Detail of GM0127


Summary

The genetically modified enzybiotic, named B30-182-Lyso , constructed by Domains Assembly strategy, change or extend lytic spectrum.
With  B30-182-Lyso
  Sequence Length:  428 AA.
  Mass:  46970.3 Da.
  Isoelectric Point:  8.64
  Function:  actively lyse S. aureus and the same streptococcal test species as the parent B30 endolysin

Construction

GM0127, constructed by Domains Assembly strategy.
    No schema construted on GM0127
Details:
GM0127[1-183]: derive from protein Q5MY96 sequence 1-183

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
GM0127[184-429]: derive from protein P10547 sequence 248-493

P10547, 493 AA., the Lysostaphin EC=3.4.24.75 from Staphylococcus simulans

Source: Staphylococcus simulans

Domains and repeats

239-382:  IPR011055, the Duplicated hybrid motif?
411-481:  IPR003646, the SH3-like domain, bacterial-type
278-367:  IPR003646, the Peptidase M23?

GO term prediction

    No GO info found on GM0127

Linking to UniprotKB
Linging to InterPro

Annotation

1-183
184-429

1-182
: EAD, CHAP domain, derived from S. agalactiae bacteriophage endolysin B30;
: EAD, Amidase domain, derived from S. agalactiae bacteriophage endolysin B31;
183-428
: EAD, full length domain, derived from lysostaphin;
Domain and repeats:
1-183
: IPR003646,SH3-like domain, bacterial-type;
1-183
: IPR007921,CHAP domain;
1-183
: IPR017853,Glycoside hydrolase, superfamily;
214-303
: IPR003646,Peptidase M23?;
347-417
: IPR003646,SH3-like domain, bacterial-type;
GO term prediction:
MATYQEYKSRSNGNAYDIDGSFGAQCWDGYADYCKYLGLPYANCTNTGYARDIWEQRHENGILNYFDEVEVMQAGDVAIFMVVDGVTPYSHVAIFDSDAGGGYGWFLGQNQGGANGAYNIVKIPYSATYPTAFRPKVFKNAVTVTGNIGLNKGDYFIDVSAYQQADLTTTCQQAGTTKTIIK-AATHEHSAQWLNNYKKGYGYGPYPLGINGGMHYGVDFFMNIGTPVKAISSGKIVEAGWSNYGGGNQIGLIENDGVHRQWYMHLSKYNVKVGDYVKAGQIIGWSGSTGYSTAPHLHFQRMVNQFSNSTAQDPMPFLKSAGYGKAGGTVTPTPNTGWKTNKYGTLYKSESASFTPNTDIITRTTGPFRSMPQSGVLKAGQTIHYDEVMKQDGHVWVGYTGNSGQRIYLPVRTWQKSTNTLGVLWGTIK
  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 GM0127

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 GM0127


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