| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Toce_0907 | Toce_2123 | Toce_0907 | Toce_2123 | COGs: COG0459 Chaperonin GroEL (HSP60 family); InterPro IPR002194:IPR017998:IPR002423; KEGG: pth:PTH_0876 chaperonin GroEL; PFAM: chaperonin Cpn60/TCP-1; SPTR: Chaperonin Cpn60/TCP-1; PFAM: TCP-1/cpn60 chaperonin family. | ATPase AAA-2 domain protein; COGs: COG0542 ATPase with chaperone activity ATP-binding subunit; InterProIPR003593:IPR018368:IPR001270:IPR004176:IPR 003959:IPR001943:IPR013093:IPR019489; KEGG: tte:TTE2327 ATPase with chaperone activity, ATP-binding subunit; PFAM: ATPase AAA-2 domain protein; Clp domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; Clp ATPase-like; SMART: AAA ATPase; SPTR: ATPases with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; ATPase family associat [...] | 0.664 |
| Toce_0907 | dnaJ | Toce_0907 | Toce_0910 | COGs: COG0459 Chaperonin GroEL (HSP60 family); InterPro IPR002194:IPR017998:IPR002423; KEGG: pth:PTH_0876 chaperonin GroEL; PFAM: chaperonin Cpn60/TCP-1; SPTR: Chaperonin Cpn60/TCP-1; PFAM: TCP-1/cpn60 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 [...] | 0.960 |
| Toce_0907 | groS | Toce_0907 | Toce_0277 | COGs: COG0459 Chaperonin GroEL (HSP60 family); InterPro IPR002194:IPR017998:IPR002423; KEGG: pth:PTH_0876 chaperonin GroEL; PFAM: chaperonin Cpn60/TCP-1; SPTR: Chaperonin Cpn60/TCP-1; PFAM: TCP-1/cpn60 chaperonin family. | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.982 |
| Toce_0907 | grpE | Toce_0907 | Toce_0908 | COGs: COG0459 Chaperonin GroEL (HSP60 family); InterPro IPR002194:IPR017998:IPR002423; KEGG: pth:PTH_0876 chaperonin GroEL; PFAM: chaperonin Cpn60/TCP-1; SPTR: Chaperonin Cpn60/TCP-1; PFAM: TCP-1/cpn60 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 [...] | 0.989 |
| Toce_0907 | hslU | Toce_0907 | Toce_1089 | COGs: COG0459 Chaperonin GroEL (HSP60 family); InterPro IPR002194:IPR017998:IPR002423; KEGG: pth:PTH_0876 chaperonin GroEL; PFAM: chaperonin Cpn60/TCP-1; SPTR: Chaperonin Cpn60/TCP-1; PFAM: TCP-1/cpn60 chaperonin family. | Heat shock protein HslVU, ATPase subunit HslU; 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. | 0.774 |
| Toce_0907 | hslV | Toce_0907 | Toce_1088 | COGs: COG0459 Chaperonin GroEL (HSP60 family); InterPro IPR002194:IPR017998:IPR002423; KEGG: pth:PTH_0876 chaperonin GroEL; PFAM: chaperonin Cpn60/TCP-1; SPTR: Chaperonin Cpn60/TCP-1; PFAM: TCP-1/cpn60 chaperonin family. | ATP dependent peptidase CodWX, CodW component; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.735 |
| Toce_0907 | lon | Toce_0907 | Toce_1764 | COGs: COG0459 Chaperonin GroEL (HSP60 family); InterPro IPR002194:IPR017998:IPR002423; KEGG: pth:PTH_0876 chaperonin GroEL; PFAM: chaperonin Cpn60/TCP-1; SPTR: Chaperonin Cpn60/TCP-1; PFAM: TCP-1/cpn60 chaperonin family. | ATP-dependent proteinase; 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. | 0.909 |
| Toce_2123 | Toce_0907 | Toce_2123 | Toce_0907 | ATPase AAA-2 domain protein; COGs: COG0542 ATPase with chaperone activity ATP-binding subunit; InterProIPR003593:IPR018368:IPR001270:IPR004176:IPR 003959:IPR001943:IPR013093:IPR019489; KEGG: tte:TTE2327 ATPase with chaperone activity, ATP-binding subunit; PFAM: ATPase AAA-2 domain protein; Clp domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; Clp ATPase-like; SMART: AAA ATPase; SPTR: ATPases with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; ATPase family associat [...] | COGs: COG0459 Chaperonin GroEL (HSP60 family); InterPro IPR002194:IPR017998:IPR002423; KEGG: pth:PTH_0876 chaperonin GroEL; PFAM: chaperonin Cpn60/TCP-1; SPTR: Chaperonin Cpn60/TCP-1; PFAM: TCP-1/cpn60 chaperonin family. | 0.664 |
| Toce_2123 | dnaJ | Toce_2123 | Toce_0910 | ATPase AAA-2 domain protein; COGs: COG0542 ATPase with chaperone activity ATP-binding subunit; InterProIPR003593:IPR018368:IPR001270:IPR004176:IPR 003959:IPR001943:IPR013093:IPR019489; KEGG: tte:TTE2327 ATPase with chaperone activity, ATP-binding subunit; PFAM: ATPase AAA-2 domain protein; Clp domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; Clp ATPase-like; SMART: AAA ATPase; SPTR: ATPases with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; ATPase family associat [...] | 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 [...] | 0.950 |
| Toce_2123 | groL | Toce_2123 | Toce_0278 | ATPase AAA-2 domain protein; COGs: COG0542 ATPase with chaperone activity ATP-binding subunit; InterProIPR003593:IPR018368:IPR001270:IPR004176:IPR 003959:IPR001943:IPR013093:IPR019489; KEGG: tte:TTE2327 ATPase with chaperone activity, ATP-binding subunit; PFAM: ATPase AAA-2 domain protein; Clp domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; Clp ATPase-like; SMART: AAA ATPase; SPTR: ATPases with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; ATPase family associat [...] | Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.664 |
