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Literature summary extracted from

  • Bogel, G.; Schrempf, H.; Ortiz de Orue Lucana, D.
    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.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.13.3 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
2.7.13.3 hemin activates slightly in presence of HbpS Streptomyces reticuli
2.7.13.3 additional information hemin-treated HbpS enhances SenS autophosphorylation by 30fold under redox conditions using either H2O2 or dithiothreitol Streptomyces reticuli

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.13.3 expressed in Escherichia coli BL21(DE3) cells Streptomyces reticuli
2.7.13.3 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

EC Number Protein Variants Comment Organism
2.7.13.3 additional information construction of a senS disruption and a truncated mutant Streptomyces reticuli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.13.3 HbpS heme-free HbpS represses the autokinase activity of SenS Streptomyces reticuli
2.7.13.3 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

EC Number Localization Comment Organism GeneOntology No. Textmining
2.7.13.3 membrane
-
 Streptomyces reticuli 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.13.3 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
2.7.13.3 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
2.7.13.3 FeCl2 enhances SenS autokinase activity in presence of HbpS, the activation is unaffected by DTT, but is enhanced by H2O2 Streptomyces reticuli
2.7.13.3 FeCl3 enhances SenS autokinase activity strongly in presence of HbpS, H2O2 and DTT inhibit the activation Streptomyces reticuli
2.7.13.3 Mg2+
-
 Streptomyces reticuli
2.7.13.3 additional information the autokinase activity of SenS is not affeted by Zn2+, H2O2, and DTT Streptomyces reticuli
2.7.13.3 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
2.7.13.3 additional information ZnCl2 is not able to change the autokinase activity of SenS Streptomyces reticuli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.13.3 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 ?
-
 ?
2.7.13.3 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

EC Number Organism UniProt Comment Textmining
2.7.13.3 Streptomyces reticuli
-
-
-
2.7.13.3 Streptomyces reticuli
-
 gene senS
-
2.7.13.3 Streptomyces reticuli Tue54
-
-
-
2.7.13.3 Streptomyces reticuli Tue54
-
 gene senS
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.13.3 phosphoprotein
-
 Streptomyces reticuli
2.7.13.3 phosphoprotein SenS performs autophosphorylation Streptomyces reticuli

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.13.3 Ni2+-NTA column chromatography, gel filtration Streptomyces reticuli
2.7.13.3 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Streptomyces reticuli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.13.3 additional information
-
 activities of wild-type and truncated mutant SenS under different conditions, overview Streptomyces reticuli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.13.3 ATP + protein L-histidine
-
 Streptomyces reticuli ADP + protein N-phospho-L-histidine
-
 ?
2.7.13.3 ATP + protein L-histidine
-
 Streptomyces reticuli Tue54 ADP + protein N-phospho-L-histidine
-
 ?
2.7.13.3 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 ?
-
 ?
2.7.13.3 additional information SenS performs autophosphorylation. HbpS/SenS interaction analysis, overview Streptomyces reticuli ?
-
 ?
2.7.13.3 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 ?
-
 ?
2.7.13.3 additional information SenS performs autophosphorylation. HbpS/SenS interaction analysis, overview Streptomyces reticuli Tue54 ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.13.3 iron-sensing histidine kinase
-
 Streptomyces reticuli
2.7.13.3 SenS
-
 Streptomyces reticuli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.13.3 30
-
 assay at Streptomyces reticuli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.13.3 7.5
-
 assay at Streptomyces reticuli

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.13.3 ATP
-
 Streptomyces reticuli