| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| clpB | dnaJ1 | PFREUD_17920 | PFREUD_17820 | Chaperone clpB 2 (ATP-dependent Clp protease B2) (Clp chaperone); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Chaperone protein dnaJ 1 (DnaJ1 protein) (Heat shock protein 40 1); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds o [...] | 0.800 |
| clpB | dnaJ2 | PFREUD_17920 | PFREUD_04650 | Chaperone clpB 2 (ATP-dependent Clp protease B2) (Clp chaperone); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Chaperone protein dnaJ 2 (DnaJ2 protein) (Heat shock protein 40 2); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds o [...] | 0.750 |
| clpB | dnaJ3 | PFREUD_17920 | PFREUD_08760 | Chaperone clpB 2 (ATP-dependent Clp protease B2) (Clp chaperone); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Chaperone protein dnaJ 3 (DnaJ3 protein) (Heat shock protein 40 3); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds o [...] | 0.732 |
| clpB | dnaK1 | PFREUD_17920 | PFREUD_17840 | Chaperone clpB 2 (ATP-dependent Clp protease B2) (Clp chaperone); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Chaperone protein dnaK 1 (Heat shock protein 70 1) (Heat shock 70 kDa protein 1) (HSP70 1); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.959 |
| clpB | dnaK2 | PFREUD_17920 | PFREUD_04630 | Chaperone clpB 2 (ATP-dependent Clp protease B2) (Clp chaperone); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Chaperone protein dnaK 2 (Heat shock protein 70 2) (Heat shock 70 kDa protein 2) (HSP70 2); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.960 |
| clpB | groS1(groES1) | PFREUD_17920 | PFREUD_06460 | Chaperone clpB 2 (ATP-dependent Clp protease B2) (Clp chaperone); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | 10 kDa chaperonin 1 (Protein Cpn10 1) (groES protein 1) (Heat shock 10 1); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.733 |
| clpB | grpE1 | PFREUD_17920 | PFREUD_17830 | Chaperone clpB 2 (ATP-dependent Clp protease B2) (Clp chaperone); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Protein GrpE 1 (HSP-70 cofactor 1) (Co-chaperone protein GrpE1); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing th [...] | 0.907 |
| clpB | hsp20 | PFREUD_17920 | PFREUD_09500 | Chaperone clpB 2 (ATP-dependent Clp protease B2) (Clp chaperone); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family. | Belongs to the small heat shock protein (HSP20) family.These seem to act as chaperones that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Structurally, this family is characterized by the presence of a conserved C-terminal domain of about 100 residues. | 0.850 |
| clpB-2 | dnaJ1 | PFREUD_19250 | PFREUD_17820 | Chaperone clpB 1 (ATP-dependent Clp protease B1) (Clp chaperone); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). | Chaperone protein dnaJ 1 (DnaJ1 protein) (Heat shock protein 40 1); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds o [...] | 0.751 |
| clpB-2 | dnaJ2 | PFREUD_19250 | PFREUD_04650 | Chaperone clpB 1 (ATP-dependent Clp protease B1) (Clp chaperone); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). | Chaperone protein dnaJ 2 (DnaJ2 protein) (Heat shock protein 40 2); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds o [...] | 0.750 |
| clpB-2 | dnaJ3 | PFREUD_19250 | PFREUD_08760 | Chaperone clpB 1 (ATP-dependent Clp protease B1) (Clp chaperone); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). | Chaperone protein dnaJ 3 (DnaJ3 protein) (Heat shock protein 40 3); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds o [...] | 0.698 |
| clpB-2 | dnaK1 | PFREUD_19250 | PFREUD_17840 | Chaperone clpB 1 (ATP-dependent Clp protease B1) (Clp chaperone); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). | Chaperone protein dnaK 1 (Heat shock protein 70 1) (Heat shock 70 kDa protein 1) (HSP70 1); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.959 |
| clpB-2 | dnaK2 | PFREUD_19250 | PFREUD_04630 | Chaperone clpB 1 (ATP-dependent Clp protease B1) (Clp chaperone); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). | Chaperone protein dnaK 2 (Heat shock protein 70 2) (Heat shock 70 kDa protein 2) (HSP70 2); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.959 |
| clpB-2 | groS1(groES1) | PFREUD_19250 | PFREUD_06460 | Chaperone clpB 1 (ATP-dependent Clp protease B1) (Clp chaperone); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). | 10 kDa chaperonin 1 (Protein Cpn10 1) (groES protein 1) (Heat shock 10 1); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.733 |
| clpB-2 | grpE1 | PFREUD_19250 | PFREUD_17830 | Chaperone clpB 1 (ATP-dependent Clp protease B1) (Clp chaperone); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). | Protein GrpE 1 (HSP-70 cofactor 1) (Co-chaperone protein GrpE1); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing th [...] | 0.906 |
| clpB-2 | hsp20 | PFREUD_19250 | PFREUD_09500 | Chaperone clpB 1 (ATP-dependent Clp protease B1) (Clp chaperone); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). | Belongs to the small heat shock protein (HSP20) family.These seem to act as chaperones that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Structurally, this family is characterized by the presence of a conserved C-terminal domain of about 100 residues. | 0.852 |
| clpC | dnaJ1 | PFREUD_20250 | PFREUD_17820 | Chaperone clpC (Clp-family ATP-binding protease) (ATP-dependent Clp protease ATP-binding subunit); Belongs to the clpA/clpB family. ClpC subfamily. The protein has been identified by proteomics as a 99 kDa protein induced by heat.Several 90 to 100 kda clp chaperones are expressed as disctinct heat shock proteins. | Chaperone protein dnaJ 1 (DnaJ1 protein) (Heat shock protein 40 1); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds o [...] | 0.809 |
| clpC | dnaJ2 | PFREUD_20250 | PFREUD_04650 | Chaperone clpC (Clp-family ATP-binding protease) (ATP-dependent Clp protease ATP-binding subunit); Belongs to the clpA/clpB family. ClpC subfamily. The protein has been identified by proteomics as a 99 kDa protein induced by heat.Several 90 to 100 kda clp chaperones are expressed as disctinct heat shock proteins. | Chaperone protein dnaJ 2 (DnaJ2 protein) (Heat shock protein 40 2); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds o [...] | 0.750 |
| clpC | dnaJ3 | PFREUD_20250 | PFREUD_08760 | Chaperone clpC (Clp-family ATP-binding protease) (ATP-dependent Clp protease ATP-binding subunit); Belongs to the clpA/clpB family. ClpC subfamily. The protein has been identified by proteomics as a 99 kDa protein induced by heat.Several 90 to 100 kda clp chaperones are expressed as disctinct heat shock proteins. | Chaperone protein dnaJ 3 (DnaJ3 protein) (Heat shock protein 40 3); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds o [...] | 0.750 |
| clpC | dnaK1 | PFREUD_20250 | PFREUD_17840 | Chaperone clpC (Clp-family ATP-binding protease) (ATP-dependent Clp protease ATP-binding subunit); Belongs to the clpA/clpB family. ClpC subfamily. The protein has been identified by proteomics as a 99 kDa protein induced by heat.Several 90 to 100 kda clp chaperones are expressed as disctinct heat shock proteins. | Chaperone protein dnaK 1 (Heat shock protein 70 1) (Heat shock 70 kDa protein 1) (HSP70 1); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.918 |
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