| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CTC_00171 | CTC_02469 | CTC_00171 | CTC_02469 | Glutamine synthetase. | Heat shock protein, molecular chaperone; Belongs to the small heat shock protein (HSP20) family. | 0.755 |
| CTC_02469 | CTC_00171 | CTC_02469 | CTC_00171 | Heat shock protein, molecular chaperone; Belongs to the small heat shock protein (HSP20) family. | Glutamine synthetase. | 0.755 |
| CTC_02469 | clpB | CTC_02469 | CTC_00536 | Heat shock protein, molecular chaperone; Belongs to the small heat shock protein (HSP20) family. | clpB protein; 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 ClpA/ClpB family. | 0.878 |
| CTC_02469 | dnaJ | CTC_02469 | CTC_02030 | Heat shock protein, molecular chaperone; Belongs to the small heat shock protein (HSP20) family. | Chaperone protein dnaJ; 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 of ATP-dependent interactions between DnaJ, D [...] | 0.724 |
| CTC_02469 | dnaK-2 | CTC_02469 | CTC_02031 | Heat shock protein, molecular chaperone; Belongs to the small heat shock protein (HSP20) family. | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.797 |
| CTC_02469 | grpE | CTC_02469 | CTC_02032 | Heat shock protein, molecular chaperone; Belongs to the small heat shock protein (HSP20) family. | Putative grpE protein; 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 the reaction cycle. Several rounds of ATP-de [...] | 0.716 |
| CTC_02469 | htpG | CTC_02469 | CTC_01489 | Heat shock protein, molecular chaperone; Belongs to the small heat shock protein (HSP20) family. | Heat shock protein htpG; Molecular chaperone. Has ATPase activity. | 0.778 |
| CTC_02469 | lon | CTC_02469 | CTC_02372 | Heat shock protein, molecular chaperone; Belongs to the small heat shock protein (HSP20) family. | ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.575 |
| CTC_02469 | mecB | CTC_02469 | CTC_00060 | Heat shock protein, molecular chaperone; Belongs to the small heat shock protein (HSP20) family. | Negative regulator of genetic competence mecB; Belongs to the ClpA/ClpB family. | 0.878 |
| CTC_02469 | mecB-2 | CTC_02469 | CTC_02633 | Heat shock protein, molecular chaperone; Belongs to the small heat shock protein (HSP20) family. | Negative regulator of genetic competence mecB/clpC; Belongs to the ClpA/ClpB family. | 0.867 |
| CTC_02469 | rplP | CTC_02469 | CTC_02595 | Heat shock protein, molecular chaperone; Belongs to the small heat shock protein (HSP20) family. | LSU ribosomal protein L16P; Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs; Belongs to the universal ribosomal protein uL16 family. | 0.529 |
| clpB | CTC_02469 | CTC_00536 | CTC_02469 | clpB protein; 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 ClpA/ClpB family. | Heat shock protein, molecular chaperone; Belongs to the small heat shock protein (HSP20) family. | 0.878 |
| clpB | dnaJ | CTC_00536 | CTC_02030 | clpB protein; 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 ClpA/ClpB family. | Chaperone protein dnaJ; 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 of ATP-dependent interactions between DnaJ, D [...] | 0.806 |
| clpB | dnaK-2 | CTC_00536 | CTC_02031 | clpB protein; 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 ClpA/ClpB family. | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.964 |
| clpB | grpE | CTC_00536 | CTC_02032 | clpB protein; 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 ClpA/ClpB family. | Putative grpE protein; 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 the reaction cycle. Several rounds of ATP-de [...] | 0.869 |
| clpB | htpG | CTC_00536 | CTC_01489 | clpB protein; 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 ClpA/ClpB family. | Heat shock protein htpG; Molecular chaperone. Has ATPase activity. | 0.871 |
| clpB | lon | CTC_00536 | CTC_02372 | clpB protein; 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 ClpA/ClpB family. | ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.742 |
| dnaJ | CTC_02469 | CTC_02030 | CTC_02469 | Chaperone protein dnaJ; 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 of ATP-dependent interactions between DnaJ, D [...] | Heat shock protein, molecular chaperone; Belongs to the small heat shock protein (HSP20) family. | 0.724 |
| dnaJ | clpB | CTC_02030 | CTC_00536 | Chaperone protein dnaJ; 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 of ATP-dependent interactions between DnaJ, D [...] | clpB protein; 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 ClpA/ClpB family. | 0.806 |
| dnaJ | dnaK-2 | CTC_02030 | CTC_02031 | Chaperone protein dnaJ; 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 of ATP-dependent interactions between DnaJ, D [...] | Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |