Detail of GM0152
Summary
The genetically modified enzybiotic, named LCA , constructed by Domains Assembly strategy, change or extend lytic spectrum.With LCA
Sequence Length: 315 AA.
Mass: 36242 Da.
Isoelectric Point: 5.07
Function: LCA exhibited amidase activities at levels similar to LYTA and switched the regulatory properties to CPL1.
Construction
GM0152, constructed by Domains Assembly strategy. No schema construted on GM0152
Details:
GM0152[1-187]: derive from protein Q8KLP2 sequence 1-187
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
GM0152[188-316]: derive from protein P15057 sequence 212-339
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
1-187
188-316
1-187
: EAD, Amidase domain, derived from S. pneumoniae 101 LytAlOl amidase;188-316
: CBD, cpl1 domain, derived from Pneumococcal phage Cp-1 endolysin Cpl1;Domain and repeats:
1-187
: IPR018337,Cell wall/choline-binding repeat; 1-187
: IPR018337,Cell wall/choline-binding repeat; 1-187
: IPR002502,N-acetylmuramoyl-L-alanine amidase domain; 1-187
: IPR018337,Cell wall/choline-binding repeat; 1-187
: IPR018337,Cell wall/choline-binding repeat; 1-187
: IPR018337,Cell wall/choline-binding repeat; 1-187
: IPR018337,Cell wall/choline-binding repeat; 196-216
: IPR018337,Cell wall/choline-binding repeat; 217-237
: IPR018337,Cell wall/choline-binding repeat; 237-257
: IPR018337,Cell wall/choline-binding repeat; 257-278
: IPR018337,Cell wall/choline-binding repeat; 279-299
: IPR018337,Cell wall/choline-binding repeat; GO term prediction:
0008745, the N-acetylmuramoyl-L-alanine amidase activity
0009253, the peptidoglycan catabolic process
MEINVSKLRTDLPQVGVQPYRQVHAHSTGNPHSTVQNEADYHWRKDPELGFFSHIVGNGCIMQVGPVDNGAWDVGGGWNAETYAAVELIESHSTKEEFMTDYRLYIELLRNLADEAGLPKTLDTGSLAGIKTHEYCTNNQPNNHSDHVDPYPYLAKWGISREQFKHDIENGLTIETGWQKNDTGYWY-RRNNGSFPYNKWEKIGGVWYYFDSKGYCLTSEWLKDNEKWYYLKDNGAMATGWVLVGSEWYYMDDSGAMVTGWVKYKNNWYYMTNERGNMVSNEFIKSGKGWYFMNTNGELADNPSFTKEPDGLITVA
Production
1. Expressed by pCL in E. coli HB101, Purified by affinity chromatography on DEAE-celluloseReference
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.. (1990) Chimeric phage-bacterial enzymes: a clue to the modular evolution of genes. Proceedings of the National Academy of Sciences of. 020:8125-8129. [doi:10.1073/pnas.87.20.8125] [PMID:1978320] [FULL TEXT]