| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| clpX | dnaJ | stu0581 | stu0121 | ATP-dependent Clp protease subunit X; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Heat shock protein, chaperonin; 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 [...] | 0.717 |
| clpX | dnaK | stu0581 | stu0120 | ATP-dependent Clp protease subunit X; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Heat shock protein, chaperonin; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.867 |
| clpX | groEL | stu0581 | stu0204 | ATP-dependent Clp protease subunit X; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Heat shock protein, chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.900 |
| clpX | groES | stu0581 | stu0203 | ATP-dependent Clp protease subunit X; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.859 |
| clpX | grpE | stu0581 | stu0119 | ATP-dependent Clp protease subunit X; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Heat shock protein, chaperonin; 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 [...] | 0.756 |
| clpX | hslO | stu0581 | stu0180 | ATP-dependent Clp protease subunit X; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Heat shock protein, chaperonin, 33 kDa; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.688 |
| clpX | msrA1 | stu0581 | stu1343 | ATP-dependent Clp protease subunit X; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.792 |
| dnaJ | clpX | stu0121 | stu0581 | Heat shock protein, chaperonin; 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 [...] | ATP-dependent Clp protease subunit X; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.717 |
| dnaJ | dnaK | stu0121 | stu0120 | Heat shock protein, chaperonin; 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 [...] | Heat shock protein, chaperonin; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | groEL | stu0121 | stu0204 | Heat shock protein, chaperonin; 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 [...] | Heat shock protein, chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.981 |
| dnaJ | groES | stu0121 | stu0203 | Heat shock protein, chaperonin; 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 [...] | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.946 |
| dnaJ | grpE | stu0121 | stu0119 | Heat shock protein, chaperonin; 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 [...] | Heat shock protein, chaperonin; 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 [...] | 0.997 |
| dnaJ | hslO | stu0121 | stu0180 | Heat shock protein, chaperonin; 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 [...] | Heat shock protein, chaperonin, 33 kDa; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.733 |
| dnaJ | msrA1 | stu0121 | stu1343 | Heat shock protein, chaperonin; 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 [...] | Peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.695 |
| dnaK | clpX | stu0120 | stu0581 | Heat shock protein, chaperonin; Acts as a chaperone; Belongs to the heat shock protein 70 family. | ATP-dependent Clp protease subunit X; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.867 |
| dnaK | dnaJ | stu0120 | stu0121 | Heat shock protein, chaperonin; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Heat shock protein, chaperonin; 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 [...] | 0.999 |
| dnaK | groEL | stu0120 | stu0204 | Heat shock protein, chaperonin; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Heat shock protein, chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.999 |
| dnaK | groES | stu0120 | stu0203 | Heat shock protein, chaperonin; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.996 |
| dnaK | grpE | stu0120 | stu0119 | Heat shock protein, chaperonin; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Heat shock protein, chaperonin; 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 [...] | 0.999 |
| dnaK | hslO | stu0120 | stu0180 | Heat shock protein, chaperonin; Acts as a chaperone; Belongs to the heat shock protein 70 family. | Heat shock protein, chaperonin, 33 kDa; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.675 |
