Detail of GM0150


Summary

The genetically modified enzybiotic, named Clc , constructed by Domains Assembly strategy, change or extend lytic spectrum.
With  Clc
  Sequence Length:  352 AA.
  Mass:  39706.9 Da.
  Isoelectric Point:  4.39
  Function:  

Construction

GM0150, constructed by Domains Assembly strategy.
    No schema construted on GM0150
Details:
GM0150[1-193]: derive from protein P34020 sequence 1-193

P34020, 324 AA., the Autolytic lysozyme EC=3.2.1.17 from Clostridium acetobutylicum (strain ATCC 824 / DSM

Source: Clostridium acetobutylicum (strain ATCC 824 / DSM

Domains and repeats

1 - 181:  IPR017853, the Glycoside hydrolase, superfamily
190 - 252:  IPR002477, the Peptidoglycan binding-like
277 - 320:  IPR002477, the Peptidoglycan binding-like

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
GM0150[194-348]: derive from protein P15057 sequence 185-339

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

Annotation

1-193
194-348

1-192
: EAD, Lysozyme domain, derived from autolysin (LYC muramidase) of Clostridium acetobutylicum ATCC824;
197-351
: CBD, choline-binding domain, derived from choline-binding domain of the pneumococcal phage CPL1 muramidase;
Domain and repeats:
1-193
: IPR002477,Peptidoglycan binding-like;
1-193
: IPR002477,Peptidoglycan binding-like;
1-193
: IPR017853,Glycoside hydrolase, superfamily;
229-248
: IPR018337,Cell wall/choline-binding repeat;
250-269
: IPR018337,Cell wall/choline-binding repeat;
270-289
: IPR018337,Cell wall/choline-binding repeat;
290-310
: IPR018337,Cell wall/choline-binding repeat;
312-331
: IPR018337,Cell wall/choline-binding repeat;
GO term prediction:
MKGIDIYSGQGSVDFNAVKESGVEVVYIKATEGLTYTDSTYKDFYDGAKNAGLKIGFYHYLRANDPTSEAEHFFNTISGLSLDCKCAIDVEVTLGQSIDQISSNVRKFADYLINKGLDVCVYTYTNFYKDNLNSTVKDLPLWIAEYGVSKPNIDASYVGFQYSDSGSVNGISGSADLDEFSEGILVGGTVVIDP-RVPIVLLDDEEDDKPKTAGTWKQDSKGWWFRRNNGSFPYNKWEKIGGVWYYFDSKGYCLTSEWLKDNEKWYYLK DNGAMATGWVLVGSEWYYMDDSGAMVTGWVKYKNNWYYMTNERGNMVSNEFIKSGKGWYFMNTNGELADNPSFTKEPDGLITVA
  BlastP to GMEnzy

Production

  1.  Expressed by pCLC100 in E. coli HB101,  Purified by affinity chromatography on DEAE-cellulose

Activity

    No activity data found on GM0150

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. Croux, C.Ronda, C.Lopez, R.Garcia, J. L.. (1993) Interchange of functional domains switches enzyme specificity: construction of a chimeric pneumococcal-clostridial cell wall lytic enzyme. Molecular microbiology. 05:1019-1025. [doi:10.1111/j.1365-2958.1993.tb01231.x] [PMID:7934908]

Comments

    No comments found on GM0150


CAPTCHA Image   Reload Image
Enter Code*: