| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| SO_2964 | clpA | SO_2964 | SO_2626 | Lambda phage head maturation protease. | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | 0.854 |
| SO_2964 | clpB | SO_2964 | SO_3577 | Lambda phage head maturation protease. | Stress-induced multi-chaperone system component ClpB; 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). Belongs to [...] | 0.860 |
| SO_2964 | clpP | SO_2964 | SO_1794 | Lambda phage head maturation protease. | ATP-dependent Clp protease proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.927 |
| SO_2964 | clpS | SO_2964 | SO_2627 | Lambda phage head maturation protease. | ATP-dependent Clp protease adaptor protein ClpS; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. | 0.742 |
| SO_2964 | clpX | SO_2964 | SO_1795 | Lambda phage head maturation protease. | ATP-dependent Clp protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.993 |
| aat | clpA | SO_2623 | SO_2626 | leucyl/phenylalanyl-tRNA--protein transferase Aat; Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl- tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine. | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | 0.552 |
| aat | clpS | SO_2623 | SO_2627 | leucyl/phenylalanyl-tRNA--protein transferase Aat; Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl- tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine. | ATP-dependent Clp protease adaptor protein ClpS; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. | 0.859 |
| aat | infA | SO_2623 | SO_2625 | leucyl/phenylalanyl-tRNA--protein transferase Aat; Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl- tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine. | Translation initiation factor IF-1 InfA; One of the essential components for the initiation of protein synthesis. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initiation complex. | 0.745 |
| clpA | SO_2964 | SO_2626 | SO_2964 | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | Lambda phage head maturation protease. | 0.854 |
| clpA | aat | SO_2626 | SO_2623 | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | leucyl/phenylalanyl-tRNA--protein transferase Aat; Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl- tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine. | 0.552 |
| clpA | clpP | SO_2626 | SO_1794 | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.961 |
| clpA | clpS | SO_2626 | SO_2627 | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease adaptor protein ClpS; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. | 0.993 |
| clpA | clpX | SO_2626 | SO_1795 | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | ATP-dependent Clp protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.923 |
| clpB | SO_2964 | SO_3577 | SO_2964 | Stress-induced multi-chaperone system component ClpB; 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). Belongs to [...] | Lambda phage head maturation protease. | 0.860 |
| clpB | clpP | SO_3577 | SO_1794 | Stress-induced multi-chaperone system component ClpB; 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). Belongs to [...] | ATP-dependent Clp protease proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | 0.915 |
| clpB | clpS | SO_3577 | SO_2627 | Stress-induced multi-chaperone system component ClpB; 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). Belongs to [...] | ATP-dependent Clp protease adaptor protein ClpS; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. | 0.906 |
| clpB | clpX | SO_3577 | SO_1795 | Stress-induced multi-chaperone system component ClpB; 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). Belongs to [...] | ATP-dependent Clp protease ATP-binding subunit ClpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.668 |
| clpP | SO_2964 | SO_1794 | SO_2964 | ATP-dependent Clp protease proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Lambda phage head maturation protease. | 0.927 |
| clpP | clpA | SO_1794 | SO_2626 | ATP-dependent Clp protease proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | 0.961 |
| clpP | clpB | SO_1794 | SO_3577 | ATP-dependent Clp protease proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. | Stress-induced multi-chaperone system component ClpB; 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). Belongs to [...] | 0.915 |
