node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
GCA_002104455_00515 | dnaJ | GCA_002104455_00515 | GCA_002104455_00402 | Unannotated protein; Belongs to the small heat shock protein (HSP20) 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 [...] | 0.688 |
GCA_002104455_00515 | grpE | GCA_002104455_00515 | GCA_002104455_00400 | Unannotated protein; Belongs to the small heat shock protein (HSP20) 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 [...] | 0.718 |
GCA_002104455_00515 | hslO | GCA_002104455_00515 | GCA_002104455_01261 | Unannotated protein; Belongs to the small heat shock protein (HSP20) 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. | 0.501 |
GCA_002104455_00515 | hslU | GCA_002104455_00515 | GCA_002104455_01288 | Unannotated protein; Belongs to the small heat shock protein (HSP20) 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. | 0.581 |
GCA_002104455_00515 | hslV | GCA_002104455_00515 | GCA_002104455_01287 | Unannotated protein; Belongs to the small heat shock protein (HSP20) family. | Unannotated protein; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.650 |
GCA_002104455_00515 | htpG | GCA_002104455_00515 | GCA_002104455_02638 | Unannotated protein; Belongs to the small heat shock protein (HSP20) family. | Unannotated protein; Molecular chaperone. Has ATPase activity. | 0.753 |
GCA_002104455_01260 | dnaJ | GCA_002104455_01260 | GCA_002104455_00402 | 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 [...] | 0.635 |
GCA_002104455_01260 | grpE | GCA_002104455_01260 | GCA_002104455_00400 | 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 [...] | 0.577 |
GCA_002104455_01260 | hslO | GCA_002104455_01260 | GCA_002104455_01261 | 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. | 0.960 |
GCA_002104455_01260 | hslU | GCA_002104455_01260 | GCA_002104455_01288 | 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. | 0.626 |
GCA_002104455_01260 | hslV | GCA_002104455_01260 | GCA_002104455_01287 | 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. | 0.716 |
GCA_002104455_01260 | htpG | GCA_002104455_01260 | GCA_002104455_02638 | Unannotated protein; Belongs to the HSP15 family. | Unannotated protein; Molecular chaperone. Has ATPase activity. | 0.427 |
coaX | hslO | GCA_002104455_02406 | GCA_002104455_01261 | Unannotated protein; Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis. | 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. | 0.474 |
dnaJ | GCA_002104455_00515 | GCA_002104455_00402 | GCA_002104455_00515 | 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 small heat shock protein (HSP20) family. | 0.688 |
dnaJ | GCA_002104455_01260 | GCA_002104455_00402 | GCA_002104455_01260 | 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. | 0.635 |
dnaJ | groL | GCA_002104455_00402 | GCA_002104455_03427 | 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. | 0.935 |
dnaJ | grpE | GCA_002104455_00402 | GCA_002104455_00400 | 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 [...] | 0.994 |
dnaJ | hslO | GCA_002104455_00402 | GCA_002104455_01261 | 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. | 0.656 |
dnaJ | hslU | GCA_002104455_00402 | GCA_002104455_01288 | 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. | 0.897 |
dnaJ | hslV | GCA_002104455_00402 | GCA_002104455_01287 | 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. | 0.839 |