| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| HP_0060 | dnaJ | HP_0060 | HP_1332 | Predicted coding region HP0060; Hypothetical protein; identified by GeneMark; putative. | Co-chaperone and heat shock 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 interact [...] | 0.985 |
| HP_0060 | groL | HP_0060 | HP_0010 | Predicted coding region HP0060; Hypothetical protein; identified by GeneMark; putative. | Chaperone and heat shock protein (groEL); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.934 |
| HP_0060 | groS | HP_0060 | HP_0011 | Predicted coding region HP0060; Hypothetical protein; identified by GeneMark; putative. | Co-chaperone (groES); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.858 |
| HP_0060 | grpE | HP_0060 | HP_0110 | Predicted coding region HP0060; Hypothetical protein; identified by GeneMark; putative. | Co-chaperone and 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. Sev [...] | 0.986 |
| HP_0060 | hslU | HP_0060 | HP_0516 | Predicted coding region HP0060; Hypothetical protein; identified by GeneMark; putative. | Heat shock protein (hslU) ORF1; 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. | 0.561 |
| HP_0060 | hslV | HP_0060 | HP_0515 | Predicted coding region HP0060; Hypothetical protein; identified by GeneMark; putative. | Heat shock protein (hslV); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.460 |
| HP_0060 | htpG | HP_0060 | HP_0210 | Predicted coding region HP0060; Hypothetical protein; identified by GeneMark; putative. | Chaperone and heat shock protein C62.5 (htpG); Molecular chaperone. Has ATPase activity. | 0.998 |
| HP_0060 | ppiA | HP_0060 | HP_1441 | Predicted coding region HP0060; Hypothetical protein; identified by GeneMark; putative. | Peptidyl-prolyl cis-trans isomerase B, cyclosporin-type rotamase (ppi); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity); Belongs to the cyclophilin-type PPIase family. | 0.726 |
| HP_1030 | groL | HP_1030 | HP_0010 | fliY protein (fliY); Similar to GB:M86738 SP:P24073 PID:142926 PID:551704 GB:AL009126 percent identity: 29.27; identified by sequence similarity; putative. | Chaperone and heat shock protein (groEL); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.943 |
| HP_1030 | grpE | HP_1030 | HP_0110 | fliY protein (fliY); Similar to GB:M86738 SP:P24073 PID:142926 PID:551704 GB:AL009126 percent identity: 29.27; identified by sequence similarity; putative. | Co-chaperone and 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. Sev [...] | 0.463 |
| dnaJ | HP_0060 | HP_1332 | HP_0060 | Co-chaperone and heat shock 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 interact [...] | Predicted coding region HP0060; Hypothetical protein; identified by GeneMark; putative. | 0.985 |
| dnaJ | dnaK | HP_1332 | HP_0109 | Co-chaperone and heat shock 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 interact [...] | Chaperone and heat shock protein 70 (dnaK); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | groL | HP_1332 | HP_0010 | Co-chaperone and heat shock 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 interact [...] | Chaperone and heat shock protein (groEL); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.916 |
| dnaJ | groS | HP_1332 | HP_0011 | Co-chaperone and heat shock 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 interact [...] | Co-chaperone (groES); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.868 |
| dnaJ | grpE | HP_1332 | HP_0110 | Co-chaperone and heat shock 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 interact [...] | Co-chaperone and 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. Sev [...] | 0.984 |
| dnaJ | hslU | HP_1332 | HP_0516 | Co-chaperone and heat shock 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 interact [...] | Heat shock protein (hslU) ORF1; 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. | 0.918 |
| dnaJ | hslV | HP_1332 | HP_0515 | Co-chaperone and heat shock 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 interact [...] | Heat shock protein (hslV); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.893 |
| dnaJ | htpG | HP_1332 | HP_0210 | Co-chaperone and heat shock 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 interact [...] | Chaperone and heat shock protein C62.5 (htpG); Molecular chaperone. Has ATPase activity. | 0.995 |
| dnaJ | ppiA | HP_1332 | HP_1441 | Co-chaperone and heat shock 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 interact [...] | Peptidyl-prolyl cis-trans isomerase B, cyclosporin-type rotamase (ppi); PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity); Belongs to the cyclophilin-type PPIase family. | 0.901 |
| dnaK | dnaJ | HP_0109 | HP_1332 | Chaperone and heat shock protein 70 (dnaK); Acts as a chaperone; Belongs to the heat shock protein 70 family. | Co-chaperone and heat shock 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 interact [...] | 0.999 |
STRING v12.5 is now available!
