node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
SCB20061.1 | SCB21299.1 | GA0061103_2795 | GA0061103_3019 | DnaJ C terminal domain-containing protein. | Hypothetical chaperone protein. | 0.974 |
SCB20061.1 | SCB31903.1 | GA0061103_2795 | GA0061103_4370 | DnaJ C terminal domain-containing protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.752 |
SCB20061.1 | dnaK | GA0061103_2795 | GA0061103_0864 | DnaJ C terminal domain-containing protein. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.991 |
SCB20061.1 | dnaK-2 | GA0061103_2795 | GA0061103_4598 | DnaJ C terminal domain-containing protein. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.991 |
SCB20061.1 | groL | GA0061103_2795 | GA0061103_2683 | DnaJ C terminal domain-containing protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.782 |
SCB20061.1 | groS | GA0061103_2795 | GA0061103_2684 | DnaJ C terminal domain-containing protein. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.709 |
SCB20061.1 | grpE-2 | GA0061103_2795 | GA0061103_5477 | DnaJ C terminal domain-containing protein. | Molecular chaperone 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 ATP [...] | 0.887 |
SCB20061.1 | hrcA | GA0061103_2795 | GA0061103_5475 | DnaJ C terminal domain-containing protein. | 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. | 0.795 |
SCB20061.1 | hslU | GA0061103_2795 | GA0061103_0333 | DnaJ C terminal domain-containing protein. | ATP-dependent HslUV protease ATP-binding subunit 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. | 0.664 |
SCB21299.1 | SCB20061.1 | GA0061103_3019 | GA0061103_2795 | Hypothetical chaperone protein. | DnaJ C terminal domain-containing protein. | 0.974 |
SCB21299.1 | SCB31903.1 | GA0061103_3019 | GA0061103_4370 | Hypothetical chaperone protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | 0.901 |
SCB21299.1 | dnaJ | GA0061103_3019 | GA0061103_0865 | Hypothetical chaperone protein. | Molecular chaperone 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, [...] | 0.965 |
SCB21299.1 | groL | GA0061103_3019 | GA0061103_2683 | Hypothetical chaperone protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.901 |
SCB21299.1 | groS | GA0061103_3019 | GA0061103_2684 | Hypothetical chaperone protein. | Chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.902 |
SCB21299.1 | grpE-2 | GA0061103_3019 | GA0061103_5477 | Hypothetical chaperone protein. | Molecular chaperone 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 ATP [...] | 0.981 |
SCB21299.1 | hrcA | GA0061103_3019 | GA0061103_5475 | Hypothetical chaperone protein. | 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. | 0.858 |
SCB21299.1 | hslU | GA0061103_3019 | GA0061103_0333 | Hypothetical chaperone protein. | ATP-dependent HslUV protease ATP-binding subunit 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. | 0.597 |
SCB31903.1 | SCB20061.1 | GA0061103_4370 | GA0061103_2795 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | DnaJ C terminal domain-containing protein. | 0.752 |
SCB31903.1 | SCB21299.1 | GA0061103_4370 | GA0061103_3019 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | Hypothetical chaperone protein. | 0.901 |
SCB31903.1 | dnaJ | GA0061103_4370 | GA0061103_0865 | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family. | Molecular chaperone 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, [...] | 0.762 |