Detail of GM0151


Summary

The genetically modified enzybiotic, named CLL , constructed by Domains Assembly strategy, change or extend lytic spectrum.
With  CLL
  Sequence Length:  342 AA.
  Mass:  39491.6 Da.
  Isoelectric Point:  4.39
  Function:  LCA exhibited lysozyme activities at levels similar to CPL1 and switched the regulatory properties to LYTA.

Construction

GM0151, constructed by Domains Assembly strategy.
P15057: Lysozyme EC=3.2.1.17
Q8KLP2: N-acetylmuramoyl-L-alanine amidase
UniProt

IPR017853:3-185
IPR018337:220-239
IPR018337:241-260
IPR018337:261-280
IPR018337:281-301
IPR018337:303-322
IPR002502:10 - 151
IPR018337:175 - 194
IPR018337:196 - 215
IPR018337:217 - 237
IPR018337:238 - 257
IPR018337:258 - 277
IPR018337:280 - 301
InterPro

GM0151:1-211
GM0151:212-343
GMEnzy

30
60
90
120
150
180
210
240
270
300
330
339
30
60
90
120
150
180
210
240
270
300
318

Details:
GM0151[1-211]: derive from protein P15057 sequence 1-211

P15057, 339 AA., the Lysozyme EC=3.2.1.17 from Streptococcus phage Cp-1

Source: Streptococcus phage Cp-1

Domains and repeats

3-185:  IPR017853, the Glycoside hydrolase, catalytic domain?
220-239:  IPR018337, the Cell wall/choline-binding repeat
241-260:  IPR018337, the Cell wall/choline-binding repeat
261-280:  IPR018337, the Cell wall/choline-binding repeat
281-301:  IPR018337, the Cell wall/choline-binding repeat
303-322:  IPR018337, the Cell wall/choline-binding repeat

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
GM0151[212-343]: derive from protein Q8KLP2 sequence 188-318

Q8KLP2, 318 AA., the N-acetylmuramoyl-L-alanine amidase from Streptococcus pneumoniae

Source: Streptococcus pneumoniae

Domains and repeats

10 - 151:  IPR002502, the N-acetylmuramoyl-L-alanine amidase domain
175 - 194:  IPR018337, the Cell wall/choline-binding repeat
196 - 215:  IPR018337, the Cell wall/choline-binding repeat
217 - 237:  IPR018337, the Cell wall/choline-binding repeat
238 - 257:  IPR018337, the Cell wall/choline-binding repeat
258 - 277:  IPR018337, the Cell wall/choline-binding repeat
280 - 301:  IPR018337, the Cell wall/choline-binding repeat

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

1-211
212-343
50
100
150
200
250
300
350
400
450
500
550
600
650
657

1-211
: CBD, choline-binding domain, derived from choline-binding domain of the pneumococcal phage CPL1 muramidase;
212-343
: EAD, amidase domain, derived from S. pneumoniae 101 LytAlOl amidase;
Domain and repeats:
212-343
: IPR018337,Cell wall/choline-binding repeat;
212-343
: IPR018337,Cell wall/choline-binding repeat;
212-343
: IPR018337,Cell wall/choline-binding repeat;
212-343
: IPR018337,Cell wall/choline-binding repeat;
212-343
: IPR002502,N-acetylmuramoyl-L-alanine amidase domain;
212-343
: IPR018337,Cell wall/choline-binding repeat;
212-343
: IPR018337,Cell wall/choline-binding repeat;
3-185
: IPR017853,Glycoside hydrolase, catalytic domain?;
GO term prediction:
0008745, the N-acetylmuramoyl-L-alanine amidase activity
0009253, the peptidoglycan catabolic process
MVKKNDLFVDVSSHNGYDITGILEQMGTTNTIIKISESTTYLNPCLSAQVEQSNPIGFYHFARFGGDVAEAEREAQFFLDNVPMQVKYLVLDYEDDPSGDAQANTNACLRFMQMIADAGYKPIYYSYKPFTHDNVDYQQILAQFPNSLWIAGYGLNDGTANFEYFPSMDGIRWWQYSSNPFDKNIVLLDDEEDDKPKTAGTWKQDSKGWWF-VHSDGSYPKDKFEKINGTWYYFDSSGYMLADRWRKHTDGNWYWFDNSGEMATGWKKIADKWYYFNEEGAMKTGWVKYKDTWYYLDAKEGAMVSNAFIQSADGTGWYYLKPDGTLADKPEFTVEPDGLITVK
  BlastP to GMEnzy

Production

  1.  Expressed by pLC in E. coli HB101,  Purified by affinity chromatography on DEAE-cellulose

Activity

  1.  Enzymatic activity test on (Lysozyme) by
  showed 800,000 unit/mg protein

Reference

  1. Lopez, R.Garcia, E.Garcia, P.Garcia, J. L.. (1997) The pneumococcal cell wall degrading enzymes: a modular design to create new lysins?. Microbial drug resistance. 02:199-211. [doi:10.1089/mdr.1997.3.199] [PMID:9185148]
  2. Diaz, E.Lopez, R.Garcia, J. L.. (1990) Chimeric phage-bacterial enzymes: a clue to the modular evolution of genes. Proceedings of the National Academy of Sciences of. 020:8125-8129. [doi:10.1073/pnas.87.20.8125] [PMID:1978320] [FULL TEXT]

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