| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BV96_00789 | BV96_01735 | BV96_00789 | BV96_01735 | Thioredoxin. | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.868 |
| BV96_00789 | BV96_01826 | BV96_00789 | BV96_01826 | Thioredoxin. | ATP-dependent proteinase. | 0.621 |
| BV96_00789 | dnaJ_1 | BV96_00789 | BV96_00842 | Thioredoxin. | 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 [...] | 0.761 |
| BV96_00789 | dnaK | BV96_00789 | BV96_00843 | Thioredoxin. | Heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.657 |
| BV96_00789 | groS | BV96_00789 | BV96_01608 | Thioredoxin. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.465 |
| BV96_00789 | groS-2 | BV96_00789 | BV96_03504 | Thioredoxin. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.530 |
| BV96_00789 | grpE_1 | BV96_00789 | BV96_02489 | Thioredoxin. | HSP-70 cofactor; 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-dependen [...] | 0.826 |
| BV96_00789 | grpE_2 | BV96_00789 | BV96_03900 | Thioredoxin. | HSP-70 cofactor; 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-dependen [...] | 0.803 |
| BV96_00789 | hslV | BV96_00789 | BV96_01736 | Thioredoxin. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.882 |
| BV96_00789 | lon | BV96_00789 | BV96_01882 | Thioredoxin. | 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. | 0.621 |
| BV96_01735 | BV96_00789 | BV96_01735 | BV96_00789 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Thioredoxin. | 0.868 |
| BV96_01735 | BV96_01826 | BV96_01735 | BV96_01826 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | ATP-dependent proteinase. | 0.835 |
| BV96_01735 | dnaJ_1 | BV96_01735 | BV96_00842 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 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 [...] | 0.934 |
| BV96_01735 | dnaK | BV96_01735 | BV96_00843 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.862 |
| BV96_01735 | groS | BV96_01735 | BV96_01608 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.825 |
| BV96_01735 | groS-2 | BV96_01735 | BV96_03504 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.825 |
| BV96_01735 | grpE_1 | BV96_01735 | BV96_02489 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | HSP-70 cofactor; 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-dependen [...] | 0.854 |
| BV96_01735 | grpE_2 | BV96_01735 | BV96_03900 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | HSP-70 cofactor; 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-dependen [...] | 0.854 |
| BV96_01735 | hslV | BV96_01735 | BV96_01736 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.999 |
| BV96_01735 | lon | BV96_01735 | BV96_01882 | ATP-dependent protease; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 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. | 0.835 |
