| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Tcur_0495 | dnaJ-2 | Tcur_0495 | Tcur_3252 | PFAM: ATP-binding region ATPase domain protein; SMART: ATP-binding region ATPase domain protein; KEGG: mxa:MXAN_1393 HSP90 family 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 [...] | 0.889 |
| Tcur_0495 | groL | Tcur_0495 | Tcur_0804 | PFAM: ATP-binding region ATPase domain protein; SMART: ATP-binding region ATPase domain protein; KEGG: mxa:MXAN_1393 HSP90 family protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.795 |
| Tcur_0495 | groL-2 | Tcur_0495 | Tcur_4257 | PFAM: ATP-binding region ATPase domain protein; SMART: ATP-binding region ATPase domain protein; KEGG: mxa:MXAN_1393 HSP90 family protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.795 |
| Tcur_0495 | groS | Tcur_0495 | Tcur_4258 | PFAM: ATP-binding region ATPase domain protein; SMART: ATP-binding region ATPase domain protein; KEGG: mxa:MXAN_1393 HSP90 family protein. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.793 |
| Tcur_0495 | grpE | Tcur_0495 | Tcur_0237 | PFAM: ATP-binding region ATPase domain protein; SMART: ATP-binding region ATPase domain protein; KEGG: mxa:MXAN_1393 HSP90 family protein. | 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 [...] | 0.609 |
| Tcur_4208 | dnaJ-2 | Tcur_4208 | Tcur_3252 | PFAM: ATP-binding region ATPase domain protein; SMART: ATP-binding region ATPase domain protein; KEGG: mxa:MXAN_1393 HSP90 family 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 [...] | 0.889 |
| Tcur_4208 | groL | Tcur_4208 | Tcur_0804 | PFAM: ATP-binding region ATPase domain protein; SMART: ATP-binding region ATPase domain protein; KEGG: mxa:MXAN_1393 HSP90 family protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.795 |
| Tcur_4208 | groL-2 | Tcur_4208 | Tcur_4257 | PFAM: ATP-binding region ATPase domain protein; SMART: ATP-binding region ATPase domain protein; KEGG: mxa:MXAN_1393 HSP90 family protein. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.795 |
| Tcur_4208 | groS | Tcur_4208 | Tcur_4258 | PFAM: ATP-binding region ATPase domain protein; SMART: ATP-binding region ATPase domain protein; KEGG: mxa:MXAN_1393 HSP90 family protein. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.793 |
| Tcur_4208 | grpE | Tcur_4208 | Tcur_0237 | PFAM: ATP-binding region ATPase domain protein; SMART: ATP-binding region ATPase domain protein; KEGG: mxa:MXAN_1393 HSP90 family protein. | 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 [...] | 0.609 |
| clpP-2 | clpX | Tcur_1530 | Tcur_1531 | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | ATP-dependent Clp protease, ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.998 |
| clpP-2 | dnaJ-2 | Tcur_1530 | Tcur_3252 | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 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 [...] | 0.471 |
| clpP-2 | groL | Tcur_1530 | Tcur_0804 | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.690 |
| clpP-2 | groL-2 | Tcur_1530 | Tcur_4257 | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.688 |
| clpP-2 | groS | Tcur_1530 | Tcur_4258 | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.747 |
| clpP-2 | grpE | Tcur_1530 | Tcur_0237 | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 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 [...] | 0.658 |
| clpP-2 | hrcA | Tcur_1530 | Tcur_3253 | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.783 |
| clpP-2 | tig | Tcur_1530 | Tcur_1528 | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.697 |
| clpX | clpP-2 | Tcur_1531 | Tcur_1530 | ATP-dependent Clp protease, ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Endopeptidase Clp; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.998 |
| clpX | groL | Tcur_1531 | Tcur_0804 | ATP-dependent Clp protease, ATP-binding subunit ClpX; 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 GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.602 |