node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
GroS_3 | GrpE | PM8797T_09674 | PM8797T_23269 | Probable GroES chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | COG0576 Molecular chaperone GrpE (heat shock protein). | 0.760 |
GroS_3 | HtpG_2 | PM8797T_09674 | PM8797T_25291 | Probable GroES chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | COG0326 Molecular chaperone, HSP90 family. | 0.667 |
GroS_3 | dnaJ | PM8797T_09674 | PM8797T_15191 | Probable GroES chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 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 [...] | 0.546 |
GroS_3 | groL | PM8797T_09674 | PM8797T_07092 | Probable GroES chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | Heat shock protein GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.882 |
GroS_3 | groL-2 | PM8797T_09674 | PM8797T_15196 | Probable GroES chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 60 kDa chaperonin 5; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.882 |
GroS_3 | groL-3 | PM8797T_09674 | PM8797T_15206 | Probable GroES chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.882 |
GroS_3 | grpE | PM8797T_09674 | PM8797T_15186 | Probable GroES chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin 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 [...] | 0.760 |
GroS_3 | hslU | PM8797T_09674 | PM8797T_21798 | Probable GroES chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | ATP-dependent protease ATP-binding subunit; 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. | 0.769 |
GrpE | GroS_3 | PM8797T_23269 | PM8797T_09674 | COG0576 Molecular chaperone GrpE (heat shock protein). | Probable GroES chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.760 |
GrpE | HtpG_2 | PM8797T_23269 | PM8797T_25291 | COG0576 Molecular chaperone GrpE (heat shock protein). | COG0326 Molecular chaperone, HSP90 family. | 0.679 |
GrpE | dnaJ | PM8797T_23269 | PM8797T_15191 | COG0576 Molecular chaperone GrpE (heat shock 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 [...] | 0.858 |
GrpE | groL | PM8797T_23269 | PM8797T_07092 | COG0576 Molecular chaperone GrpE (heat shock protein). | Heat shock protein GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.823 |
GrpE | groL-2 | PM8797T_23269 | PM8797T_15196 | COG0576 Molecular chaperone GrpE (heat shock protein). | 60 kDa chaperonin 5; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.823 |
GrpE | groL-3 | PM8797T_23269 | PM8797T_15206 | COG0576 Molecular chaperone GrpE (heat shock protein). | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.823 |
GrpE | groS | PM8797T_23269 | PM8797T_07097 | COG0576 Molecular chaperone GrpE (heat shock protein). | 10 kDa chaperonin (Protein Cpn10) (groES protein); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.760 |
GrpE | groS-2 | PM8797T_23269 | PM8797T_15201 | COG0576 Molecular chaperone GrpE (heat shock protein). | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.760 |
GrpE | hslU | PM8797T_23269 | PM8797T_21798 | COG0576 Molecular chaperone GrpE (heat shock protein). | ATP-dependent protease ATP-binding subunit; 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. | 0.812 |
HtpG_2 | GroS_3 | PM8797T_25291 | PM8797T_09674 | COG0326 Molecular chaperone, HSP90 family. | Probable GroES chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.667 |
HtpG_2 | GrpE | PM8797T_25291 | PM8797T_23269 | COG0326 Molecular chaperone, HSP90 family. | COG0576 Molecular chaperone GrpE (heat shock protein). | 0.679 |
HtpG_2 | dnaJ | PM8797T_25291 | PM8797T_15191 | COG0326 Molecular chaperone, HSP90 family. | 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 [...] | 0.932 |