| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| CCK82162.1 | CCK82165.1 | TOL2_C40070 | TOL2_C40100 | Heat shock protein, Hsp 20 family; Belongs to the small heat shock protein (HSP20) family. | Histidinol-phosphate phosphatase family protein. | 0.633 |
| CCK82162.1 | grpE | TOL2_C40070 | TOL2_C03490 | Heat shock protein, Hsp 20 family; Belongs to the small heat shock protein (HSP20) family. | GrpE: HSP70 cofactor; 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-dep [...] | 0.507 |
| CCK82162.1 | hslU | TOL2_C40070 | TOL2_C24590 | Heat shock protein, Hsp 20 family; Belongs to the small heat shock protein (HSP20) family. | HslU: ATP-dependent hsl 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. | 0.448 |
| CCK82162.1 | htpG | TOL2_C40070 | TOL2_C43050 | Heat shock protein, Hsp 20 family; Belongs to the small heat shock protein (HSP20) family. | HtpG: chaperone protein; Molecular chaperone. Has ATPase activity. | 0.526 |
| CCK82162.1 | lonA5 | TOL2_C40070 | TOL2_C40080 | Heat shock protein, Hsp 20 family; Belongs to the small heat shock protein (HSP20) family. | Lon5: ATP-dependent protease La; 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. | 0.805 |
| CCK82162.1 | recD2 | TOL2_C40070 | TOL2_C40110 | Heat shock protein, Hsp 20 family; Belongs to the small heat shock protein (HSP20) family. | RecD2: helicase, RecD/TraA family; DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase. Has no activity on blunt DNA or DNA with 3'-overhangs, requires at least 10 bases of 5'-ssDNA for helicase activity; Belongs to the RecD family. RecD-like subfamily. | 0.620 |
| CCK82162.1 | rlpA | TOL2_C40070 | TOL2_C40090 | Heat shock protein, Hsp 20 family; Belongs to the small heat shock protein (HSP20) family. | RlpA: rare lipoprotein A; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. | 0.561 |
| CCK82165.1 | CCK82162.1 | TOL2_C40100 | TOL2_C40070 | Histidinol-phosphate phosphatase family protein. | Heat shock protein, Hsp 20 family; Belongs to the small heat shock protein (HSP20) family. | 0.633 |
| CCK82165.1 | lonA5 | TOL2_C40100 | TOL2_C40080 | Histidinol-phosphate phosphatase family protein. | Lon5: ATP-dependent protease La; 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. | 0.731 |
| CCK82165.1 | recD2 | TOL2_C40100 | TOL2_C40110 | Histidinol-phosphate phosphatase family protein. | RecD2: helicase, RecD/TraA family; DNA-dependent ATPase and ATP-dependent 5'-3' DNA helicase. Has no activity on blunt DNA or DNA with 3'-overhangs, requires at least 10 bases of 5'-ssDNA for helicase activity; Belongs to the RecD family. RecD-like subfamily. | 0.836 |
| CCK82165.1 | rlpA | TOL2_C40100 | TOL2_C40090 | Histidinol-phosphate phosphatase family protein. | RlpA: rare lipoprotein A; Lytic transglycosylase with a strong preference for naked glycan strands that lack stem peptides. | 0.798 |
| dnaJ | ftsH | TOL2_C37060 | TOL2_C39270 | DnaJ: chaperone protein; 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, [...] | FtsH: cell division protease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | 0.667 |
| dnaJ | groL | TOL2_C37060 | TOL2_C13490 | DnaJ: chaperone protein; 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, [...] | GroL: 60kDa chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.952 |
| dnaJ | grpE | TOL2_C37060 | TOL2_C03490 | DnaJ: chaperone protein; 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, [...] | GrpE: HSP70 cofactor; 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-dep [...] | 0.987 |
| dnaJ | hslU | TOL2_C37060 | TOL2_C24590 | DnaJ: chaperone protein; 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, [...] | HslU: ATP-dependent hsl 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. | 0.934 |
| dnaJ | htpG | TOL2_C37060 | TOL2_C43050 | DnaJ: chaperone protein; 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, [...] | HtpG: chaperone protein; Molecular chaperone. Has ATPase activity. | 0.964 |
| dnaJ | lonA5 | TOL2_C37060 | TOL2_C40080 | DnaJ: chaperone protein; 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, [...] | Lon5: ATP-dependent protease La; 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. | 0.641 |
| ftsH | dnaJ | TOL2_C39270 | TOL2_C37060 | FtsH: cell division protease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | DnaJ: chaperone protein; 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, [...] | 0.667 |
| ftsH | groL | TOL2_C39270 | TOL2_C13490 | FtsH: cell division protease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | GroL: 60kDa chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.671 |
| ftsH | grpE | TOL2_C39270 | TOL2_C03490 | FtsH: cell division protease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. | GrpE: HSP70 cofactor; 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-dep [...] | 0.625 |
