| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CEM60657.1 | CEM61310.1 | TPHV1_10325 | TPHV1_170041 | LysM domain protein. | ATPase/histidine kinase/DNA gyrase B/HSP90 domain protein (modular protein). | 0.709 |
| CEM60657.1 | clpX | TPHV1_10325 | TPHV1_120047 | LysM domain protein. | ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.539 |
| CEM60657.1 | groL | TPHV1_10325 | TPHV1_100069 | LysM domain protein. | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.966 |
| CEM60657.1 | grpE | TPHV1_10325 | TPHV1_110013 | LysM domain protein. | 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 ATP-dependent i [...] | 0.972 |
| CEM60657.1 | hslU | TPHV1_10325 | TPHV1_110046 | LysM domain protein. | Molecular chaperone and ATPase component of HslUV protease; 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. | 0.683 |
| CEM60657.1 | hslV | TPHV1_10325 | TPHV1_110045 | LysM domain protein. | Peptidase component of the HslUV protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.624 |
| CEM60657.1 | htpG | TPHV1_10325 | TPHV1_500015 | LysM domain protein. | Chaperone protein HtpG; Molecular chaperone. Has ATPase activity. | 0.984 |
| CEM60657.1 | lon | TPHV1_10325 | TPHV1_20056 | LysM domain protein. | Lon protease; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.898 |
| CEM61310.1 | CEM60657.1 | TPHV1_170041 | TPHV1_10325 | ATPase/histidine kinase/DNA gyrase B/HSP90 domain protein (modular protein). | LysM domain protein. | 0.709 |
| CEM61310.1 | clpX | TPHV1_170041 | TPHV1_120047 | ATPase/histidine kinase/DNA gyrase B/HSP90 domain protein (modular protein). | ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.621 |
| CEM61310.1 | dnaK | TPHV1_170041 | TPHV1_110012 | ATPase/histidine kinase/DNA gyrase B/HSP90 domain protein (modular protein). | Chaperone Hsp70, co-chaperone with DnaJ; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.564 |
| CEM61310.1 | groL | TPHV1_170041 | TPHV1_100069 | ATPase/histidine kinase/DNA gyrase B/HSP90 domain protein (modular protein). | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.685 |
| CEM61310.1 | grpE | TPHV1_170041 | TPHV1_110013 | ATPase/histidine kinase/DNA gyrase B/HSP90 domain protein (modular protein). | 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 ATP-dependent i [...] | 0.511 |
| CEM61310.1 | ileS | TPHV1_170041 | TPHV1_20065 | ATPase/histidine kinase/DNA gyrase B/HSP90 domain protein (modular protein). | Isoleucine--tRNA ligase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily. | 0.479 |
| CEM61310.1 | lon | TPHV1_170041 | TPHV1_20056 | ATPase/histidine kinase/DNA gyrase B/HSP90 domain protein (modular protein). | Lon protease; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.834 |
| clpX | CEM60657.1 | TPHV1_120047 | TPHV1_10325 | ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | LysM domain protein. | 0.539 |
| clpX | CEM61310.1 | TPHV1_120047 | TPHV1_170041 | ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | ATPase/histidine kinase/DNA gyrase B/HSP90 domain protein (modular protein). | 0.621 |
| clpX | dnaK | TPHV1_120047 | TPHV1_110012 | ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Chaperone Hsp70, co-chaperone with DnaJ; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.464 |
| clpX | groL | TPHV1_120047 | TPHV1_100069 | ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.832 |
| clpX | grpE | TPHV1_120047 | TPHV1_110013 | ATPase and specificity subunit of ClpX-ClpP ATP-dependent serine protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 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 ATP-dependent i [...] | 0.521 |
