| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| amb0494 | amb1123 | amb0494 | amb1123 | Hypothetical protein. | ATPase with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | 0.701 |
| amb0494 | amb1560 | amb0494 | amb1560 | Hypothetical protein. | ATPase with chaperone activity; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK. | 0.701 |
| amb0494 | amb4304 | amb0494 | amb4304 | Hypothetical protein. | Molecular chaperone. | 0.810 |
| amb0494 | groL | amb0494 | amb0203 | Hypothetical protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.771 |
| amb0494 | grpE | amb0494 | 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 [...] | 0.837 |
| amb0494 | hrcA | amb0494 | amb4497 | Hypothetical protein. | Transcriptional regulator of heat shock gene; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.684 |
| amb0494 | htpG | amb0494 | amb4343 | Hypothetical protein. | Molecular chaperone, HSP90 family; Molecular chaperone. Has ATPase activity. | 0.929 |
| amb0888 | amb1123 | amb0888 | amb1123 | DnaJ-class molecular chaperone. | ATPase with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | 0.760 |
| amb0888 | amb1560 | amb0888 | amb1560 | DnaJ-class molecular chaperone. | ATPase with chaperone activity; 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. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK. | 0.760 |
| amb0888 | amb4304 | amb0888 | amb4304 | DnaJ-class molecular chaperone. | Molecular chaperone. | 0.968 |
| 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. | 0.846 |
| 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 [...] | 0.899 |
| amb0888 | hrcA | amb0888 | amb4497 | DnaJ-class molecular chaperone. | Transcriptional regulator of heat shock gene; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.733 |
| amb0888 | htpG | amb0888 | amb4343 | DnaJ-class molecular chaperone. | Molecular chaperone, HSP90 family; Molecular chaperone. Has ATPase activity. | 0.934 |
| amb1123 | amb0494 | amb1123 | amb0494 | ATPase with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | Hypothetical protein. | 0.701 |
| amb1123 | amb0888 | amb1123 | amb0888 | ATPase with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | DnaJ-class molecular chaperone. | 0.760 |
| amb1123 | amb3914 | amb1123 | amb3914 | ATPase with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | DnaJ-class molecular chaperone. | 0.700 |
| amb1123 | amb4304 | amb1123 | amb4304 | ATPase with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | Molecular chaperone. | 0.873 |
| amb1123 | dnaJ | amb1123 | amb4441 | ATPase with chaperone activity, ATP-binding subunit; 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 [...] | 0.703 |
| amb1123 | groL | amb1123 | amb0203 | ATPase with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.688 |