Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | inactive pre-proprotein | Geobacillus stearothermophilus | 5829 | - |
extracellular | the enzyme is secreted | Geobacillus stearothermophilus | - |
- |
additional information | the protein is translocated through the membrane at the expense of ATP and the pre-peptide is cleaved off by a type I signal peptidase | Geobacillus stearothermophilus | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ca2+ | protease binds calcium ions in the regions that are involved in the autolytic maturation process, at least one of the calcium ions plays a regulatory role. This calcium ion plays an important role as a switch that modulates the protease between stable and unstable states as appropriate to the biological need | Geobacillus stearothermophilus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Geobacillus stearothermophilus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | autolytic processing. Secreted proteases are produced as prepro-proteins. The pre-peptide is cleaved-off during Sec-controlled secretion, and the active protease emerges outside the cell after folding of the proprotein and autolytic removal of the pro-peptide. The protein is translocated through the membrane at the expense of ATP and the pre-peptide is cleaved off by a type I signal peptidase. The pro-part plays two roles in this process: it facilitates folding by acting as an intra-molecular chaperone and it inhibits protease activity of the folded pro-enzyme | Geobacillus stearothermophilus |
Subunits | Comment | Organism |
---|---|---|
More | TLPs have a two domain structure | Geobacillus stearothermophilus |
Synonyms | Comment | Organism |
---|---|---|
thermolysin-like protease | - |
Geobacillus stearothermophilus |
TLP | - |
Geobacillus stearothermophilus |
General Information | Comment | Organism |
---|---|---|
additional information | life cycle of the thermolysin-like protease from Bacillus stearothermophilus in light of the calcium-dependent stability and instability of the N-terminal domain. | Geobacillus stearothermophilus |