| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| SERP1235 | clpX | SERP1235 | SERP1238 | hemX protein; Identified by similarity to EGAD:15411; match to protein family HMM PF01578. | 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. | 0.738 |
| SERP1235 | engB | SERP1235 | SERP1237 | hemX protein; Identified by similarity to EGAD:15411; match to protein family HMM PF01578. | GTP-binding protein, EngB family; Necessary for normal cell division and for the maintenance of normal septation; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngB GTPase family. | 0.784 |
| SERP1235 | hemA | SERP1235 | SERP1236 | hemX protein; Identified by similarity to EGAD:15411; match to protein family HMM PF01578. | glutamyl-tRNA reductase; Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). | 0.934 |
| SERP1235 | hemB | SERP1235 | SERP1232 | hemX protein; Identified by similarity to EGAD:15411; match to protein family HMM PF01578. | Delta-aminolevulinic acid dehydratase; Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen (By similarity). | 0.881 |
| SERP1235 | hemC | SERP1235 | SERP1234 | hemX protein; Identified by similarity to EGAD:15411; match to protein family HMM PF01578. | Porphobilinogen deaminase; Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. Belongs to the HMBS family. | 0.918 |
| atpD | clpX | SERP1709 | SERP1238 | ATP synthase F1, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains 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. | 0.748 |
| clpC | clpP | SERP0165 | SERP0436 | ATP-dependent Clp protease, ATP-binding subunit ClpC; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. | 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. | 0.981 |
| clpC | clpX | SERP0165 | SERP1238 | ATP-dependent Clp protease, ATP-binding subunit ClpC; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. | 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. | 0.772 |
| clpC | groES | SERP0165 | SERP1485 | ATP-dependent Clp protease, ATP-binding subunit ClpC; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.802 |
| clpC | grpE | SERP0165 | SERP1149 | ATP-dependent Clp protease, ATP-binding subunit ClpC; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. | Heat shock protein 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 of ATP- [...] | 0.823 |
| clpP | clpC | SERP0436 | SERP0165 | 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, ATP-binding subunit ClpC; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. | 0.981 |
| clpP | clpX | SERP0436 | SERP1238 | 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, 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 |
| clpP | groES | SERP0436 | SERP1485 | 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. | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.745 |
| clpP | grpE | SERP0436 | SERP1149 | 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. | Heat shock protein 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 of ATP- [...] | 0.687 |
| clpX | SERP1235 | SERP1238 | SERP1235 | 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. | hemX protein; Identified by similarity to EGAD:15411; match to protein family HMM PF01578. | 0.738 |
| clpX | atpD | SERP1238 | SERP1709 | 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. | ATP synthase F1, beta subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits; Belongs to the ATPase alpha/beta chains family. | 0.748 |
| clpX | clpC | SERP1238 | SERP0165 | 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. | ATP-dependent Clp protease, ATP-binding subunit ClpC; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. | 0.772 |
| clpX | clpP | SERP1238 | SERP0436 | 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. | 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. | 0.993 |
| clpX | engB | SERP1238 | SERP1237 | 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. | GTP-binding protein, EngB family; Necessary for normal cell division and for the maintenance of normal septation; Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. EngB GTPase family. | 0.819 |
| clpX | groES | SERP1238 | SERP1485 | 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. | Chaperonin, 10 kDa; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.717 |