| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| RPA0268 | trx | RPA0268 | RPA0267 | Putative Lon family ATP-dependent protease; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Possible thioredoxin; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.835 |
| RPA3954 | gor | RPA3954 | RPA1983 | Thioredoxin reductase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Putative glutathione reductase; Maintains high levels of reduced glutathione. | 0.448 |
| RPA3954 | trx | RPA3954 | RPA0267 | Thioredoxin reductase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | Possible thioredoxin; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.712 |
| dnaJ | groEL1 | RPA0334 | RPA1140 | Heat shock protein DnaJ (40); 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 D [...] | Chaperonin GroEL1, cpn60; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.970 |
| dnaJ | groEL2 | RPA0334 | RPA2164 | Heat shock protein DnaJ (40); 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 D [...] | Chaperonin GroEL2, cpn60; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.972 |
| dnaJ | grpE | RPA0334 | RPA0331 | Heat shock protein DnaJ (40); 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 D [...] | Possible heat shock protein (HSP-70 COFACTOR), 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 c [...] | 0.975 |
| dnaJ | hslU | RPA0334 | RPA0306 | Heat shock protein DnaJ (40); 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 D [...] | Heat shock protein HslU, proteasome-related ATPase subunit; 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. | 0.970 |
| dnaJ | hslV | RPA0334 | RPA0308 | Heat shock protein DnaJ (40); 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 D [...] | Heat shock protein HslV, proteasome-related peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.964 |
| dnaJ | trx | RPA0334 | RPA0267 | Heat shock protein DnaJ (40); 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 D [...] | Possible thioredoxin; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.780 |
| gor | RPA3954 | RPA1983 | RPA3954 | Putative glutathione reductase; Maintains high levels of reduced glutathione. | Thioredoxin reductase; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.448 |
| gor | groEL1 | RPA1983 | RPA1140 | Putative glutathione reductase; Maintains high levels of reduced glutathione. | Chaperonin GroEL1, cpn60; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.525 |
| gor | groEL2 | RPA1983 | RPA2164 | Putative glutathione reductase; Maintains high levels of reduced glutathione. | Chaperonin GroEL2, cpn60; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.525 |
| gor | hslU | RPA1983 | RPA0306 | Putative glutathione reductase; Maintains high levels of reduced glutathione. | Heat shock protein HslU, proteasome-related ATPase subunit; 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. | 0.411 |
| gor | trx | RPA1983 | RPA0267 | Putative glutathione reductase; Maintains high levels of reduced glutathione. | Possible thioredoxin; Observed by proteomics; Citation: Proteomics from VerBerkmoes et al. (2003) unpublished. | 0.946 |
| groEL1 | dnaJ | RPA1140 | RPA0334 | Chaperonin GroEL1, cpn60; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Heat shock protein DnaJ (40); 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 D [...] | 0.970 |
| groEL1 | gor | RPA1140 | RPA1983 | Chaperonin GroEL1, cpn60; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Putative glutathione reductase; Maintains high levels of reduced glutathione. | 0.525 |
| groEL1 | groEL2 | RPA1140 | RPA2164 | Chaperonin GroEL1, cpn60; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Chaperonin GroEL2, cpn60; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.903 |
| groEL1 | grpE | RPA1140 | RPA0331 | Chaperonin GroEL1, cpn60; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Possible heat shock protein (HSP-70 COFACTOR), 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 c [...] | 0.975 |
| groEL1 | hslU | RPA1140 | RPA0306 | Chaperonin GroEL1, cpn60; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Heat shock protein HslU, proteasome-related ATPase subunit; 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. | 0.924 |
| groEL1 | hslV | RPA1140 | RPA0308 | Chaperonin GroEL1, cpn60; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | Heat shock protein HslV, proteasome-related peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.892 |
