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Literature summary for 3.1.1.74 extracted from
- Extracellular expression of Thermobifida fusca cutinase with pelB signal peptide depends on more than type II secretion pathway in Escherichia coli (2015), J. Biotechnol., 204, 47-52 .
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Thermobifida fusca |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| S130A | catalytically inactive | Thermobifida fusca |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermobifida fusca | Q47RJ6 | - |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Tfu_0883 | - |
Thermobifida fusca |
General Information
| General Information | Comment | Organism |
|---|---|---|
| physiological function | expression of cutinase fused to pelB signal peptide in a secB knockout strain, defective in type II secretion pathway, still leads to accumulation of cutinase in the culture medium. The phospholipid hydrolase activity of pelB-cutinase plays a role in its extracellular production | Thermobifida fusca |
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Release 2023.1 (January 2023)
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