| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EU95_0190 | EU95_0195 | EU95_0190 | EU95_0195 | DnaJ-class molecular chaperone CbpA; Alternative locus ID: PMIT9201_0865. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.893 |
| EU95_0190 | EU95_0957 | EU95_0190 | EU95_0957 | DnaJ-class molecular chaperone CbpA; Alternative locus ID: PMIT9201_0865. | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMIT9201_0780; Belongs to the heat shock protein 70 family. | 0.897 |
| EU95_0190 | EU95_1876 | EU95_0190 | EU95_1876 | DnaJ-class molecular chaperone CbpA; Alternative locus ID: PMIT9201_0865. | Putative heat shock protein DnaJ; Alternative locus ID: PMIT9201_0208. | 0.462 |
| EU95_0190 | dnaK | EU95_0190 | EU95_0191 | DnaJ-class molecular chaperone CbpA; Alternative locus ID: PMIT9201_0865. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.990 |
| EU95_0190 | dnaK-2 | EU95_0190 | EU95_1573 | DnaJ-class molecular chaperone CbpA; Alternative locus ID: PMIT9201_0865. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.953 |
| EU95_0190 | groL | EU95_0190 | EU95_0126 | DnaJ-class molecular chaperone CbpA; Alternative locus ID: PMIT9201_0865. | Heat shock protein 60 family chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.627 |
| EU95_0190 | groL-2 | EU95_0190 | EU95_0953 | DnaJ-class molecular chaperone CbpA; Alternative locus ID: PMIT9201_0865. | Heat shock protein 60 family chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.627 |
| EU95_0190 | groS | EU95_0190 | EU95_0952 | DnaJ-class molecular chaperone CbpA; Alternative locus ID: PMIT9201_0865. | Heat shock protein 60 family co-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.461 |
| EU95_0195 | EU95_0190 | EU95_0195 | EU95_0190 | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | DnaJ-class molecular chaperone CbpA; Alternative locus ID: PMIT9201_0865. | 0.893 |
| EU95_0195 | EU95_0506 | EU95_0195 | EU95_0506 | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase); Alternative locus ID: PMIT9201_0471. | 0.910 |
| EU95_0195 | EU95_0957 | EU95_0195 | EU95_0957 | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMIT9201_0780; Belongs to the heat shock protein 70 family. | 0.954 |
| EU95_0195 | EU95_1876 | EU95_0195 | EU95_1876 | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | Putative heat shock protein DnaJ; Alternative locus ID: PMIT9201_0208. | 0.918 |
| EU95_0195 | dnaJ | EU95_0195 | EU95_1995 | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 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 [...] | 0.919 |
| EU95_0195 | dnaK | EU95_0195 | EU95_0191 | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.978 |
| EU95_0195 | dnaK-2 | EU95_0195 | EU95_1573 | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.967 |
| EU95_0195 | groL | EU95_0195 | EU95_0126 | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | Heat shock protein 60 family chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.960 |
| EU95_0195 | groL-2 | EU95_0195 | EU95_0953 | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | Heat shock protein 60 family chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.960 |
| EU95_0195 | groS | EU95_0195 | EU95_0952 | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | Heat shock protein 60 family co-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.923 |
| EU95_0506 | EU95_0195 | EU95_0506 | EU95_0195 | FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase); Alternative locus ID: PMIT9201_0471. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.910 |
| EU95_0506 | EU95_0957 | EU95_0506 | EU95_0957 | FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase); Alternative locus ID: PMIT9201_0471. | Putative DnaK-type molecular chaperone (HSP70 family); Alternative locus ID: PMIT9201_0780; Belongs to the heat shock protein 70 family. | 0.698 |