Detail of GM0123


Summary

The genetically modified enzybiotic, named phill 389 , constructed by Truncation strategy, decrease the lytic activity.
With  phill 389
  Sequence Length:  389 AA.
  Mass:  43483 Da.
  Isoelectric Point:  9.25
  Function:  decrease the lytic activity

Construction

GM0123, constructed by Truncation strategy.
    No schema construted on GM0123
Details:
GM0123[1-389]: derive from protein Q2FX77 sequence 1-389

Q2FX77, 481 AA., the Autolysin from Staphylococcus aureus (strain NCTC 8325)

Source: Staphylococcus aureus (strain NCTC 8325)

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

1-389

1-389
: EAD, CHAP domain, derived from S. aureus bacteriophage phi11 endolysin;
: EAD, Amidase domain, derived from S. aureus bacteriophage phi12 endolysin;
Domain and repeats:
1-389
: IPR002502,N-acetylmuramoyl-L-alanine amidase domain;
1-389
: IPR003646,SH3-like domain, bacterial-type;
1-389
: IPR007921,CHAP domain;
GO term prediction:
0008745, the N-acetylmuramoyl-L-alanine amidase activity
0009253, the peptidoglycan catabolic process
MQAKLTKNEFIEWLKTSEGKQFNVDLWYGFQCFDYANAGWKVLFGLLLKGLGAKDIPFANNFDGLATVYQNTPDFLAQPGDMVVFGSNYGAGYGHVAWVIEATLDYIIVYEQNWLGGGWTDGIEQPGWGWEKVTRRQHAYDFPMWFIRPNFKSETAPRSVQSPTQAPKKETAKPQPKAVELKIIKDVVKGYDLPKRGSNPKGIVIHNDAGSKGATAEAYRNGLVNAPLSRLEAGIAHSYVSGNTVWQALDESQVGWHTANQIGNKYYYGIEVCQSMGADNATFLKNEQATFQECARLLKKWGLPANRNTIRLHNEFTSTSCPHRSSVLHTGFDPVTRGLLPEDKRLQLKDYFIKQIRAYMDGKIPVATVSNESSASSNTVKPVASAWKR
  BlastP to GMEnzy

Production

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

Activity

    No activity data found on GM0123

Reference

  1. Donovan, D. M.Lardeo, M.Foster-Frey, J.. (2006) Lysis of staphylococcal mastitis pathogens by bacteriophage phi11 endolysin. FEMS microbiology letters. 01:133-39. [doi:10.1111/j.1574-6968.2006.00483.x] [PMID:17054440]

Comments

    No comments found on GM0123


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