| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| THII_0915 | groL | THII_0915 | THII_1490 | Ni,Fe-hydrogenase III large subunit. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.914 |
| THII_2208 | dnaJ | THII_2208 | THII_2709 | Polyketide synthase. | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | 0.737 |
| THII_2208 | dnaK | THII_2208 | THII_2710 | Polyketide synthase. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.841 |
| THII_2208 | groL | THII_2208 | THII_1490 | Polyketide synthase. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.904 |
| THII_2208 | groS | THII_2208 | THII_1489 | Polyketide synthase. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.734 |
| THII_2208 | hscA | THII_2208 | THII_2630 | Polyketide synthase. | Chaperone protein HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.841 |
| THII_2208 | htpG | THII_2208 | THII_0411 | Polyketide synthase. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.812 |
| THII_2208 | mdh | THII_2208 | THII_3446 | Polyketide synthase. | Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. Belongs to the LDH/MDH superfamily. MDH type 2 family. | 0.947 |
| dnaJ | THII_2208 | THII_2709 | THII_2208 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | Polyketide synthase. | 0.737 |
| dnaJ | dnaK | THII_2709 | THII_2710 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.993 |
| dnaJ | groL | THII_2709 | THII_1490 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.972 |
| dnaJ | groS | THII_2709 | THII_1489 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.886 |
| dnaJ | grpE | THII_2709 | THII_2711 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | GrpE 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-dependent i [...] | 0.985 |
| dnaJ | hscA | THII_2709 | THII_2630 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | Chaperone protein HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. | 0.987 |
| dnaJ | hslU | THII_2709 | THII_1597 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | ATP-dependent 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. | 0.966 |
| dnaJ | htpG | THII_2709 | THII_0411 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.982 |
| dnaK | THII_2208 | THII_2710 | THII_2208 | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Polyketide synthase. | 0.841 |
| dnaK | dnaJ | THII_2710 | THII_2709 | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | DnaJ-class molecular chaperone with C-terminal Zn finger domain; 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 A [...] | 0.993 |
| dnaK | groL | THII_2710 | THII_1490 | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.973 |
| dnaK | groS | THII_2710 | THII_1489 | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.922 |
