Application | Comment | Organism |
---|---|---|
agriculture | the beta domain of the IgA1 protease is able to transport alternative proteins to the protease domain of IgA1 protease as N terminal passenger proteins. This technology has been applied to immobilised heavy metals in soil | Haemophilus influenzae |
agriculture | the beta domain of the IgA1 protease is able to transport alternative proteins to the protease domain of IgA1 protease as N terminal passenger proteins. This technology has been applied to immobilised heavy metals in soil | Neisseria gonorrhoeae |
agriculture | the beta domain of the IgA1 protease is able to transport alternative proteins to the protease domain of IgA1 protease as N terminal passenger proteins. This technology has been applied to immobilised heavy metals in soil | Neisseria meningitidis |
agriculture | the beta domain of the IgA1 protease is able to transport alternative proteins to the protease domain of IgA1 protease as N terminal passenger proteins. This technology has been applied to immobilised heavy metals in soil | Streptococcus pneumoniae |
drug development | a fusion protein of the beta domain and a single-chain antibody to transmissible gastroenteritis coronavirus has been expressed on the surface of Escherichia coli. The single-chain antibody is then able to target and block the virus from infecting epithelial cells | Haemophilus influenzae |
drug development | a fusion protein of the beta domain and a single-chain antibody to transmissible gastroenteritis coronavirus has been expressed on the surface of Escherichia coli. The single-chain antibody is then able to target and block the virus from infecting epithelial cells | Neisseria gonorrhoeae |
drug development | a fusion protein of the beta domain and a single-chain antibody to transmissible gastroenteritis coronavirus has been expressed on the surface of Escherichia coli. The single-chain antibody is then able to target and block the virus from infecting epithelial cells | Neisseria meningitidis |
drug development | a fusion protein of the beta domain and a single-chain antibody to transmissible gastroenteritis coronavirus has been expressed on the surface of Escherichia coli. The single-chain antibody is then able to target and block the virus from infecting epithelial cells | Streptococcus pneumoniae |
medicine | inactivation of the enzyme has the potential to reduce bacterial colonisation at mucosal surrfaces | Haemophilus influenzae |
medicine | inactivation of the enzyme has the potential to reduce bacterial colonisation at mucosal surrfaces | Neisseria gonorrhoeae |
medicine | inactivation of the enzyme has the potential to reduce bacterial colonisation at mucosal surrfaces | Neisseria meningitidis |
medicine | inactivation of the enzyme has the potential to reduce bacterial colonisation at mucosal surrfaces | Streptococcus pneumoniae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cell membrane | - |
Haemophilus influenzae | - |
- |
cell membrane | - |
Neisseria gonorrhoeae | - |
- |
cell membrane | - |
Neisseria meningitidis | - |
- |
cell membrane | - |
Streptococcus pneumoniae | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
IgA1 + H2O | Haemophilus influenzae | - |
? | - |
? | |
IgA1 + H2O | Neisseria gonorrhoeae | - |
? | - |
? | |
IgA1 + H2O | Neisseria meningitidis | - |
? | - |
? | |
IgA1 + H2O | Streptococcus pneumoniae | - |
? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Haemophilus influenzae | - |
- |
- |
Neisseria gonorrhoeae | - |
- |
- |
Neisseria meningitidis | - |
- |
- |
Streptococcus pneumoniae | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
IgA1 + H2O | - |
Haemophilus influenzae | ? | - |
? | |
IgA1 + H2O | - |
Neisseria gonorrhoeae | ? | - |
? | |
IgA1 + H2O | - |
Neisseria meningitidis | ? | - |
? | |
IgA1 + H2O | - |
Streptococcus pneumoniae | ? | - |
? | |
additional information | in vitro studies show that the enzyme also cleaves human chorionic gonadotrophin hormone, granulocyte-macrophage colony stimulating factor, the CD8 surface antigen of cytotoxic T lymphocytes and LAMP 1 a membrane glycoprotein of lysosomes | Haemophilus influenzae | ? | - |
? | |
additional information | in vitro studies showed that the enzyme also cleaves human chorionic gonadotrophin hormone, granulocyte-macrophage colony stimulating factor, the CD8 surface antigen of cytotoxic T lymphocytes and LAMP 1 a membrane glycoprotein of lysosomes | Neisseria gonorrhoeae | ? | - |
? | |
additional information | in vitro studies showed that the enzyme also cleaves human chorionic gonadotrophin hormone, granulocyte-macrophage colony stimulating factor, the CD8 surface antigen of cytotoxic T lymphocytes and LAMP 1 a membrane glycoprotein of lysosomes | Neisseria meningitidis | ? | - |
? | |
additional information | in vitro studies showed that the enzyme also cleaves human chorionic gonadotrophin hormone, granulocyte-macrophage colony stimulating factor, the CD8 surface antigen of cytotoxic T lymphocytes and LAMP 1 a membrane glycoprotein of lysosomes | Streptococcus pneumoniae | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
IgA1 protease | - |
Haemophilus influenzae |
IgA1 protease | - |
Neisseria gonorrhoeae |
IgA1 protease | - |
Neisseria meningitidis |
IgA1 protease | - |
Streptococcus pneumoniae |