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Literature summary for 2.7.13.3 extracted from
- The heme-binding protein HbpS regulates the activity of the Streptomyces reticuli iron-sensing histidine kinase SenS in a redox-dependent manner (2008), Amino Acids, 37, 681-691.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| heme-binding protein HbpS | inhibits autophosphorylation activity of the enzyme in absence of redox reagents and hemin, but activates slightly in presence of hemin and strongly in presence of FeCl2 and FeCl3, DTT increases the activation with FeCl2, but inhibits activation with FeCl3, while H2O2 strongly increases the activation by FeCl2 and completely inhibits activation with FeCl3, overview | Streptomyces reticuli | |
| hemin | activates slightly in presence of HbpS | Streptomyces reticuli |  |
| additional information | hemin-treated HbpS enhances SenS autophosphorylation by 30fold under redox conditions using either H2O2 or dithiothreitol | Streptomyces reticuli |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expressed in Escherichia coli BL21(DE3) cells | Streptomyces reticuli |
| gene senS, expression of His-tagged enzyme in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain XL-1 Blue | Streptomyces reticuli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | construction of a senS disruption and a truncated mutant | Streptomyces reticuli |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| HbpS | heme-free HbpS represses the autokinase activity of SenS | Streptomyces reticuli | |
| heme-binding protein HbpS | inhibits autophosphorylation activity of the enzyme in absence of redox reagents and hemin, but activates slightly in presence of hemin and strongly in presence of FeCl2 and FeCl3, DTT increases the activation with FeCl2, but inhibits activation with FeCl3, while H2O2 strongly increases the activation by FeCl2 and completely inhibits activation with FeCl3, overview | Streptomyces reticuli |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| membrane | - |
Streptomyces reticuli | 16020 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | the presence of iron ions alone or in combination with H2O2 or dithiothreitol leads to significantly increased phosphorylation levels of SenS. 0.005 mM Fe2+ is able to enhance the phosphorylation level of SenS by a factor of 10 relative to the basal level, a combination of FeCl2 and H2O2 increases autophosphorylation activity by a factor of 20 | Streptomyces reticuli | |
| Fe3+ | 0.005 mM Fe3+ is able to enhance the phosphorylation level of SenS by a factor of 10 relative to the basal level | Streptomyces reticuli | |
| FeCl2 | enhances SenS autokinase activity in presence of HbpS, the activation is unaffected by DTT, but is enhanced by H2O2 | Streptomyces reticuli | |
| FeCl3 | enhances SenS autokinase activity strongly in presence of HbpS, H2O2 and DTT inhibit the activation | Streptomyces reticuli | |
| Mg2+ | - |
Streptomyces reticuli | |
| additional information | the autokinase activity of SenS is not affeted by Zn2+, H2O2, and DTT | Streptomyces reticuli | |
| additional information | the combination of 5 mM dithiothreitol and 0.005 mM FeCl2, or 5 mM dithiothreitol and 0.005 mM FeCl3, or 0.005 mM FeCl3 and 5 mM H2O2 has no effect on phosphorylation level of SenS, H2O2 prevents the activation by Fe3+ | Streptomyces reticuli | |
| additional information | ZnCl2 is not able to change the autokinase activity of SenS | Streptomyces reticuli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Streptomyces reticuli | the SenS/SenR system of Streptomyces reticuli regulates the expression of the redox regulator FurS, the catalase-peroxidase CpeB and the heme-binding protein HbpS. SenS/SenR also participates in sensing redox changes, mediated by HbpS. The heme-binding protein HbpS regulates the activity of the Streptomyces reticuli iron-sensing histidine kinase SenS in a redox-dependent manner, presence of SenS/SenR leads to the synthesis of extracellular redox active proteins, overview | ? | - |
? | |
| additional information | Streptomyces reticuli Tue54 | the SenS/SenR system of Streptomyces reticuli regulates the expression of the redox regulator FurS, the catalase-peroxidase CpeB and the heme-binding protein HbpS. SenS/SenR also participates in sensing redox changes, mediated by HbpS. The heme-binding protein HbpS regulates the activity of the Streptomyces reticuli iron-sensing histidine kinase SenS in a redox-dependent manner, presence of SenS/SenR leads to the synthesis of extracellular redox active proteins, overview | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Streptomyces reticuli | - |
- |
- |
| Streptomyces reticuli | - |
gene senS | - |
| Streptomyces reticuli Tue54 | - |
- |
- |
| Streptomyces reticuli Tue54 | - |
gene senS | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| phosphoprotein | - |
Streptomyces reticuli |
| phosphoprotein | SenS performs autophosphorylation | Streptomyces reticuli |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| Ni2+-NTA column chromatography, gel filtration | Streptomyces reticuli |
| recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography | Streptomyces reticuli |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
activities of wild-type and truncated mutant SenS under different conditions, overview | Streptomyces reticuli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + protein L-histidine | - |
Streptomyces reticuli | ADP + protein N-phospho-L-histidine | - |
? | |
| ATP + protein L-histidine | - |
Streptomyces reticuli Tue54 | ADP + protein N-phospho-L-histidine | - |
? | |
| additional information | the SenS/SenR system of Streptomyces reticuli regulates the expression of the redox regulator FurS, the catalase-peroxidase CpeB and the heme-binding protein HbpS. SenS/SenR also participates in sensing redox changes, mediated by HbpS. The heme-binding protein HbpS regulates the activity of the Streptomyces reticuli iron-sensing histidine kinase SenS in a redox-dependent manner, presence of SenS/SenR leads to the synthesis of extracellular redox active proteins, overview | Streptomyces reticuli | ? | - |
? | |
| additional information | SenS performs autophosphorylation. HbpS/SenS interaction analysis, overview | Streptomyces reticuli | ? | - |
? | |
| additional information | the SenS/SenR system of Streptomyces reticuli regulates the expression of the redox regulator FurS, the catalase-peroxidase CpeB and the heme-binding protein HbpS. SenS/SenR also participates in sensing redox changes, mediated by HbpS. The heme-binding protein HbpS regulates the activity of the Streptomyces reticuli iron-sensing histidine kinase SenS in a redox-dependent manner, presence of SenS/SenR leads to the synthesis of extracellular redox active proteins, overview | Streptomyces reticuli Tue54 | ? | - |
? | |
| additional information | SenS performs autophosphorylation. HbpS/SenS interaction analysis, overview | Streptomyces reticuli Tue54 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| iron-sensing histidine kinase | - |
Streptomyces reticuli |
| SenS | - |
Streptomyces reticuli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Streptomyces reticuli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Streptomyces reticuli |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| ATP | - |
Streptomyces reticuli | |
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