| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| clpB | dnaJ | Cla_0711 | Cla_0493 | Protein disaggregating chaperone ClpB; Pfam matches to PF02861.11 Clp_N, and to PF00004.20 AAA; Belongs to the ClpA/ClpB family. | Co-chaperone and heat shock 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 be [...] | 0.786 |
| clpB | dnaK | Cla_0711 | Cla_0935 | Protein disaggregating chaperone ClpB; Pfam matches to PF02861.11 Clp_N, and to PF00004.20 AAA; Belongs to the ClpA/ClpB family. | Chaperone and heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.988 |
| clpB | groEL | Cla_0711 | Cla_1034 | Protein disaggregating chaperone ClpB; Pfam matches to PF02861.11 Clp_N, and to PF00004.20 AAA; Belongs to the ClpA/ClpB family. | 60 kD chaperonin (cpn60); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.828 |
| clpB | groES | Cla_0711 | Cla_1035 | Protein disaggregating chaperone ClpB; Pfam matches to PF02861.11 Clp_N, and to PF00004.20 AAA; Belongs to the ClpA/ClpB family. | 10 kD chaperonin (cpn10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.837 |
| clpB | grpE | Cla_0711 | Cla_0936 | Protein disaggregating chaperone ClpB; Pfam matches to PF02861.11 Clp_N, and to PF00004.20 AAA; Belongs to the ClpA/ClpB family. | Co-chaperone 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 AT [...] | 0.915 |
| clpB | hslU | Cla_0711 | Cla_0757 | Protein disaggregating chaperone ClpB; Pfam matches to PF02861.11 Clp_N, and to PF00004.20 AAA; Belongs to the ClpA/ClpB family. | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.706 |
| clpB | hslV | Cla_0711 | Cla_0756 | Protein disaggregating chaperone ClpB; Pfam matches to PF02861.11 Clp_N, and to PF00004.20 AAA; Belongs to the ClpA/ClpB family. | Heat shock protein HslVU, ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.480 |
| clpB | htpG | Cla_0711 | Cla_0703 | Protein disaggregating chaperone ClpB; Pfam matches to PF02861.11 Clp_N, and to PF00004.20 AAA; Belongs to the ClpA/ClpB family. | Heat shock protein HtpG, chaperone Hsp90; Molecular chaperone. Has ATPase activity. | 0.958 |
| dnaJ | clpB | Cla_0493 | Cla_0711 | Co-chaperone and heat shock 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 be [...] | Protein disaggregating chaperone ClpB; Pfam matches to PF02861.11 Clp_N, and to PF00004.20 AAA; Belongs to the ClpA/ClpB family. | 0.786 |
| dnaJ | dnaK | Cla_0493 | Cla_0935 | Co-chaperone and heat shock 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 be [...] | Chaperone and heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.996 |
| dnaJ | groEL | Cla_0493 | Cla_1034 | Co-chaperone and heat shock 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 be [...] | 60 kD chaperonin (cpn60); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.963 |
| dnaJ | groES | Cla_0493 | Cla_1035 | Co-chaperone and heat shock 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 be [...] | 10 kD chaperonin (cpn10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.855 |
| dnaJ | grpE | Cla_0493 | Cla_0936 | Co-chaperone and heat shock 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 be [...] | Co-chaperone 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 AT [...] | 0.988 |
| dnaJ | hslU | Cla_0493 | Cla_0757 | Co-chaperone and heat shock 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 be [...] | Heat shock protein HslVU, ATPase subunit HslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.894 |
| dnaJ | hslV | Cla_0493 | Cla_0756 | Co-chaperone and heat shock 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 be [...] | Heat shock protein HslVU, ATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.885 |
| dnaJ | htpG | Cla_0493 | Cla_0703 | Co-chaperone and heat shock 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 be [...] | Heat shock protein HtpG, chaperone Hsp90; Molecular chaperone. Has ATPase activity. | 0.950 |
| dnaK | clpB | Cla_0935 | Cla_0711 | Chaperone and heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Protein disaggregating chaperone ClpB; Pfam matches to PF02861.11 Clp_N, and to PF00004.20 AAA; Belongs to the ClpA/ClpB family. | 0.988 |
| dnaK | dnaJ | Cla_0935 | Cla_0493 | Chaperone and heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Co-chaperone and heat shock 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 be [...] | 0.996 |
| dnaK | groEL | Cla_0935 | Cla_1034 | Chaperone and heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 60 kD chaperonin (cpn60); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.994 |
| dnaK | groES | Cla_0935 | Cla_1035 | Chaperone and heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 10 kD chaperonin (cpn10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.985 |
