Detail of GM0021


Summary

The genetically modified enzybiotic, named XlyACAT:PlyLCBD , constructed by Domains Assembly strategy, lose the activities of cell targeting.
With  XlyACAT:PlyLCBD
  Sequence Length:  253 AA.
  Mass:  27548.6 Da.
  Isoelectric Point:  5.56
  Function:  the chimeric lysin that we constructed (XlyACAT:PlyLCBD), where both charge and PG preference reduce but do not eliminate lysis.

Construction

GM0021, constructed by Domains Assembly strategy.
P39800: N-acetylmuramoyl-L-alanine amidase XlyA
W0CKA7: N-acetylmuramoyl-L-alanine amidase
UniProt

IPR002502:1-153
IPR018392:160-204
IPR002477:225-293
InterPro

GM0021:1-178
GM0021:179-253
GMEnzy

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297
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180
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234

Details:
GM0021[1-178]: derive from protein P39800 sequence 1-178

P39800, 297 AA., the N-acetylmuramoyl-L-alanine amidase XlyA from Bacillus subtilis

Source: Bacillus subtilis

Domains and repeats

1-153:  IPR002502, the N-acetylmuramoyl-L-alanine amidase domain
160-204:  IPR018392, the LysM domain
225-293:  IPR002477, the Peptidoglycan binding-like?

GO term prediction

Biological Process:  0009253, the peptidoglycan catabolic process
Biological Process:  0016998, the cell wall macromolecule catabolic process?
Molecular Function:  0008745, the N-acetylmuramoyl-L-alanine amidase activity?


Linking to UniprotKB
Linging to InterPro
GM0021[179-253]: derive from protein W0CKA7 sequence 160-234

W0CKA7, 234 AA., the N-acetylmuramoyl-L-alanine amidase from Bacillus anthracis str. A16R?

Source: Bacillus anthracis str. A16R?

Domains and repeats

:  IPR021976, the Amidase02_C
:  IPR002502, the Amidase_domain

GO term prediction

    No GO info found on GM0021

Linking to UniprotKB
Linging to InterPro

Annotation

1-178
179-253
50
100
150
200
250
300
350
400
450
500
531

1-178
: EAD, Amidase domain, derived from bacteriophage PBSX N-acetylmuramoyl-L-alanine amidase;
179-253
: CBD, Cell wall-targeting domain, derived from Bacillus anthracis str. Ames endolysin PlyL;
Domain and repeats:
1-153
: IPR002502,N-acetylmuramoyl-L-alanine amidase domain;
179-253
: IPR002502,Amidase_domain;
179-253
: IPR021976,Amidase02_C;
GO term prediction:
0008745, the N-acetylmuramoyl-L-alanine amidase activity
0009253, the peptidoglycan catabolic process
MVNIIQDFIPVGANNRPGYAMTPLYITVHNTANTAVGADAAAHARYLKNPDTTTSWHFTVDDTEIYQHLPLNENGWHAGDGNGSGNRASIGIEICENADGDFAKATANAQWLIKTLMAEHNISLANVVPHKYWSGKECPRKLLDTWDSFKAGIGGGGSQTYVVKQGDTLTSIARAFGV-ASATVTPKQNIIQTGAFSPYELPDAVGALKSLNMTGKAIINPEGLTYIVTDPTSDVQLQAFKEYLERKDWWYDDK
  BlastP to GMEnzy

Production

  1.  Expressed by pET15b in E. coli BL21(DE3),  Purified by Ni(II)-chargedHITRAPchelat-ing column (GE Healthcare),Superdex S200 (GE Healthcare) gel filtration was used to further purify.

Activity

    No activity data found on GM0021

Reference

  1. Low, L. Y.Yang, C.Perego, M.Osterman, A.Liddington, R. (2011) Role of net charge on catalytic domain and influence of cell wall binding domain on bactericidal activity, specificity,and host range of phage lysins.. The Journal of biological chemistry. 039:34391-34403. [doi:10.1074/jbc.M111.244160] [PMID:21816821] [FULL TEXT]

Comments

    No comments found on GM0021


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