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. No schema construted on GM0154
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
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
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
Domains and repeats
3-185: IPR013781, the Glycoside hydrolase, catalytic domain205-246: 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 processBiological 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
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 - 151: 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
Biological Process: 0009253, the peptidoglycan catabolic process?Molecular Function: 0008745, the N-acetylmuramoyl-L-alanine amidase activity?
Linking to UniprotKB
Linging to InterPro
Annotation
1-203
204-344
1-203
: EAD, Lysozyme domain, derived from Pneumococcal phage CP-7 endolysin Cpl7;204-344
: CBD, lytA domain, derived from S. pneumoniae 101 LytAlOl amidase;Domain and repeats:
1-203
: IPR013168,Cpl-7 lysozyme, C-terminal ; 1-203
: IPR013168,Cpl-7 lysozyme, C-terminal; 1-203
: IPR013168,Cpl-7 lysozyme, C-terminal ; 1-203
: IPR017853,Glycoside hydrolase, superfamily; 204-344
: IPR018337,Cell wall/choline-binding repeat; 204-344
: IPR018337,Cell wall/choline-binding repeat; 204-344
: IPR002502,N-acetylmuramoyl-L-alanine amidase domain; 204-344
: IPR018337,Cell wall/choline-binding repeat; 204-344
: IPR018337,Cell wall/choline-binding repeat; 204-344
: IPR018337,Cell wall/choline-binding repeat; 204-344
: IPR018337,Cell wall/choline-binding repeat; 3-185
: IPR013781,Glycoside hydrolase, catalytic domain; GO term prediction:
0005975, the carbohydrate metabolic process
0008745, the N-acetylmuramoyl-L-alanine amidase activity
0009253, the peptidoglycan catabolic process
MVKKNDLFVDVASHQGYDISGILEEAGTTNTIIKVSESTSYLNPCLSAQVSQSNPIGFYHFAWFGGNEEEAEAEARYFLDNVPTQVKYLVLDYEDHASASVQRNTTACLRFMQIIAEAGYTPIYYSYKPFTLDNVDYQQILAQFPNSLWIAGYGLNDGTANFEYFPSMDGIRWWQYSSNPFDKNIVLLDDEKEDNINNENTLQ-KNDTGYWYVHSDGSYPKDKFEKINGTWYYFDSSGYMLADRWRKHTDGNWYWFDNSGEMATGWKKIADKWYYFNEEGAMKTGWVKYKDTWYYLDAKEGAMVSNAFIQSADGTGWYYLKPDGTLADKPEFTVEPDGLITVK
Production
1. Expressed by pLC7 in E. coli DHl, Purified by Bio-Gel P-60Activity
No activity data found on GM0154Reference
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]