| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| argB | hslU | TOL2_C24580 | TOL2_C24590 | ArgB: acetylglutamate kinase; Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate; Belongs to the acetylglutamate kinase family. ArgB subfamily. | 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. | 0.828 |
| argB | hslV | TOL2_C24580 | TOL2_C24600 | ArgB: acetylglutamate kinase; Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate; Belongs to the acetylglutamate kinase family. ArgB subfamily. | HslV: ATP-dependent protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.791 |
| argB | xerC2 | TOL2_C24580 | TOL2_C24610 | ArgB: acetylglutamate kinase; Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate; Belongs to the acetylglutamate kinase family. ArgB subfamily. | XerC2: tyrosine recombinase, subunit C; 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 |
| clpX | dnaJ | TOL2_C04380 | TOL2_C37060 | ClpX: ATP-dependent Clp protease, ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 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, [...] | 0.438 |
| clpX | groL | TOL2_C04380 | TOL2_C13490 | ClpX: ATP-dependent Clp protease, ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | GroL: 60kDa chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.688 |
| clpX | groS | TOL2_C04380 | TOL2_C13480 | ClpX: ATP-dependent Clp protease, ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | GroS: 10kDa chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.596 |
| clpX | grpE | TOL2_C04380 | TOL2_C03490 | ClpX: ATP-dependent Clp protease, ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 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 [...] | 0.495 |
| clpX | hslU | TOL2_C04380 | TOL2_C24590 | ClpX: ATP-dependent Clp protease, ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 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. | 0.716 |
| clpX | hslV | TOL2_C04380 | TOL2_C24600 | ClpX: ATP-dependent Clp protease, ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | HslV: ATP-dependent protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.694 |
| clpX | htpG | TOL2_C04380 | TOL2_C43050 | ClpX: ATP-dependent Clp protease, ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | HtpG: chaperone protein; Molecular chaperone. Has ATPase activity. | 0.451 |
| dnaJ | clpX | TOL2_C37060 | TOL2_C04380 | 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, [...] | ClpX: ATP-dependent Clp protease, ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.438 |
| 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 | groS | TOL2_C37060 | TOL2_C13480 | 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, [...] | GroS: 10kDa chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.862 |
| 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 | hslV | TOL2_C37060 | TOL2_C24600 | 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, [...] | HslV: ATP-dependent protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.917 |
| 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 |
| fsxA | grpE | TOL2_C30050 | TOL2_C03490 | FxsA: predicted cytoplasmic membrane protein; Signal peptide. | 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 [...] | 0.460 |
| fsxA | hslU | TOL2_C30050 | TOL2_C24590 | FxsA: predicted cytoplasmic membrane protein; Signal peptide. | 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. | 0.558 |
| fsxA | hslV | TOL2_C30050 | TOL2_C24600 | FxsA: predicted cytoplasmic membrane protein; Signal peptide. | HslV: ATP-dependent protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.737 |
