental specificities. Applied and environmental microbiology. 04:2988-2996. [doi:10.1128/AEM.72.4.2988-2996.2006] [PMID:16598006] [FULL TEXT]

Comments

    No comments found on GM0125


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