| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| SO_1850 | SO_2017 | SO_1850 | SO_2017 | DnaJ domain protein. | Heat shock response protein. | 0.636 |
| SO_1850 | dnaK | SO_1850 | SO_1126 | DnaJ domain protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.958 |
| SO_1850 | groEL | SO_1850 | SO_0704 | DnaJ domain protein. | 60 kDa chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.775 |
| SO_1850 | groES | SO_1850 | SO_0703 | DnaJ domain protein. | 10 kDa chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.693 |
| SO_1850 | grpE | SO_1850 | SO_1524 | DnaJ domain protein. | Heat shock nucleotide exchange factor 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. Sev [...] | 0.902 |
| SO_1850 | hslU | SO_1850 | SO_4163 | DnaJ domain protein. | HlsVU protease ATPase component 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. | 0.819 |
| SO_1850 | hslV | SO_1850 | SO_4162 | DnaJ domain protein. | HlsVU protease peptidase component HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.728 |
| SO_1850 | htpG | SO_1850 | SO_2016 | DnaJ domain protein. | Heat shock chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.931 |
| SO_1850 | lon | SO_1850 | SO_1796 | DnaJ domain protein. | ATP-dependent protease La 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. | 0.730 |
| SO_2017 | SO_1850 | SO_2017 | SO_1850 | Heat shock response protein. | DnaJ domain protein. | 0.636 |
| SO_2017 | dnaJ | SO_2017 | SO_1127 | Heat shock response protein. | 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 [...] | 0.767 |
| SO_2017 | dnaK | SO_2017 | SO_1126 | Heat shock response protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.748 |
| SO_2017 | groEL | SO_2017 | SO_0704 | Heat shock response protein. | 60 kDa chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.817 |
| SO_2017 | groES | SO_2017 | SO_0703 | Heat shock response protein. | 10 kDa chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.802 |
| SO_2017 | grpE | SO_2017 | SO_1524 | Heat shock response protein. | Heat shock nucleotide exchange factor 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. Sev [...] | 0.907 |
| SO_2017 | hslU | SO_2017 | SO_4163 | Heat shock response protein. | HlsVU protease ATPase component 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. | 0.906 |
| SO_2017 | hslV | SO_2017 | SO_4162 | Heat shock response protein. | HlsVU protease peptidase component HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.953 |
| SO_2017 | htpG | SO_2017 | SO_2016 | Heat shock response protein. | Heat shock chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.949 |
| SO_2017 | lon | SO_2017 | SO_1796 | Heat shock response protein. | ATP-dependent protease La 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. | 0.613 |
| dnaJ | SO_2017 | SO_1127 | SO_2017 | 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 response protein. | 0.767 |