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Literature summary extracted from
- Functional domains of Brevibacillus thermoruber lon protease for oligomerization and DNA binding: role of N-terminal and sensor and substrate discrimination domains (2004), J. Biol. Chem., 279, 34903-34912.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.4.21.53 | - |
Brevibacillus thermoruber |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.4.21.53 | additional information | design of truncated enzyme mutants. N-terminal domain is essential for oligomerization. Truncation of N-terminal domain also leads to inactivation of proteolytic, ATPase, and chaperone-like activities of enzyme but retains the DNA-binding activity | Brevibacillus thermoruber |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.53 | 90000 | - |
x * 90000, SDS-PAGE | Brevibacillus thermoruber |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.53 | Brevibacillus thermoruber | Q84FG5 | stain WR-249 | - |
| 3.4.21.53 | Brevibacillus thermoruber WR-249 | Q84FG5 | stain WR-249 | - |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.21.53 | ? | x * 90000, SDS-PAGE | Brevibacillus thermoruber |
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