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Literature summary for 3.6.4.10 extracted from
- Biochemical characterization of the apicoplast-targeted AAA+ ATPase ClpB from Plasmodium falciparum (2013), Biochem. Biophys. Res. Commun., 439, 191-195.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| casein | - |
Plasmodium falciparum |  |
| polylysine | - |
Plasmodium falciparum | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| apicoplast | - |
Plasmodium falciparum | 20011 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Mg2+ | required | Plasmodium falciparum | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | Plasmodium falciparum | - |
ADP + phosphate | - |
? | |
| additional information | Plasmodium falciparum | PfClpB1 reactivates aggregated firefly luciferase, but the PfClpB1-mediated aggregate reactivation is inhibited in the presence of Escherichia coli DnaK, DnaJ, and GrpE. The lack of effective cooperation between PfClpB1 and the bacterial DnaK system may arise from the Plasmodium-specific sequence of the ClpB middle domain. The recombinant PfClpB1 interacts with and reactivates aggregated luciferase even in the absence of the co-chaperones | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Plasmodium falciparum | Q8IB03 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| proteolytic modification | the enzyme contains the endoplasmic reticulum-targeting signal sequence with the predicted signal peptide cleavage between Ser23 and Lys24 in PfClpB1 | Plasmodium falciparum |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + H2O | - |
Plasmodium falciparum | ADP + phosphate | - |
? | |
| additional information | PfClpB1 reactivates aggregated firefly luciferase, but the PfClpB1-mediated aggregate reactivation is inhibited in the presence of Escherichia coli DnaK, DnaJ, and GrpE. The lack of effective cooperation between PfClpB1 and the bacterial DnaK system may arise from the Plasmodium-specific sequence of the ClpB middle domain. The recombinant PfClpB1 interacts with and reactivates aggregated luciferase even in the absence of the co-chaperones | Plasmodium falciparum | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| hexamer | the biologically active form of bacterial ClpB is a cylinder-shaped homohexamer. The self-association of ClpB into hexamers is induced by nucleotide binding | Plasmodium falciparum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AAA+ ATPase ClpB | - |
Plasmodium falciparum |
| ClpB | - |
Plasmodium falciparum |
| PfClpB1 | - |
Plasmodium falciparum |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 37 | - |
assay at | Plasmodium falciparum |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
aggregate reactivation activity at | Plasmodium falciparum |
| 8 | - |
ATPase activity at | Plasmodium falciparum |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | ClpB is a molecular chaperone from the AAA+ superfamily of ATPases, Hsp100 subfamily of AAA+ ATPases | Plasmodium falciparum |
| additional information | the enzyme structure contains two highly-conserved ATP-binding modules D1 and D2, the N-terminal domain, and the middle domain. The nucleotide-binding Walker A/B and sensor-1/-2 motifs as well as the substrate-binding pore motifs are present in the sequence, the N-terminal leader sequences that specify their cellular localization, and the endoplasmic reticulum-targeting signal sequence with the predicted signal peptide cleavage between Ser23 and Lys24 in PfClpB1. PfClpB1 also contains a 120-residue long predominantly basic, K- and N-rich segment, which is a predictor of an apicoplast-targeting sequence | Plasmodium falciparum |
| physiological function | ClpB is a molecular chaperone, which reactivates aggregated proteins in cooperation with the DnaK chaperone system. ClpB is essential for infectivity and in-host survival. The chaperone activity of PfClpB1 may support survival of Plasmodium falciparum by maintaining the folding status and activity of apicoplast proteins. The ATP hydrolysis-driven reactivation of aggregates mediated by ClpB is linked to substrate translocation through the narrow central pore in the hexameric assembly | Plasmodium falciparum |
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