Detail of GM0005
Summary
The genetically modified enzybiotic, named CHL , constructed by Domains Assembly strategy, change or extend lytic spectrum.With CHL
Sequence Length: 501 AA.
Mass: 57305 Da.
Isoelectric Point: 4.57
Function: The chimeric enzyme behaves as a chuline-dependent enzyme and its activity is comparable to that of the parent enzymes.
Construction
GM0005, constructed by Domains Assembly strategy. No schema construted on GM0005
Details:
GM0005[1-185]: derive from protein P15057 sequence 1-185
P15057, 339 AA., the CP-1 lysin 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
GM0005[186-503]: derive from protein P32762 sequence 1-318
P32762, 318 AA., the Lytic amidase from Streptococcus pneumoniae phage HB-3
Source: Streptococcus pneumoniae phage HB-3
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?
Molecular Function: 0008745, the N-acetylmuramoyl-L-alanine amidase activity
Linking to UniprotKB
Linging to InterPro
Domains and repeats
10-170: IPR002502, the N-acetylmuramoyl-L-alanine amidase domain175-194: 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
Molecular Function: 0009253, the peptidoglycan catabolic processMolecular Function: 0008745, the N-acetylmuramoyl-L-alanine amidase activity
Linking to UniprotKB
Linging to InterPro
Annotation
1-185
186-503
1-183
: EAD, Lysozyme domain, derived from Pneumococcal phage Cp-1 endolysin Cpl1;184-318
: EAD, Amidase domain, derived from Pneumococcal phage endolysin HBL3;319-482
: CBD, choline-binding domain, derived from Pneumococcal phage endolysin HBL3;Domain and repeats:
195-355
: IPR002502,N-acetylmuramoyl-L-alanine amidase domain; 3-185
: IPR017853,Glycoside hydrolase, catalytic domain?; 360-379
: IPR018337,Cell wall/choline-binding repeat?; 381-400
: IPR018337,Cell wall/choline-binding repeat?; 402-422
: IPR018337,Cell wall/choline-binding repeat?; 423-442
: IPR018337,Cell wall/choline-binding repeat?; 443-462
: IPR018337,Cell wall/choline-binding repeat?; 465-486
: IPR018337,Cell wall/choline-binding repeat?; GO term prediction:
0008745, the N-acetylmuramoyl-L-alanine amidase activity
0009253, the peptidoglycan catabolic process
DLFVDVSSHNGYDITGILEQMGTTNTIIKISESTTYLNPCLSAQVEQSNPIGFYHFARFGGDVAEAEREAQFFLDNVPMQVKYLVLDYEDDPSGDAQANTNACLRFMQMIADAGYKPIYYSYKPFTHDNVDYQQILAQFPNSLWIAGYGLNDGTANFEYFPSMDGIRWWQYSSNPFDKNIVLL-MDIDRNRLRTGLPQVGVQPYRQVHAHSTGNRNSTVQNEADYHWRKDPELGFFSHVVGNFRIMQVGPVNNGSWDVGGGWNAETYAAVELIESHSTKEEFMADYRLYIELLRNLADEAGLPKTLDTDDLAGIKTHEYCTNNQPNNHSDHVDPYPY-LASWGISREQFKQDIENGLSAATGWQKNGTGYWYVHSDGSYSKDKFEKINGTWYYFDGSGYMLSDRWKKHTDGNWYYFDQSGEMATGWKKIADKWYYFDVEGAMKTGWVKYKDTWYYLDAKEGAMVSNAFIQSADGTGWYYLKPDGTLADKPEFTVEPDGLITVK
Production
1. Expressed by in E. coli TG1, Purified by affinity chromatography on DEAE-celluloseActivity
No activity data found on GM0005Reference
1. Jesus M. SANZ, Pedro GARCIA and Josei. CARCIA. (1996) Construction of a multifunctional pneumococcal murein hydrolase by module assembly. Eur. J. Biochem.. 235:601-605. [doi:10.1111/j.1432-1033.1996.00601.x] [PMID:8654407]Comments
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