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Literature summary for 2.7.13.3 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.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
DTT required Staphylococcus aureus

Cloned(Commentary)

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

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 [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

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

Metals/Ions Comment Organism Structure
Mg2+ required Staphylococcus aureus

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Staphylococcus aureus
-
-
-

Purification (Commentary)

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 (Commentary)

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 and Products (Substrate)

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

Synonyms Comment Organism
AgrC
-
Staphylococcus aureus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Staphylococcus aureus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Staphylococcus aureus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Staphylococcus aureus

General Information

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