Literature summary extracted from
Wang, L.; Quan, C.; Liu, B.; Wang, J.; Xiong, W.; Zhao, P.; Fan, S.
Functional reconstitution of Staphylococcus aureus truncated AgrC histidine kinase in a model membrane system (2013), PLoS ONE, 8, e80400.
Activating Compound
EC Number |
Activating Compound |
Comment |
Organism |
Structure |
---|
2.7.13.3 |
DTT |
required |
Staphylococcus aureus |
|
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.7.13.3 |
gene agrC, recombinant overexpression of His-tagged and GFP-tagged truncated enzyme from pET-28a-AgrCTM5-6C or pET-28-AgrCTM5-6C-GFP vector in Escherichia coli strain C43(DE3) |
Staphylococcus aureus |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.7.13.3 |
additional information |
construction of a truncated AgrCTM5-6C enzyme version, a hydrophobic polypeptide of 297 amino acids, that has two transmembrane helices connected by a small polar loop that is exposed to the periplasm |
Staphylococcus aureus |
KM Value [mM]
EC Number |
KM Value [mM] |
KM Value Maximum [mM] |
Substrate |
Comment |
Organism |
Structure |
---|
2.7.13.3 |
additional information |
- |
additional information |
kinase activity of recombinant enzyme AgrCTM5-6C in N,N-dimethyldodecylamine N-oxide micelles or proteoliposomes |
Staphylococcus aureus |
|
Localization
EC Number |
Localization |
Comment |
Organism |
GeneOntology No. |
Textmining |
---|
2.7.13.3 |
membrane |
an integral membrane protein, protein transmembrane topology in proteoliposomes is determined using membrane-impermeable and membrane-permeable thiol-reactive reagents, overview |
Staphylococcus aureus |
16020 |
- |
Metals/Ions
EC Number |
Metals/Ions |
Comment |
Organism |
Structure |
---|
2.7.13.3 |
Mg2+ |
required |
Staphylococcus aureus |
|
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
2.7.13.3 |
ATP + protein L-histidine |
Staphylococcus aureus |
- |
ADP + protein N-phospho-L-histidine |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.7.13.3 |
Staphylococcus aureus |
- |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.7.13.3 |
recombinant His-tagged truncated enzyme from Escherichia coli strain C43(DE3) membranes by ultracentrifugation and affinity chromatography, followed by gel filtration |
Staphylococcus aureus |
Renatured (Commentary)
EC Number |
Renatured (Comment) |
Organism |
---|
2.7.13.3 |
purified recombinant truncated enzyme proteins are reconstituted into liposomes by a detergent-mediated method, effect of different detergents on protein reconstitution efficiency, overview. The highest incorporation is found with N,N-dimethyldode-cylamine N-oxide resulting in a yield of 85%, liposomes are consisting of dioleoyl-phosphatidyl-choline : 1,2-dipalmitoyl-sn-glycero-3-phosphocholine : egg L-alpha-phosphatidic acid : cholesterol at molar ratios of 4:4:1:1, pH 7.4. Determination of the morphology and size of liposome, overview |
Staphylococcus aureus |
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.7.13.3 |
ATP + protein L-histidine |
- |
Staphylococcus aureus |
ADP + protein N-phospho-L-histidine |
- |
? |
|
2.7.13.3 |
additional information |
in vitro autokinase activity of recombinant truncated enzyme mutant AgrCTM5-6C in N,N-dimethyldodecylamine N-oxide proteoliposomes |
Staphylococcus aureus |
? |
- |
? |
|
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.7.13.3 |
AgrC |
- |
Staphylococcus aureus |
Temperature Optimum [°C]
EC Number |
Temperature Optimum [°C] |
Temperature Optimum Maximum [°C] |
Comment |
Organism |
---|
2.7.13.3 |
37 |
- |
assay at |
Staphylococcus aureus |
pH Optimum
EC Number |
pH Optimum Minimum |
pH Optimum Maximum |
Comment |
Organism |
---|
2.7.13.3 |
7.4 |
- |
assay at |
Staphylococcus aureus |
Cofactor
EC Number |
Cofactor |
Comment |
Organism |
Structure |
---|
2.7.13.3 |
ATP |
- |
Staphylococcus aureus |
|
General Information
EC Number |
General Information |
Comment |
Organism |
---|
2.7.13.3 |
physiological function |
the integral membrane protein AgrC is a histidine kinase whose sensor domains interact with an autoinducing peptide, resulting in a series of downstream responses |
Staphylococcus aureus |