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
190 - 252: IPR002477, the Peptidoglycan binding-like
277 - 320: IPR002477, the Peptidoglycan binding-like
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
Domains and repeats
1 - 181: IPR017853, the Glycoside hydrolase, superfamily190 - 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
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
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
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 processBiological 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
Production
1. Expressed by pCLC100 in E. coli HB101, Purified by affinity chromatography on DEAE-celluloseActivity
No activity data found on GM0150Reference
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]