node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
HI_1159 | clpB | HI_1159 | HI_0859 | Conserved hypothetical protein; Similar to GB:U00096 SP:P77395 PID:1773174 PID:1786700 percent identity: 50.89; identified by sequence similarity; putative. | ATP-dependent Clp protease, ATPase subunit (clpB); 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 th [...] | 0.401 |
HI_1159 | dnaJ | HI_1159 | HI_1238 | Conserved hypothetical protein; Similar to GB:U00096 SP:P77395 PID:1773174 PID:1786700 percent identity: 50.89; identified by sequence similarity; putative. | Heat shock 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 [...] | 0.622 |
HI_1159 | groL | HI_1159 | HI_0543 | Conserved hypothetical protein; Similar to GB:U00096 SP:P77395 PID:1773174 PID:1786700 percent identity: 50.89; identified by sequence similarity; putative. | Heat shock protein (groEL); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.612 |
HI_1159 | groS | HI_1159 | HI_0542 | Conserved hypothetical protein; Similar to GB:U00096 SP:P77395 PID:1773174 PID:1786700 percent identity: 50.89; identified by sequence similarity; putative. | Chaperonin (groES); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.448 |
HI_1159 | grpE | HI_1159 | HI_0071 | Conserved hypothetical protein; Similar to GB:U00096 SP:P77395 PID:1773174 PID:1786700 percent identity: 50.89; identified by sequence similarity; putative. | Heat shock protein (grpE); 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 AT [...] | 0.680 |
HI_1159 | hslU | HI_1159 | HI_0497 | Conserved hypothetical protein; Similar to GB:U00096 SP:P77395 PID:1773174 PID:1786700 percent identity: 50.89; identified by sequence similarity; putative. | Heat shock protein (hslU); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.742 |
HI_1159 | hslV | HI_1159 | HI_0496 | Conserved hypothetical protein; Similar to GB:U00096 SP:P77395 PID:1773174 PID:1786700 percent identity: 50.89; identified by sequence similarity; putative. | Heat shock protein (hslV); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.700 |
HI_1159 | htpG | HI_1159 | HI_0104 | Conserved hypothetical protein; Similar to GB:U00096 SP:P77395 PID:1773174 PID:1786700 percent identity: 50.89; identified by sequence similarity; putative. | Heat shock protein (htpG); Molecular chaperone. Has ATPase activity. | 0.692 |
HI_1159 | lon | HI_1159 | HI_0462 | Conserved hypothetical protein; Similar to GB:U00096 SP:P77395 PID:1773174 PID:1786700 percent identity: 50.89; identified by sequence similarity; putative. | ATP-dependent proteinase (lon); 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. | 0.405 |
clpB | HI_1159 | HI_0859 | HI_1159 | ATP-dependent Clp protease, ATPase subunit (clpB); 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 th [...] | Conserved hypothetical protein; Similar to GB:U00096 SP:P77395 PID:1773174 PID:1786700 percent identity: 50.89; identified by sequence similarity; putative. | 0.401 |
clpB | clpX | HI_0859 | HI_0715 | ATP-dependent Clp protease, ATPase subunit (clpB); 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 th [...] | ATP-dependent Clp protease, ATP-binding subunit (clpX); ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.655 |
clpB | dnaJ | HI_0859 | HI_1238 | ATP-dependent Clp protease, ATPase subunit (clpB); 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 th [...] | Heat shock 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 [...] | 0.899 |
clpB | groL | HI_0859 | HI_0543 | ATP-dependent Clp protease, ATPase subunit (clpB); 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 th [...] | Heat shock protein (groEL); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.780 |
clpB | groS | HI_0859 | HI_0542 | ATP-dependent Clp protease, ATPase subunit (clpB); 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 th [...] | Chaperonin (groES); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.821 |
clpB | grpE | HI_0859 | HI_0071 | ATP-dependent Clp protease, ATPase subunit (clpB); 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 th [...] | Heat shock protein (grpE); 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 AT [...] | 0.834 |
clpB | hslU | HI_0859 | HI_0497 | ATP-dependent Clp protease, ATPase subunit (clpB); 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 th [...] | Heat shock protein (hslU); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.804 |
clpB | hslV | HI_0859 | HI_0496 | ATP-dependent Clp protease, ATPase subunit (clpB); 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 th [...] | Heat shock protein (hslV); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.591 |
clpB | htpG | HI_0859 | HI_0104 | ATP-dependent Clp protease, ATPase subunit (clpB); 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 th [...] | Heat shock protein (htpG); Molecular chaperone. Has ATPase activity. | 0.867 |
clpB | lon | HI_0859 | HI_0462 | ATP-dependent Clp protease, ATPase subunit (clpB); 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 th [...] | ATP-dependent proteinase (lon); 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. | 0.731 |
clpX | clpB | HI_0715 | HI_0859 | ATP-dependent Clp protease, ATP-binding subunit (clpX); ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | ATP-dependent Clp protease, ATPase subunit (clpB); 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 th [...] | 0.655 |