node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Atu0988 | dnaJ | Atu0988 | Atu0121 | Molecular chaperone, Hsp70 family. | Molecular chaperone, DnaJ family; 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 betwe [...] | 0.899 |
Atu0988 | dnaJ-2 | Atu0988 | Atu0758 | Molecular chaperone, Hsp70 family. | Molecular chaperone, DnaJ family. | 0.899 |
Atu0988 | dnaJ-3 | Atu0988 | Atu2006 | Molecular chaperone, Hsp70 family. | Molecular chaperone, DnaJ family. | 0.892 |
Atu0988 | groEL | Atu0988 | Atu0682 | Molecular chaperone, Hsp70 family. | GroEL chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.908 |
Atu0988 | groES | Atu0988 | Atu0683 | Molecular chaperone, Hsp70 family. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.855 |
Atu0988 | grpE | Atu0988 | Atu0329 | Molecular chaperone, Hsp70 family. | GRPE protein; 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 ATP-dependent i [...] | 0.944 |
Atu0988 | hslU | Atu0988 | Atu0045 | Molecular chaperone, Hsp70 family. | Heat shock chaperone; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.593 |
Atu0988 | hslV | Atu0988 | Atu0044 | Molecular chaperone, Hsp70 family. | Heat shock protein hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.539 |
dnaJ | Atu0988 | Atu0121 | Atu0988 | Molecular chaperone, DnaJ family; 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 betwe [...] | Molecular chaperone, Hsp70 family. | 0.899 |
dnaJ | dnaK | Atu0121 | Atu0122 | Molecular chaperone, DnaJ family; 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 betwe [...] | DNAK Protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
dnaJ | groEL | Atu0121 | Atu0682 | Molecular chaperone, DnaJ family; 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 betwe [...] | GroEL chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.915 |
dnaJ | groES | Atu0121 | Atu0683 | Molecular chaperone, DnaJ family; 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 betwe [...] | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.866 |
dnaJ | grpE | Atu0121 | Atu0329 | Molecular chaperone, DnaJ family; 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 betwe [...] | GRPE protein; 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 ATP-dependent i [...] | 0.943 |
dnaJ | hslU | Atu0121 | Atu0045 | Molecular chaperone, DnaJ family; 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 betwe [...] | Heat shock chaperone; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. | 0.782 |
dnaJ | hslV | Atu0121 | Atu0044 | Molecular chaperone, DnaJ family; 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 betwe [...] | Heat shock protein hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.710 |
dnaJ-2 | Atu0988 | Atu0758 | Atu0988 | Molecular chaperone, DnaJ family. | Molecular chaperone, Hsp70 family. | 0.899 |
dnaJ-2 | dnaK | Atu0758 | Atu0122 | Molecular chaperone, DnaJ family. | DNAK Protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.987 |
dnaJ-2 | groEL | Atu0758 | Atu0682 | Molecular chaperone, DnaJ family. | GroEL chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.875 |
dnaJ-2 | groES | Atu0758 | Atu0683 | Molecular chaperone, DnaJ family. | Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.798 |
dnaJ-2 | grpE | Atu0758 | Atu0329 | Molecular chaperone, DnaJ family. | GRPE protein; 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 ATP-dependent i [...] | 0.912 |