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Literature summary for 3.5.1.28 extracted from
- Novel cell wall hydrolase CwlC from Bacillus thuringiensis is essential for mother cell lysis (2018), Appl. Environ. Microbiol., 84, e02640-17 .
Application
| Application | Comment | Organism |
|---|---|---|
| agriculture | Bacillus thuringiensis strains targeting cwlC have the potential to become more effective biological control agents in agricultural applications since the crystal inclusion remains encapsulated in the mother cell at the end of sporulation | Bacillus thuringiensis |
| additional information | cwlC gene deletion completely blocks the release of spores and crystals from the mother cell without affecting insecticidal activity. This may provide an effective strategy for crystal encapsulation against UV light inactivation | Bacillus thuringiensis |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene cwlC or RS15875, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), cwlC is transcribed as a monocistronic unit and its expression is dependent on sporulation sigma factor K | Bacillus thuringiensis |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| E140A | site-directed mutagenesis, catalytically inactive mutant | Bacillus thuringiensis |
| E24A | site-directed mutagenesis, catalytically inactive mutant | Bacillus thuringiensis |
| E24A/E140A | site-directed mutagenesis, catalytically inactive mutant | Bacillus thuringiensis |
| additional information | construction of a deletion by gene replacement in Bacillus thuringiensis strain HD73. Deletion of cwlC completely blocked mother cell lysis during sporulation without impacting the sporulation frequency, Cry1Ac protein production, and insecticidal activity. Engineered Bacillus thuringiensis strains targeting cwlC allow the crystal inclusion to remain encapsulated in the mother cell at the end of sporulation. Although the cwlH, cwlC, or cwlB single mutation do not affect mother cell lysis, cwlB cwlC and cwlC cwlH double deletion mutants show defects in the initiation of mother cell lysis, while the cwlB cwlC cwlH triple deletion mutant has a significant decrease in mother cell lysis | Bacillus thuringiensis |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cell wall | - |
Bacillus thuringiensis | 5618 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus thuringiensis | - |
- |
- |
| Bacillus thuringiensis HD73 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) | Bacillus thuringiensis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | recombinant His-tagged CwlC proteins purified from Escherichia coli were able to directly bind to and digest the Bacillus thuringiensis cell wall | Bacillus thuringiensis | ? | - |
? |  |
| additional information | recombinant His-tagged CwlC proteins purified from Escherichia coli were able to directly bind to and digest the Bacillus thuringiensis cell wall | Bacillus thuringiensis HD73 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 27900-28000, recombinant His-tagged enzyme, SDS-PAGE | Bacillus thuringiensis |
| More | domain analysis | Bacillus thuringiensis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Cell wall hydrolase | - |
Bacillus thuringiensis |
| cwlC | - |
Bacillus thuringiensis |
| MurnAc-lAA | - |
Bacillus thuringiensis |
| RS15875 | - |
Bacillus thuringiensis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Bacillus thuringiensis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | three main cell wall lytic enzymes, CwlB (also named LytC), CwlC, and CwlH, are identified in Bacillus subtilis. CwlB is the major vegetative autolysin produced at the end of exponential growth phase, and it is also present during sporulation. CwlC and CwlH are sporulation-specific autolysins whose production is Sigma K-dependent | Bacillus thuringiensis |
| malfunction | CwlC point mutations at the two conserved catalytic glutamic acid residues, Glu24 and Glu140, result in a complete loss of cell wall lytic activity. The CwlC protein consists of an N-terminal N-acetylmuramoyl-L-alanine amidase (MurNAc-LAA) domain and a C-terminal amidase02 domain. Deletion of cwlC completely blocked mother cell lysis during sporulation without impacting the sporulation frequency, Cry1Ac protein production, and insecticidal activity. Although the cwlH, cwlC, or cwlB single mutation do not affect mother cell lysis, cwlB cwlC and cwlC cwlH double deletion mutants show defects in the initiation of mother cell lysis, while the cwlB cwlC cwlH triple deletion mutant has a significant decrease in mother cell lysis | Bacillus thuringiensis |
| additional information | the two conserved glutamic acid residues, Glu24 and Glu140, are critical for the catalytic activity, CwlC is an N-acetylmuramoyl-L-alanine amidase | Bacillus thuringiensis |
| physiological function | the cell wall hydrolase CwlC from Bacillus thuringiensis is essential for mother cell lysis. CwlC is an essential cell wall hydrolase for Bacillus thuringiensis mother cell lysis during sporulation | Bacillus thuringiensis |
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