Activating Compound | Comment | Organism | Structure |
---|---|---|---|
DTT | required | Staphylococcus aureus |
Cloned (Comment) | Organism |
---|---|
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 | Comment | Organism |
---|---|---|
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] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinase activity of recombinant enzyme AgrCTM5-6C in N,N-dimethyldodecylamine N-oxide micelles or proteoliposomes | Staphylococcus aureus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
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 | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Staphylococcus aureus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + protein L-histidine | Staphylococcus aureus | - |
ADP + protein N-phospho-L-histidine | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Staphylococcus aureus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged truncated enzyme from Escherichia coli strain C43(DE3) membranes by ultracentrifugation and affinity chromatography, followed by gel filtration | Staphylococcus aureus |
Renatured (Comment) | Organism |
---|---|
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 | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + protein L-histidine | - |
Staphylococcus aureus | ADP + protein N-phospho-L-histidine | - |
? | |
additional information | in vitro autokinase activity of recombinant truncated enzyme mutant AgrCTM5-6C in N,N-dimethyldodecylamine N-oxide proteoliposomes | Staphylococcus aureus | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
AgrC | - |
Staphylococcus aureus |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Staphylococcus aureus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Staphylococcus aureus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Staphylococcus aureus |
General Information | Comment | Organism |
---|---|---|
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 |