Activating Compound | Comment | Organism | Structure |
---|---|---|---|
casein | 2.5fold activation | Bacteria | |
DKVLVVWAGQQ | full-length denatured alpha-amylase, as well as alpha-amylase fragments and the C-terminus of alpha-amylase, amplify DegP proteolysis | Bacteria | |
DNRNGNVYDF | - |
Bacteria | |
DNRNGNVYFF | 2.5fold activation | Bacteria | |
DNRNGNVYGF | - |
Bacteria | |
DNRNGNVYIF | - |
Bacteria | |
DNRNGNVYKF | - |
Bacteria | |
DNRNGNVYLF | - |
Bacteria | |
DNRNGNVYQF | 1.5fold activation | Bacteria | |
DNRNGNVYSF | - |
Bacteria | |
DNRNGNVYWF | 2fold activation | Bacteria | |
DNRNGNVYYF | - |
Bacteria | |
IVALGLVYQF | outer membrane porin C, 3fold activation | Bacteria | |
YTMKAAGLGK | alkaline phosphatase A | Bacteria |
Application | Comment | Organism |
---|---|---|
additional information | the bacterial protein quality control factor DegP is allosterically regulated by model peptides mimicking cellular stress signals. Strategy for the development of antimicrobials | Bacteria |
Protein Variants | Comment | Organism |
---|---|---|
R262A | completely abolishes proteolytic activation | Bacteria |
V328S | completely abolishes proteolytic activation | Bacteria |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacteria | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | no cleavage of STDGGV-para-nitroaniline and SKAKGGEEPLPEGV-para-nitroaniline | Bacteria | ? | - |
? | |
SPMFKGV-p-nitroanilide + H2O | - |
Bacteria | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DegP | - |
Bacteria |
HtrA protease | - |
Bacteria |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.56 | - |
SPMFKGV-para-nitroaniline | - |
Bacteria |