| 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 | 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 |
| SO_2964 | fadB | SO_2964 | SO_0021 | Lambda phage head maturation protease. | Aerobic fatty oxidation complex 3-hydroxyacyl-CoA epimerase alpha subunit FadB; Involved in the aerobic and anaerobic degradation of long- chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family. | 0.897 |
| SO_2964 | fadJ | SO_2964 | SO_3088 | Lambda phage head maturation protease. | Anaerobic fatty oxidation complex alpha subunit FadJ; Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3- hydroxyacyl-CoA dehydrogenase activities; In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family. | 0.910 |
| SO_2964 | groES | SO_2964 | SO_0703 | Lambda phage head maturation protease. | 10 kDa chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.704 |
| SO_2964 | hslV | SO_2964 | SO_4162 | Lambda phage head maturation protease. | HlsVU protease peptidase component HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.513 |
| SO_2964 | lon | SO_2964 | SO_1796 | Lambda phage head maturation protease. | ATP-dependent protease La Lon; 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. | 0.697 |
| SO_2964 | tig | SO_2964 | SO_1793 | Lambda phage head maturation protease. | Trigger factor peptidyl-prolyl cis-trans isomerase Tig; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.404 |
| 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 | 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 | 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 |
| clpA | groES | SO_2626 | SO_0703 | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | 10 kDa chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.670 |
| clpA | hslV | SO_2626 | SO_4162 | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | HlsVU protease peptidase component HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. | 0.571 |
| clpA | lon | SO_2626 | SO_1796 | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | ATP-dependent protease La Lon; 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. | 0.715 |
| clpA | tig | SO_2626 | SO_1793 | ATP-dependent Clp protease ATPase and specificity subunit ClpA; Belongs to the ClpA/ClpB family. | Trigger factor peptidyl-prolyl cis-trans isomerase Tig; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.441 |
| 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 | 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 |