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Literature summary extracted from
- The HtrA family of proteases: implications for protein composition and cell fate (2002), Mol. Cell, 10, 443-455.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.107 | additional information | largely indpependent of activating compounds such as reducing agents | Escherichia coli |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.107 | diisopropylfluorophosphate | - |
Escherichia coli |  |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.4.21.107 | chloroplast | - |
Arabidopsis thaliana | 9507 | - |
| 3.4.21.107 | periplasm | - |
Escherichia coli | - |
- |
| 3.4.21.107 | periplasm | - |
Rickettsia sp. | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.107 | additional information | largely independent of divalent cations | Escherichia coli |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.107 | additional information | Arabidopsis thaliana | involved in the degradation of damaged proteins | ? | - |
? | |
| 3.4.21.107 | additional information | Homo sapiens | involved in the degradation of damaged proteins, involved in arthritis, cell growth, stress response, apoptosis and aging, possible tumor suppressor function | ? | - |
? | |
| 3.4.21.107 | additional information | Escherichia coli | involved in the degradation of damaged proteins, switches from chaperone to protease function in a temperature-dependent manner | ? | - |
? | |
| 3.4.21.107 | Protein + H2O | Escherichia coli | - |
? | - |
? | |
| 3.4.21.107 | Protein + H2O | Homo sapiens | - |
? | - |
? | |
| 3.4.21.107 | Protein + H2O | Arabidopsis thaliana | - |
? | - |
? | |
| 3.4.21.107 | Protein + H2O | Rickettsia sp. | - |
? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.4.21.107 | Arabidopsis thaliana | - |
- |
- |
| 3.4.21.107 | Escherichia coli | - |
- |
- |
| 3.4.21.107 | Homo sapiens | - |
- |
- |
| 3.4.21.107 | Rickettsia sp. | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.4.21.107 | colon | alternative splice form lacing exons 3 and 7 | Homo sapiens | - |
| 3.4.21.107 | fibroblast | - |
Homo sapiens | - |
| 3.4.21.107 | kidney | alternative splice form lacing exons 3 and 7 | Homo sapiens | - |
| 3.4.21.107 | thyroid gland | alternative splice form lacing exons 3 and 7 | Homo sapiens | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.4.21.107 | amylase MalS + H2O | - |
Rickettsia sp. | ? | - |
? | |
| 3.4.21.107 | beta-casein + H2O | cleaves beta-casein yielding several polypeptide fragments | Escherichia coli | ? | - |
? | |
| 3.4.21.107 | D1 protein + H2O | degrades photodamaged D1 protein of photosystem II | Arabidopsis thaliana | ? | - |
? | |
| 3.4.21.107 | additional information | acts on substrates that are at least partially unfolded, does not cleave stably folded proteins, acts as a general chaperone forming stable complexes with several misfolded proteins | Escherichia coli | ? | - |
? | |
| 3.4.21.107 | additional information | involved in the degradation of damaged proteins | Arabidopsis thaliana | ? | - |
? | |
| 3.4.21.107 | additional information | involved in the degradation of damaged proteins, involved in arthritis, cell growth, stress response, apoptosis and aging, possible tumor suppressor function | Homo sapiens | ? | - |
? | |
| 3.4.21.107 | additional information | involved in the degradation of damaged proteins, switches from chaperone to protease function in a temperature-dependent manner | Escherichia coli | ? | - |
? | |
| 3.4.21.107 | Protein + H2O | - |
Escherichia coli | ? | - |
? | |
| 3.4.21.107 | Protein + H2O | - |
Homo sapiens | ? | - |
? | |
| 3.4.21.107 | Protein + H2O | - |
Arabidopsis thaliana | ? | - |
? | |
| 3.4.21.107 | Protein + H2O | - |
Rickettsia sp. | ? | - |
? | |
| 3.4.21.107 | Protein + H2O | cleaves preferably at hydrophobic side chains at the P1 position | Escherichia coli | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.4.21.107 | hexamer | two trimeric rings for a functional DegP hexamer | Escherichia coli |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.4.21.107 | DegP | - |
Arabidopsis thaliana |
| 3.4.21.107 | DegP | - |
Rickettsia sp. |
| 3.4.21.107 | HtrA | - |
Homo sapiens |
| 3.4.21.107 | HtrA | classification of proteases | Escherichia coli |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.4.21.107 | 20 | 30 | almost no activity below 20°C, activity rapidly increases above 30°C | Escherichia coli |
Cofactor
| EC Number | Cofactor | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.4.21.107 | additional information | largely indpependent of cofactors such as ATP | Escherichia coli |
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Release 2023.1 (January 2023)
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