| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Mnod_2958 | dnaJ | Mnod_2958 | Mnod_6930 | PFAM: Heat shock protein 70; KEGG: rso:RSp0521 chaperone transmembrane 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 [...] | 0.993 |
| Mnod_2958 | groL | Mnod_2958 | Mnod_0673 | PFAM: Heat shock protein 70; KEGG: rso:RSp0521 chaperone transmembrane protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.927 |
| Mnod_2958 | groL-2 | Mnod_2958 | Mnod_1767 | PFAM: Heat shock protein 70; KEGG: rso:RSp0521 chaperone transmembrane protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.927 |
| Mnod_2958 | groS | Mnod_2958 | Mnod_0674 | PFAM: Heat shock protein 70; KEGG: rso:RSp0521 chaperone transmembrane protein. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.872 |
| Mnod_2958 | groS-2 | Mnod_2958 | Mnod_1768 | PFAM: Heat shock protein 70; KEGG: rso:RSp0521 chaperone transmembrane protein. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.872 |
| Mnod_2958 | grpE | Mnod_2958 | Mnod_1146 | PFAM: Heat shock protein 70; KEGG: rso:RSp0521 chaperone transmembrane protein. | 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 [...] | 0.983 |
| Mnod_2958 | htpG | Mnod_2958 | Mnod_0044 | PFAM: Heat shock protein 70; KEGG: rso:RSp0521 chaperone transmembrane protein. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.922 |
| Mnod_2958 | lon | Mnod_2958 | Mnod_7407 | PFAM: Heat shock protein 70; KEGG: rso:RSp0521 chaperone transmembrane protein. | ATP-dependent protease La; 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. | 0.837 |
| Mnod_4817 | dnaJ | Mnod_4817 | Mnod_6930 | KEGG: met:M446_2578 HSP70 family molecular chaperone. | 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 [...] | 0.898 |
| Mnod_4817 | groL | Mnod_4817 | Mnod_0673 | KEGG: met:M446_2578 HSP70 family molecular chaperone. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.913 |
| Mnod_4817 | groL-2 | Mnod_4817 | Mnod_1767 | KEGG: met:M446_2578 HSP70 family molecular chaperone. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.913 |
| Mnod_4817 | groS | Mnod_4817 | Mnod_0674 | KEGG: met:M446_2578 HSP70 family molecular chaperone. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.871 |
| Mnod_4817 | groS-2 | Mnod_4817 | Mnod_1768 | KEGG: met:M446_2578 HSP70 family molecular chaperone. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.871 |
| Mnod_4817 | grpE | Mnod_4817 | Mnod_1146 | KEGG: met:M446_2578 HSP70 family molecular chaperone. | 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 [...] | 0.966 |
| Mnod_4817 | htpG | Mnod_4817 | Mnod_0044 | KEGG: met:M446_2578 HSP70 family molecular chaperone. | Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity. | 0.866 |
| Mnod_4817 | lon | Mnod_4817 | Mnod_7407 | KEGG: met:M446_2578 HSP70 family molecular chaperone. | ATP-dependent protease La; 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. | 0.779 |
| dnaJ | Mnod_2958 | Mnod_6930 | Mnod_2958 | 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 [...] | PFAM: Heat shock protein 70; KEGG: rso:RSp0521 chaperone transmembrane protein. | 0.993 |
| dnaJ | Mnod_4817 | Mnod_6930 | Mnod_4817 | 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 [...] | KEGG: met:M446_2578 HSP70 family molecular chaperone. | 0.898 |
| dnaJ | dnaK | Mnod_6930 | Mnod_6931 | 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 [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.997 |
| dnaJ | groL | Mnod_6930 | Mnod_0673 | 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 [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.918 |
