| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| STM2405 | prlC | STM2405 | STM3594 | Putative thiamine pyrophosphate enzymes; Similar to E. coli acetolactate synthase III, valine sensitive, large subunit (AAC73188.1); Blastp hit to AAC73188.1 (604 aa), 24% identity in aa 37 - 505. | Oligopeptidase A; May play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. Can cleave N-acetyl-L-Ala(4). | 0.511 |
| asd | prlC | STM3539 | STM3594 | Aspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family. | Oligopeptidase A; May play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. Can cleave N-acetyl-L-Ala(4). | 0.485 |
| clpB | dnaK | STM2660 | STM0012 | ATP-dependent protease; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Required for colonization of the gastroi [...] | Chaperone Hsp70; Acts as a chaperone. | 0.999 |
| clpB | hslU | STM2660 | STM4091 | ATP-dependent protease; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Required for colonization of the gastroi [...] | ATPase component of the 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. | 0.966 |
| clpB | htpG | STM2660 | STM0487 | ATP-dependent protease; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Required for colonization of the gastroi [...] | Chaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity. | 0.983 |
| clpB | prlC | STM2660 | STM3594 | ATP-dependent protease; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Required for colonization of the gastroi [...] | Oligopeptidase A; May play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. Can cleave N-acetyl-L-Ala(4). | 0.496 |
| clpB | rpoH | STM2660 | STM3568 | ATP-dependent protease; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Required for colonization of the gastroi [...] | Sigma H factor of RNA polymerase; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. | 0.734 |
| dnaK | clpB | STM0012 | STM2660 | Chaperone Hsp70; Acts as a chaperone. | ATP-dependent protease; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Required for colonization of the gastroi [...] | 0.999 |
| dnaK | hslU | STM0012 | STM4091 | Chaperone Hsp70; Acts as a chaperone. | ATPase component of the 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. | 0.958 |
| dnaK | htpG | STM0012 | STM0487 | Chaperone Hsp70; Acts as a chaperone. | Chaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity. | 0.998 |
| dnaK | prlC | STM0012 | STM3594 | Chaperone Hsp70; Acts as a chaperone. | Oligopeptidase A; May play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. Can cleave N-acetyl-L-Ala(4). | 0.475 |
| dnaK | rpoH | STM0012 | STM3568 | Chaperone Hsp70; Acts as a chaperone. | Sigma H factor of RNA polymerase; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. | 0.988 |
| gor | prlC | STM3597 | STM3594 | Similar to E. coli glutathione oxidoreductase (AAC76525.1); Blastp hit to AAC76525.1 (450 aa), 94% identity in aa 1 - 450. | Oligopeptidase A; May play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. Can cleave N-acetyl-L-Ala(4). | 0.467 |
| hslU | clpB | STM4091 | STM2660 | ATPase component of the 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. | ATP-dependent protease; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Required for colonization of the gastroi [...] | 0.966 |
| hslU | dnaK | STM4091 | STM0012 | ATPase component of the 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. | Chaperone Hsp70; Acts as a chaperone. | 0.958 |
| hslU | htpG | STM4091 | STM0487 | ATPase component of the 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. | Chaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity. | 0.985 |
| hslU | prlC | STM4091 | STM3594 | ATPase component of the 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. | Oligopeptidase A; May play a specific role in the degradation of signal peptides after they are released from precursor forms of secreted proteins. Can cleave N-acetyl-L-Ala(4). | 0.479 |
| htpG | clpB | STM0487 | STM2660 | Chaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity. | ATP-dependent protease; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity). Required for colonization of the gastroi [...] | 0.983 |
| htpG | dnaK | STM0487 | STM0012 | Chaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity. | Chaperone Hsp70; Acts as a chaperone. | 0.998 |
| htpG | hslU | STM0487 | STM4091 | Chaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity. | ATPase component of the 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. | 0.985 |
