node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ACH50_21815 | ACH50_21820 | GCA_000621185_03308 | GCA_000621185_03307 | Unannotated protein; Belongs to the HSP15 family. | Unannotated protein. | 0.913 |
ACH50_21815 | ACH50_21825 | GCA_000621185_03308 | GCA_000621185_03306 | Unannotated protein; Belongs to the HSP15 family. | Unannotated protein. | 0.605 |
ACH50_21815 | dnaJ | GCA_000621185_03308 | GCA_000621185_01872 | Unannotated protein; Belongs to the HSP15 family. | Unannotated protein; 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, DnaK [...] | 0.625 |
ACH50_21815 | grpE | GCA_000621185_03308 | GCA_000621185_04048 | Unannotated protein; Belongs to the HSP15 family. | Unannotated protein; 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-depe [...] | 0.585 |
ACH50_21815 | hslO | GCA_000621185_03308 | GCA_000621185_03309 | Unannotated protein; Belongs to the HSP15 family. | Unannotated protein; 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. | 0.946 |
ACH50_21815 | hslU | GCA_000621185_03308 | GCA_000621185_03456 | Unannotated protein; Belongs to the HSP15 family. | Unannotated protein; 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. | 0.649 |
ACH50_21815 | hslV | GCA_000621185_03308 | GCA_000621185_03455 | Unannotated protein; Belongs to the HSP15 family. | Unannotated protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.693 |
ACH50_21815 | htpG | GCA_000621185_03308 | GCA_000621185_00554 | Unannotated protein; Belongs to the HSP15 family. | Unannotated protein; Molecular chaperone. Has ATPase activity. | 0.460 |
ACH50_21820 | ACH50_21815 | GCA_000621185_03307 | GCA_000621185_03308 | Unannotated protein. | Unannotated protein; Belongs to the HSP15 family. | 0.913 |
ACH50_21820 | ACH50_21825 | GCA_000621185_03307 | GCA_000621185_03306 | Unannotated protein. | Unannotated protein. | 0.622 |
ACH50_21820 | hslO | GCA_000621185_03307 | GCA_000621185_03309 | Unannotated protein. | Unannotated protein; 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. | 0.754 |
ACH50_21825 | ACH50_21815 | GCA_000621185_03306 | GCA_000621185_03308 | Unannotated protein. | Unannotated protein; Belongs to the HSP15 family. | 0.605 |
ACH50_21825 | ACH50_21820 | GCA_000621185_03306 | GCA_000621185_03307 | Unannotated protein. | Unannotated protein. | 0.622 |
ACH50_21825 | hslO | GCA_000621185_03306 | GCA_000621185_03309 | Unannotated protein. | Unannotated protein; 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. | 0.607 |
dnaJ | ACH50_21815 | GCA_000621185_01872 | GCA_000621185_03308 | Unannotated protein; 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, DnaK [...] | Unannotated protein; Belongs to the HSP15 family. | 0.625 |
dnaJ | groEL | GCA_000621185_01872 | GCA_000621185_01625 | Unannotated protein; 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, DnaK [...] | Unannotated protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.915 |
dnaJ | grpE | GCA_000621185_01872 | GCA_000621185_04048 | Unannotated protein; 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, DnaK [...] | Unannotated protein; 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-depe [...] | 0.978 |
dnaJ | hslO | GCA_000621185_01872 | GCA_000621185_03309 | Unannotated protein; 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, DnaK [...] | Unannotated protein; 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. | 0.582 |
dnaJ | hslU | GCA_000621185_01872 | GCA_000621185_03456 | Unannotated protein; 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, DnaK [...] | Unannotated protein; 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. | 0.912 |
dnaJ | hslV | GCA_000621185_01872 | GCA_000621185_03455 | Unannotated protein; 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, DnaK [...] | Unannotated protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.855 |