| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| PMM1293 | PMM1432 | PMM1293 | PMM1432 | FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase); Alternative locus ID: PMED4_14591. | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMED4_16401; Belongs to the heat shock protein 70 family. | 0.456 |
| PMM1293 | dnaK | PMM1293 | PMM0897 | FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase); Alternative locus ID: PMED4_14591. | Molecular chaperone DnaK, heat shock protein hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.456 |
| PMM1293 | dnaK2 | PMM1293 | PMM1704 | FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase); Alternative locus ID: PMED4_14591. | Molecular chaperone DnaK2, heat shock protein hsp70-2; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.465 |
| PMM1293 | htpG | PMM1293 | PMM0901 | FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase); Alternative locus ID: PMED4_14591. | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity. | 0.920 |
| PMM1432 | PMM1293 | PMM1432 | PMM1293 | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMED4_16401; Belongs to the heat shock protein 70 family. | FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase); Alternative locus ID: PMED4_14591. | 0.456 |
| PMM1432 | dnaJ | PMM1432 | PMM0017 | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMED4_16401; Belongs to the heat shock protein 70 family. | DnaJ 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 and Gr [...] | 0.863 |
| PMM1432 | dnaJ2 | PMM1432 | PMM0896 | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMED4_16401; Belongs to the heat shock protein 70 family. | DnaJ2 protein; Alternative locus ID: PMED4_10071. | 0.822 |
| PMM1432 | groEL | PMM1432 | PMM1436 | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMED4_16401; Belongs to the heat shock protein 70 family. | GroEL protein (Chaperonin cpn60); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.688 |
| PMM1432 | groEL2,cpn60-2 | PMM1432 | PMM0452 | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMED4_16401; Belongs to the heat shock protein 70 family. | GroEL2 protein (Chaperonin cpn60 2); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.691 |
| PMM1432 | groES | PMM1432 | PMM1437 | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMED4_16401; Belongs to the heat shock protein 70 family. | GroES protein (Chaperonin cpn10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.718 |
| PMM1432 | grpE | PMM1432 | PMM0016 | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMED4_16401; Belongs to the heat shock protein 70 family. | 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. Several rounds of ATP- [...] | 0.888 |
| PMM1432 | htpG | PMM1432 | PMM0901 | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMED4_16401; Belongs to the heat shock protein 70 family. | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity. | 0.897 |
| dnaJ | PMM1432 | PMM0017 | PMM1432 | DnaJ 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 and Gr [...] | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMED4_16401; Belongs to the heat shock protein 70 family. | 0.863 |
| dnaJ | dnaK | PMM0017 | PMM0897 | DnaJ 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 and Gr [...] | Molecular chaperone DnaK, heat shock protein hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.975 |
| dnaJ | dnaK2 | PMM0017 | PMM1704 | DnaJ 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 and Gr [...] | Molecular chaperone DnaK2, heat shock protein hsp70-2; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.963 |
| dnaJ | groEL | PMM0017 | PMM1436 | DnaJ 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 and Gr [...] | GroEL protein (Chaperonin cpn60); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.785 |
| dnaJ | groEL2,cpn60-2 | PMM0017 | PMM0452 | DnaJ 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 and Gr [...] | GroEL2 protein (Chaperonin cpn60 2); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.525 |
| dnaJ | groES | PMM0017 | PMM1437 | DnaJ 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 and Gr [...] | GroES protein (Chaperonin cpn10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.876 |
| dnaJ | grpE | PMM0017 | PMM0016 | DnaJ 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 and Gr [...] | 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. Several rounds of ATP- [...] | 0.988 |
| dnaJ | htpG | PMM0017 | PMM0901 | DnaJ 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 and Gr [...] | Heat shock protein HtpG; Molecular chaperone. Has ATPase activity. | 0.889 |