node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
LVIS_1554 | clpP | LVIS_1554 | LVIS_0654 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.869 |
LVIS_1554 | dnaJ | LVIS_1554 | LVIS_1328 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | 0.722 |
LVIS_1554 | dnaK | LVIS_1554 | LVIS_1329 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.859 |
LVIS_1554 | groL | LVIS_1554 | LVIS_0618 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | Chaperonin GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.620 |
LVIS_1554 | groS | LVIS_1554 | LVIS_0617 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | Co-chaperonin GroES (HSP10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.636 |
LVIS_1554 | grpE | LVIS_1554 | LVIS_1330 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | Molecular chaperone GrpE (heat shock 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. [...] | 0.685 |
LVIS_1554 | hrcA | LVIS_1554 | LVIS_1331 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.609 |
LVIS_1554 | hslU | LVIS_1554 | LVIS_0801 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | ATP-dependent protease HslVU (ClpYQ), ATPase subunit; 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. | 0.544 |
clpB | clpP | LVIS_0762 | LVIS_0654 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; 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. | ATP-dependent Clp protease proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.880 |
clpB | dnaJ | LVIS_0762 | LVIS_1328 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; 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. | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | 0.738 |
clpB | dnaK | LVIS_0762 | LVIS_1329 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; 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. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.957 |
clpB | groL | LVIS_0762 | LVIS_0618 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; 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. | Chaperonin GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.703 |
clpB | groS | LVIS_0762 | LVIS_0617 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; 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. | Co-chaperonin GroES (HSP10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.739 |
clpB | grpE | LVIS_0762 | LVIS_1330 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; 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. | Molecular chaperone GrpE (heat shock 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. [...] | 0.743 |
clpB | hrcA | LVIS_0762 | LVIS_1331 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; 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. | Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.855 |
clpB | hslU | LVIS_0762 | LVIS_0801 | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; 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. | ATP-dependent protease HslVU (ClpYQ), ATPase subunit; 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. | 0.419 |
clpP | LVIS_1554 | LVIS_0654 | LVIS_1554 | ATP-dependent Clp protease proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; Belongs to the ClpA/ClpB family. | 0.869 |
clpP | clpB | LVIS_0654 | LVIS_0762 | ATP-dependent Clp protease proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | ATP-binding subunit of Clp protease and DnaK/DnaJ chaperones; 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. | 0.880 |
clpP | dnaJ | LVIS_0654 | LVIS_1328 | ATP-dependent Clp protease proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | 0.594 |
clpP | dnaK | LVIS_0654 | LVIS_1329 | ATP-dependent Clp protease proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.938 |