node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
BG454_03495 | dnaK | GCA_001870665_00524 | GCA_001870665_03043 | Unannotated protein. | Unannotated protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.989 |
BG454_03495 | groL | GCA_001870665_00524 | GCA_001870665_02939 | Unannotated protein. | Unannotated protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.910 |
BG454_03495 | groS | GCA_001870665_00524 | GCA_001870665_02940 | Unannotated protein. | Unannotated protein; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.668 |
BG454_03495 | grpE | GCA_001870665_00524 | GCA_001870665_00888 | Unannotated protein. | Unannotated 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-depe [...] | 0.904 |
BG454_03495 | hrcA | GCA_001870665_00524 | GCA_001870665_00889 | Unannotated protein. | Unannotated protein; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.863 |
BG454_03495 | hslU | GCA_001870665_00524 | GCA_001870665_02922 | Unannotated protein. | Unannotated protein; 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. | 0.793 |
BG454_03495 | hslV | GCA_001870665_00524 | GCA_001870665_02923 | Unannotated protein. | Unannotated protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.574 |
BG454_03495 | lon | GCA_001870665_00524 | GCA_001870665_03581 | Unannotated protein. | Unannotated protein; 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. | 0.673 |
dnaJ | dnaK | GCA_001870665_03042 | GCA_001870665_03043 | Unannotated protein; 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, DnaK [...] | Unannotated protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
dnaJ | groL | GCA_001870665_03042 | GCA_001870665_02939 | Unannotated protein; 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, DnaK [...] | Unannotated protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.942 |
dnaJ | groS | GCA_001870665_03042 | GCA_001870665_02940 | Unannotated protein; 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, DnaK [...] | Unannotated protein; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.896 |
dnaJ | grpE | GCA_001870665_03042 | GCA_001870665_00888 | Unannotated protein; 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, DnaK [...] | Unannotated 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-depe [...] | 0.985 |
dnaJ | hrcA | GCA_001870665_03042 | GCA_001870665_00889 | Unannotated protein; 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, DnaK [...] | Unannotated protein; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.858 |
dnaJ | hslU | GCA_001870665_03042 | GCA_001870665_02922 | Unannotated protein; 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, DnaK [...] | Unannotated protein; 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. | 0.870 |
dnaJ | hslV | GCA_001870665_03042 | GCA_001870665_02923 | Unannotated protein; 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, DnaK [...] | Unannotated protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.852 |
dnaJ | lon | GCA_001870665_03042 | GCA_001870665_03581 | Unannotated protein; 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, DnaK [...] | Unannotated protein; 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. | 0.852 |
dnaK | BG454_03495 | GCA_001870665_03043 | GCA_001870665_00524 | Unannotated protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Unannotated protein. | 0.989 |
dnaK | dnaJ | GCA_001870665_03043 | GCA_001870665_03042 | Unannotated protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Unannotated protein; 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, DnaK [...] | 0.999 |
dnaK | groL | GCA_001870665_03043 | GCA_001870665_02939 | Unannotated protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Unannotated protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.992 |
dnaK | groS | GCA_001870665_03043 | GCA_001870665_02940 | Unannotated protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Unannotated protein; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.941 |