Detail of GM0154


Summary

The genetically modified enzybiotic, named CL7 , constructed by Domains Assembly strategy, change or extend lytic spectrum.
With  CL7
  Sequence Length:  342 AA.
  Mass:  39468.4 Da.
  Isoelectric Point:  4.31
  Function:  CL7 exhibited a choline-dependent lysozyme activity

Construction

GM0154, constructed by Domains Assembly strategy.
P19385: Lysozyme EC=3.2.1.17
Q8KLP2: N-acetylmuramoyl-L-alanine amidase
UniProt

IPR013781:3-185
IPR017853:3 - 185
IPR013168:205-246
IPR013168:205 - 246
IPR013168:253-294
IPR013168:253 - 294
IPR013168:301-342
IPR013168:301 - 342
IPR002502:10 - 151
IPR018337:175 - 194
IPR018337:196 - 215
IPR018337:217 - 237
IPR018337:238 - 257
IPR018337:258 - 277
IPR018337:280 - 301
InterPro

GM0154:1-203
GM0154:204-344
GMEnzy

30
60
90
120
150
180
210
240
270
300
330
342
30
60
90
120
150
180
210
240
270
300
318

Details:
GM0154[1-203]: derive from protein P19385 sequence 1-203

P19385, 342 AA., the Lysozyme EC=3.2.1.17 from Streptococcus phage Cp-7

Source: Streptococcus phage Cp-7

Domains and repeats

3-185:  IPR013781, the Glycoside hydrolase, catalytic domain
205-246:  IPR013168, the Cpl-7 lysozyme, C-terminal
253-294:  IPR013168, the Cpl-7 lysozyme, C-terminal
301-342:  IPR013168, the Cpl-7 lysozyme, C-terminal
3 - 185:  IPR017853, the Glycoside hydrolase, superfamily
205 - 246:  IPR013168, the Cpl-7 lysozyme, C-terminal
253 - 294:  IPR013168, the Cpl-7 lysozyme, C-terminal
301 - 342:  IPR013168, the Cpl-7 lysozyme, C-terminal

GO term prediction

Biological Process:  0009253, the peptidoglycan catabolic process
Biological Process:  0005975, the carbohydrate metabolic process
Biological Process:  0016998, the cell wall macromolecule catabolic process?
Molecular Function:  0003796, the lysozyme activity?
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
GM0154[204-344]: derive from protein Q8KLP2 sequence 180-318

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
MVKKNDLFVDVASHQGYDISGILEEAGTTNTIIKVSESTSYLNPCLSAQVSQSNPIGFYHFAWFGGNEEEAEAEARYFLDNVPTQVKYLVLDYEDHASASVQRNTTACLRFMQIIAEAGYTPIYYSYKPFTLDNVDYQQILAQFPNSLWIAGYGLNDGTANFEYFPSMDGIRWWQYSSNPFDKNIVLLDDEKEDNINNENTLQ-KNDTGYWYVHSDGSYPKDKFEKINGTWYYFDSSGYMLADRWRKHTDGNWYWFDNSGEMATGWKKIADKWYYFNEEGAMKTGWVKYKDTWYYLDAKEGAMVSNAFIQSADGTGWYYLKPDGTLADKPEFTVEPDGLITVK
  BlastP to GMEnzy

Production

  1.  Expressed by pLC7 in E. coli DHl,  Purified by Bio-Gel P-60

Activity

    No activity data found on GM0154

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.. (1991) Chimeric pneumococcal cell wall lytic enzymes reveal important physiological and evolutionary traits. Journal of biological chemistry. 09:5464-5471 [PMID:1672313]

Comments

    No comments found on GM0154


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