Detail of GM0004


The genetically modified enzybiotic, named Lambda SA2-E-LysK-SH3b , constructed by Domains Assembly strategy, change or extend lytic spectrum.
With  Lambda SA2-E-LysK-SH3b
  Sequence Length:  218 AA.
  Mass:  24016.7 Da.
  Isoelectric Point:  6.91
  Function:  reduced the S. aureus bacterial load by 1 log units within 3 h


GM0004, constructed by Domains Assembly strategy.
    No schema construted on GM0004
GM0004[1-142]: derive from protein C5WI88 sequence 5-145

C5WI88, 449 AA., the Putative prophage LambdaSa2, lysin from Streptococcus dysgalactiae subsp. equisimilis (str

Source: Streptococcus dysgalactiae subsp. equisimilis (str

Domains and repeats

5-145:  IPR008044, the Bacteriophage lysin
6-138:  IPR000064, the Endopeptidase, NLPC/P60 domain
154-192:  IPR013168, the Cpl-7 lysozyme, C-terminal?
198-236:  IPR013169, the Cpl-7 lysozyme, C-terminal?
270-399:  IPR002901, the Mannosyl-glycoprotein endo-beta-N-acetylglucosamid

GO term prediction

Biological Process:  0009253, the peptidoglycan catabolic process
Molecular Function:  0004040, the amidase activity?

Linking to UniprotKB
Linging to InterPro
GM0004[143-216]: derive from protein I6X5A8 sequence 409-481

I6X5A8, 495 AA., the LysK from Staphylococcus phage Fi200W

Source: Staphylococcus phage Fi200W

Domains and repeats

29-160:  IPR007921, the CHAP domain
196-369:  IPR002502, the N-acetylmuramoyl-L-alanine amidase domain
409-481:  IPR003646, the SH3-like domain, bacterial-type?

GO term prediction

Molecular Function:  0008745, the N-acetylmuramoyl-L-alanine amidase activity

Linking to UniprotKB
Linging to InterPro



: EAD, Endopeptidase domain, derived from streptococcal ??SA2 endolysin;
: CBD, SH3b domain, derived from the staphylococcal phage K endolysin(LysK);
Domain and repeats:
: IPR008044,Bacteriophage lysin;
: IPR003646,SH3-like domain, bacterial-type?;
: IPR000064,Endopeptidase, NLPC/P60 domain;
GO term prediction:
  BlastP to GMEnzy


  1.  Expressed by pET21a in E. coli BL21 (DE3),  Purified by immobilized metal ion affinity chromatography, using nickel-NTA Superflow resin(QIAGEN, Valencia, CA)


    No activity data found on GM0004


  1. Mathias Schmelcher, Anne M. Powell, Stephen C. Becker, Mary J. Camp, and David M. Donovan. (2012) Chimeric phage lysins act synergistically with Lysostaphin to kill mastitis causing Staphylococcus aureus in murine mammary glands. Appl. Environ. Microbiol.. 960:729-737. [doi:10.1128/AEM.07050-11] [PMID:22286996] [FULL TEXT]
  2. Stephen C. Becker, Juli Foster-Frey, Angeline J. Stodola, Daniel Anacker, David M. Donovan. (2009) Differentially conserved staphylococcal SH3b_5 cell wall binding domains confer increased staphylolytic and streptolytic activity to a streptococcal prophage endolysin domain. Gene. 4431-5:32-41. [doi:10.1016/j.gene.2009.04.023] [PMID:19422893]


  •   [1]  In a mouse model of mastitis, infusion of 25 μg of λSA2-E-Lyso-SH3b or λSA2-E-LysK-SH3b into mammary glands reduced S. aureus CFUs by 0.63 or 0.81 log units, compared to >2 log for lysostaphin
  •   ----   at  2013-09-06 16:08:25

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