| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| amb0888 | amb2961 | amb0888 | amb2961 | DnaJ-class molecular chaperone. | Hypothetical protein. | 0.962 |
| amb0888 | amb4304 | amb0888 | amb4304 | DnaJ-class molecular chaperone. | Molecular chaperone. | 0.968 |
| amb0888 | dnaK | amb0888 | amb4440 | DnaJ-class molecular chaperone. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.995 |
| amb0888 | groL | amb0888 | amb0203 | DnaJ-class molecular chaperone. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.928 |
| amb0888 | grpE | amb0888 | amb4496 | DnaJ-class molecular chaperone. | 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 [...] | 0.945 |
| amb0888 | hscA | amb0888 | amb3024 | DnaJ-class molecular chaperone. | Molecular chaperone; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.991 |
| amb0888 | hslU | amb0888 | amb4537 | DnaJ-class molecular chaperone. | ATP-dependent protease HslVU; 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. | 0.817 |
| amb0888 | htpG | amb0888 | amb4343 | DnaJ-class molecular chaperone. | Molecular chaperone, HSP90 family; Molecular chaperone. Has ATPase activity. | 0.915 |
| amb0888 | lon | amb0888 | amb2790 | DnaJ-class molecular chaperone. | ATP-dependent Lon protease; 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. | 0.804 |
| amb2961 | amb0888 | amb2961 | amb0888 | Hypothetical protein. | DnaJ-class molecular chaperone. | 0.962 |
| amb2961 | dnaJ | amb2961 | amb4441 | Hypothetical protein. | 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 [...] | 0.796 |
| amb2961 | groL | amb2961 | amb0203 | Hypothetical protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.906 |
| amb2961 | grpE | amb2961 | amb4496 | Hypothetical 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 [...] | 0.940 |
| amb2961 | hslU | amb2961 | amb4537 | Hypothetical protein. | ATP-dependent protease HslVU; 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. | 0.525 |
| amb2961 | htpG | amb2961 | amb4343 | Hypothetical protein. | Molecular chaperone, HSP90 family; Molecular chaperone. Has ATPase activity. | 0.936 |
| amb2961 | lon | amb2961 | amb2790 | Hypothetical protein. | ATP-dependent Lon protease; 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. | 0.664 |
| amb4304 | amb0888 | amb4304 | amb0888 | Molecular chaperone. | DnaJ-class molecular chaperone. | 0.968 |
| amb4304 | dnaJ | amb4304 | amb4441 | Molecular chaperone. | 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 [...] | 0.812 |
| amb4304 | groL | amb4304 | amb0203 | Molecular chaperone. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.935 |
| amb4304 | grpE | amb4304 | amb4496 | Molecular chaperone. | 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 [...] | 0.958 |
