| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EEX37589.1 | dnaJ | VIB_001714 | VIB_001794 | 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 [...] | 0.744 |
| EEX37589.1 | groL | VIB_001714 | VIB_000481 | 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. | 0.917 |
| EEX37589.1 | groS | VIB_001714 | VIB_000480 | Thioredoxin domain-containing protein. | Heat shock protein 60 family co-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.643 |
| EEX37589.1 | grpE | VIB_001714 | VIB_001796 | 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- [...] | 0.916 |
| EEX37589.1 | hslO | VIB_001714 | VIB_000404 | Thioredoxin domain-containing protein. | Heat-shock chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.486 |
| EEX37589.1 | hslU | VIB_001714 | VIB_000472 | Thioredoxin domain-containing protein. | ATP-dependent hsl 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. | 0.928 |
| EEX37589.1 | hslV | VIB_001714 | VIB_000471 | Thioredoxin domain-containing protein. | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.922 |
| EEX37589.1 | htpG | VIB_001714 | VIB_001710 | Thioredoxin domain-containing protein. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.834 |
| EEX37589.1 | lon | VIB_001714 | VIB_001659 | Thioredoxin domain-containing protein. | ATP-dependent protease La Type 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. | 0.644 |
| EEX38036.1 | dnaJ | VIB_000405 | VIB_001794 | Ribosome-associated heat shock protein; Implicated in the recycling of the LSU (S4 paralog). | 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 [...] | 0.684 |
| EEX38036.1 | groL | VIB_000405 | VIB_000481 | Ribosome-associated heat shock protein; Implicated in the recycling of the LSU (S4 paralog). | Heat shock protein 60 family chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.461 |
| EEX38036.1 | grpE | VIB_000405 | VIB_001796 | Ribosome-associated heat shock protein; Implicated in the recycling of the LSU (S4 paralog). | 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- [...] | 0.684 |
| EEX38036.1 | hslO | VIB_000405 | VIB_000404 | Ribosome-associated heat shock protein; Implicated in the recycling of the LSU (S4 paralog). | Heat-shock chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.977 |
| EEX38036.1 | hslU | VIB_000405 | VIB_000472 | Ribosome-associated heat shock protein; Implicated in the recycling of the LSU (S4 paralog). | ATP-dependent hsl 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. | 0.730 |
| EEX38036.1 | hslV | VIB_000405 | VIB_000471 | Ribosome-associated heat shock protein; Implicated in the recycling of the LSU (S4 paralog). | ATP-dependent protease HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.789 |
| EEX38036.1 | htpG | VIB_000405 | VIB_001710 | Ribosome-associated heat shock protein; Implicated in the recycling of the LSU (S4 paralog). | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.545 |
| EEX38036.1 | lon | VIB_000405 | VIB_001659 | Ribosome-associated heat shock protein; Implicated in the recycling of the LSU (S4 paralog). | ATP-dependent protease La Type 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. | 0.444 |
| dnaJ | EEX37589.1 | VIB_001794 | VIB_001714 | 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 [...] | Thioredoxin domain-containing protein. | 0.744 |
| dnaJ | EEX38036.1 | VIB_001794 | VIB_000405 | 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 [...] | Ribosome-associated heat shock protein; Implicated in the recycling of the LSU (S4 paralog). | 0.684 |
| dnaJ | groL | VIB_001794 | VIB_000481 | 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 [...] | Heat shock protein 60 family chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.985 |