| Toce_2123 | groS | Toce_2123 | Toce_0277 | ATPase AAA-2 domain protein; COGs: COG0542 ATPase with chaperone activity ATP-binding subunit; InterProIPR003593:IPR018368:IPR001270:IPR004176:IPR 003959:IPR001943:IPR013093:IPR019489; KEGG: tte:TTE2327 ATPase with chaperone activity, ATP-binding subunit; PFAM: ATPase AAA-2 domain protein; Clp domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; Clp ATPase-like; SMART: AAA ATPase; SPTR: ATPases with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; ATPase family associat [...] | Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.786 |
| Toce_2123 | grpE | Toce_2123 | Toce_0908 | ATPase AAA-2 domain protein; COGs: COG0542 ATPase with chaperone activity ATP-binding subunit; InterProIPR003593:IPR018368:IPR001270:IPR004176:IPR 003959:IPR001943:IPR013093:IPR019489; KEGG: tte:TTE2327 ATPase with chaperone activity, ATP-binding subunit; PFAM: ATPase AAA-2 domain protein; Clp domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; Clp ATPase-like; SMART: AAA ATPase; SPTR: ATPases with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; ATPase family associat [...] | 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 [...] | 0.911 |
| Toce_2123 | hslU | Toce_2123 | Toce_1089 | ATPase AAA-2 domain protein; COGs: COG0542 ATPase with chaperone activity ATP-binding subunit; InterProIPR003593:IPR018368:IPR001270:IPR004176:IPR 003959:IPR001943:IPR013093:IPR019489; KEGG: tte:TTE2327 ATPase with chaperone activity, ATP-binding subunit; PFAM: ATPase AAA-2 domain protein; Clp domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; Clp ATPase-like; SMART: AAA ATPase; SPTR: ATPases with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; ATPase family associat [...] | Heat shock protein HslVU, ATPase subunit HslU; 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. | 0.817 |
| Toce_2123 | hslV | Toce_2123 | Toce_1088 | ATPase AAA-2 domain protein; COGs: COG0542 ATPase with chaperone activity ATP-binding subunit; InterProIPR003593:IPR018368:IPR001270:IPR004176:IPR 003959:IPR001943:IPR013093:IPR019489; KEGG: tte:TTE2327 ATPase with chaperone activity, ATP-binding subunit; PFAM: ATPase AAA-2 domain protein; Clp domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; Clp ATPase-like; SMART: AAA ATPase; SPTR: ATPases with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; ATPase family associat [...] | ATP dependent peptidase CodWX, CodW component; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.712 |
| Toce_2123 | lon | Toce_2123 | Toce_1764 | ATPase AAA-2 domain protein; COGs: COG0542 ATPase with chaperone activity ATP-binding subunit; InterProIPR003593:IPR018368:IPR001270:IPR004176:IPR 003959:IPR001943:IPR013093:IPR019489; KEGG: tte:TTE2327 ATPase with chaperone activity, ATP-binding subunit; PFAM: ATPase AAA-2 domain protein; Clp domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; Clp ATPase-like; SMART: AAA ATPase; SPTR: ATPases with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; ATPase family associat [...] | ATP-dependent proteinase; 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. | 0.823 |
| codY | hslU | Toce_1090 | Toce_1089 | GTP-sensing pleiotropic transcriptional repressor CodY; DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor; Belongs to the CodY family. | Heat shock protein HslVU, ATPase subunit HslU; 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. | 0.944 |
| codY | hslV | Toce_1090 | Toce_1088 | GTP-sensing pleiotropic transcriptional repressor CodY; DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor; Belongs to the CodY family. | ATP dependent peptidase CodWX, CodW component; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.796 |
| codY | xerC | Toce_1090 | Toce_1087 | GTP-sensing pleiotropic transcriptional repressor CodY; DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase. It is a GTP-binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor; Belongs to the CodY family. | Tyrosine recombinase XerC; Site-specific tyrosine recombinase, which acts by catalyzing the cutting and rejoining of the recombining DNA molecules. The XerC- XerD complex is essential to convert dimers of the bacterial chromosome into monomers to permit their segregation at cell division. It also contributes to the segregational stability of plasmids. | 0.626 |
| dnaJ | Toce_0907 | Toce_0910 | Toce_0907 | 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 [...] | COGs: COG0459 Chaperonin GroEL (HSP60 family); InterPro IPR002194:IPR017998:IPR002423; KEGG: pth:PTH_0876 chaperonin GroEL; PFAM: chaperonin Cpn60/TCP-1; SPTR: Chaperonin Cpn60/TCP-1; PFAM: TCP-1/cpn60 chaperonin family. | 0.960 |
| dnaJ | Toce_2123 | Toce_0910 | Toce_2123 | 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 [...] | ATPase AAA-2 domain protein; COGs: COG0542 ATPase with chaperone activity ATP-binding subunit; InterProIPR003593:IPR018368:IPR001270:IPR004176:IPR 003959:IPR001943:IPR013093:IPR019489; KEGG: tte:TTE2327 ATPase with chaperone activity, ATP-binding subunit; PFAM: ATPase AAA-2 domain protein; Clp domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; Clp ATPase-like; SMART: AAA ATPase; SPTR: ATPases with chaperone activity, ATP-binding subunit; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; Clp amino terminal domain; ATPase family associat [...] | 0.950 |