| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ACPL_142 | ACPL_8205 | ACPL_142 | ACPL_8205 | Hypothetical protein; FOG: TPR repeat. | Hypothetical protein. | 0.690 |
| ACPL_142 | htpG | ACPL_142 | ACPL_141 | Hypothetical protein; FOG: TPR repeat. | Chaperone protein htpG; Molecular chaperone, HSP90 family. | 0.979 |
| ACPL_3161 | ACPL_8205 | ACPL_3161 | ACPL_8205 | Hypothetical protein. | Hypothetical protein. | 0.971 |
| ACPL_3161 | htpG | ACPL_3161 | ACPL_141 | Hypothetical protein. | Chaperone protein htpG; Molecular chaperone, HSP90 family. | 0.884 |
| ACPL_6712 | ACPL_8205 | ACPL_6712 | ACPL_8205 | Serine/threonine protein kinase. | Hypothetical protein. | 0.974 |
| ACPL_6712 | htpG | ACPL_6712 | ACPL_141 | Serine/threonine protein kinase. | Chaperone protein htpG; Molecular chaperone, HSP90 family. | 0.884 |
| ACPL_8205 | ACPL_142 | ACPL_8205 | ACPL_142 | Hypothetical protein. | Hypothetical protein; FOG: TPR repeat. | 0.690 |
| ACPL_8205 | ACPL_3161 | ACPL_8205 | ACPL_3161 | Hypothetical protein. | Hypothetical protein. | 0.971 |
| ACPL_8205 | ACPL_6712 | ACPL_8205 | ACPL_6712 | Hypothetical protein. | Serine/threonine protein kinase. | 0.974 |
| ACPL_8205 | dnaJ | ACPL_8205 | ACPL_1406 | Hypothetical 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 [...] | 0.643 |
| ACPL_8205 | dnaJ-2 | ACPL_8205 | ACPL_202 | Hypothetical protein. | Molecular chaperone 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, [...] | 0.643 |
| ACPL_8205 | dnaK-4 | ACPL_8205 | ACPL_8203 | Hypothetical protein. | Heat shock protein 70; Molecular chaperone; Belongs to the heat shock protein 70 family. | 0.917 |
| ACPL_8205 | groL | ACPL_8205 | ACPL_7986 | Hypothetical protein. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.453 |
| ACPL_8205 | groL-2 | ACPL_8205 | ACPL_854 | Hypothetical protein. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.453 |
| ACPL_8205 | htpG | ACPL_8205 | ACPL_141 | Hypothetical protein. | Chaperone protein htpG; Molecular chaperone, HSP90 family. | 0.908 |
| dnaJ | ACPL_8205 | ACPL_1406 | ACPL_8205 | 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 [...] | Hypothetical protein. | 0.643 |
| dnaJ | dnaK-4 | ACPL_1406 | ACPL_8203 | 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 [...] | Heat shock protein 70; Molecular chaperone; Belongs to the heat shock protein 70 family. | 0.933 |
| dnaJ | groL | ACPL_1406 | ACPL_7986 | 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 [...] | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.809 |
| dnaJ | groL-2 | ACPL_1406 | ACPL_854 | 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 [...] | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.808 |
| dnaJ | groS | ACPL_1406 | ACPL_855 | 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 [...] | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.739 |