| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| EccCa1_2 | RMCT_0537 | RMCT_4070 | RMCT_0537 | Cell division protein FtsK. | Putative uncharacterized protein. | 0.974 |
| EccCa1_2 | RMCT_0539 | RMCT_4070 | RMCT_0539 | Cell division protein FtsK. | Putative uncharacterized protein. | 0.781 |
| EccCa1_3 | RMCT_0537 | RMCT_0538 | RMCT_0537 | Cell division FtsK/SpoIIIE. | Putative uncharacterized protein. | 0.986 |
| EccCa1_3 | RMCT_0539 | RMCT_0538 | RMCT_0539 | Cell division FtsK/SpoIIIE. | Putative uncharacterized protein. | 0.948 |
| RMCT_0537 | EccCa1_2 | RMCT_0537 | RMCT_4070 | Putative uncharacterized protein. | Cell division protein FtsK. | 0.974 |
| RMCT_0537 | EccCa1_3 | RMCT_0537 | RMCT_0538 | Putative uncharacterized protein. | Cell division FtsK/SpoIIIE. | 0.986 |
| RMCT_0537 | RMCT_0539 | RMCT_0537 | RMCT_0539 | Putative uncharacterized protein. | Putative uncharacterized protein. | 0.956 |
| RMCT_0539 | EccCa1_2 | RMCT_0539 | RMCT_4070 | Putative uncharacterized protein. | Cell division protein FtsK. | 0.781 |
| RMCT_0539 | EccCa1_3 | RMCT_0539 | RMCT_0538 | Putative uncharacterized protein. | Cell division FtsK/SpoIIIE. | 0.948 |
| RMCT_0539 | RMCT_0537 | RMCT_0539 | RMCT_0537 | Putative uncharacterized protein. | Putative uncharacterized protein. | 0.956 |
| RMCT_0539 | dnaJ | RMCT_0539 | RMCT_0768 | Putative uncharacterized protein. | Chaperone dnaJ2; 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 [...] | 0.872 |
| RMCT_0539 | dnaJ-2 | RMCT_0539 | RMCT_4021 | Putative uncharacterized protein. | Chaperone dnaJ1; 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 [...] | 0.872 |
| RMCT_0539 | groEL | RMCT_0539 | RMCT_0566 | Putative uncharacterized protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.810 |
| RMCT_0539 | groEL-2 | RMCT_0539 | RMCT_2684 | Putative uncharacterized protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.810 |
| RMCT_0539 | groES | RMCT_0539 | RMCT_0565 | Putative uncharacterized protein. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.794 |
| RMCT_0539 | grpE | RMCT_0539 | RMCT_4022 | Putative uncharacterized protein. | GrpE protein HSP-70 cofactor; 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 [...] | 0.948 |
| RMCT_0539 | rplM | RMCT_0539 | RMCT_0542 | Putative uncharacterized protein. | 50S ribosomal protein L13; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. | 0.764 |
| dnaJ | RMCT_0539 | RMCT_0768 | RMCT_0539 | Chaperone dnaJ2; 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 [...] | Putative uncharacterized protein. | 0.872 |
| dnaJ | groEL | RMCT_0768 | RMCT_0566 | Chaperone dnaJ2; 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 [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.955 |
| dnaJ | groEL-2 | RMCT_0768 | RMCT_2684 | Chaperone dnaJ2; 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 [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.948 |