| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CSIRO_0930 | hslU | CSIRO_0930 | CSIRO_0931 | Hypothetical protein. | ATP-dependent 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. | 0.642 |
| CSIRO_0930 | hslV | CSIRO_0930 | CSIRO_0929 | Hypothetical protein. | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.800 |
| CSIRO_0970 | CSIRO_4236 | CSIRO_0970 | CSIRO_4236 | Thioredoxin domain-containing protein. | Hypothetical protein. | 0.488 |
| CSIRO_0970 | cbpA | CSIRO_0970 | CSIRO_4192 | Thioredoxin domain-containing protein. | DnaJ-class molecular chaperone CbpA. | 0.686 |
| CSIRO_0970 | dnaJ | CSIRO_0970 | CSIRO_0889 | Thioredoxin domain-containing 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 [...] | 0.584 |
| CSIRO_0970 | dnaK | CSIRO_0970 | CSIRO_0890 | Thioredoxin domain-containing protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.622 |
| CSIRO_0970 | groL | CSIRO_0970 | CSIRO_0458 | Thioredoxin domain-containing protein. | Heat shock protein 60 family chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.542 |
| CSIRO_0970 | grpE | CSIRO_0970 | CSIRO_0892 | Thioredoxin domain-containing protein. | Heat shock protein 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- [...] | 0.895 |
| CSIRO_0970 | hslU | CSIRO_0970 | CSIRO_0931 | Thioredoxin domain-containing protein. | ATP-dependent 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. | 0.887 |
| CSIRO_0970 | hslV | CSIRO_0970 | CSIRO_0929 | Thioredoxin domain-containing protein. | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.866 |
| CSIRO_0970 | lon | CSIRO_0970 | CSIRO_2706 | Thioredoxin domain-containing protein. | ATP-dependent protease LaType I; 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. | 0.618 |
| CSIRO_4236 | CSIRO_0970 | CSIRO_4236 | CSIRO_0970 | Hypothetical protein. | Thioredoxin domain-containing protein. | 0.488 |
| CSIRO_4236 | cbpA | CSIRO_4236 | CSIRO_4192 | Hypothetical protein. | DnaJ-class molecular chaperone CbpA. | 0.959 |
| CSIRO_4236 | dnaJ | CSIRO_4236 | CSIRO_0889 | Hypothetical 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 [...] | 0.959 |
| CSIRO_4236 | dnaK | CSIRO_4236 | CSIRO_0890 | Hypothetical protein. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| CSIRO_4236 | groL | CSIRO_4236 | CSIRO_0458 | Hypothetical protein. | Heat shock protein 60 family chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.889 |
| CSIRO_4236 | grpE | CSIRO_4236 | CSIRO_0892 | Hypothetical protein. | Heat shock protein 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- [...] | 0.876 |
| CSIRO_4236 | hslU | CSIRO_4236 | CSIRO_0931 | Hypothetical protein. | ATP-dependent 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. | 0.888 |
| CSIRO_4236 | hslV | CSIRO_4236 | CSIRO_0929 | Hypothetical protein. | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.890 |
| CSIRO_4236 | lon | CSIRO_4236 | CSIRO_2706 | Hypothetical protein. | ATP-dependent protease LaType I; 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. | 0.847 |