| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| HA50_19040 | HA50_19045 | HA50_19040 | HA50_19045 | Intracellular growth attenuator protein igaA; Derived by automated computational analysis using gene prediction method: Protein Homology. | GMP/IMP nucleotidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.698 |
| HA50_19040 | HA50_19050 | HA50_19040 | HA50_19050 | Intracellular growth attenuator protein igaA; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | 0.661 |
| HA50_19040 | hslO | HA50_19040 | HA50_19055 | Intracellular growth attenuator protein igaA; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hsp33 family molecular chaperone; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.671 |
| HA50_19045 | HA50_19040 | HA50_19045 | HA50_19040 | GMP/IMP nucleotidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Intracellular growth attenuator protein igaA; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.698 |
| HA50_19045 | HA50_19050 | HA50_19045 | HA50_19050 | GMP/IMP nucleotidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | 0.913 |
| HA50_19045 | hslO | HA50_19045 | HA50_19055 | GMP/IMP nucleotidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hsp33 family molecular chaperone; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.746 |
| HA50_19050 | HA50_19040 | HA50_19050 | HA50_19040 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | Intracellular growth attenuator protein igaA; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.661 |
| HA50_19050 | HA50_19045 | HA50_19050 | HA50_19045 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | GMP/IMP nucleotidase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.913 |
| HA50_19050 | dnaJ | HA50_19050 | HA50_03240 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | Molecular chaperone 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, [...] | 0.666 |
| HA50_19050 | dnaK | HA50_19050 | HA50_03235 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.583 |
| HA50_19050 | grpE | HA50_19050 | HA50_14725 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | Nucleotide exchange factor 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 [...] | 0.654 |
| HA50_19050 | hslO | HA50_19050 | HA50_19055 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | Hsp33 family molecular chaperone; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.944 |
| HA50_19050 | hslU | HA50_19050 | HA50_19895 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | HslU--HslV peptidase ATPase 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. | 0.657 |
| HA50_19050 | hslV | HA50_19050 | HA50_19890 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.706 |
| HA50_19050 | htpG | HA50_19050 | HA50_04900 | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity. | 0.474 |
| dnaJ | HA50_19050 | HA50_03240 | HA50_19050 | Molecular chaperone 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, [...] | Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HSP15 family. | 0.666 |
| dnaJ | dnaK | HA50_03240 | HA50_03235 | Molecular chaperone 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, [...] | Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | grpE | HA50_03240 | HA50_14725 | Molecular chaperone 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, [...] | Nucleotide exchange factor 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 [...] | 0.990 |
| dnaJ | hslO | HA50_03240 | HA50_19055 | Molecular chaperone 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, [...] | Hsp33 family molecular chaperone; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.720 |
| dnaJ | hslU | HA50_03240 | HA50_19895 | Molecular chaperone 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, [...] | HslU--HslV peptidase ATPase 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. | 0.871 |