| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| clpB | clpX | SAOUHSC_00912 | SAOUHSC_01778 | ATP-dependent Clp protease, ATP-binding subunit 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; 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. | 0.708 |
| clpB | ctsR | SAOUHSC_00912 | SAOUHSC_00502 | ATP-dependent Clp protease, ATP-binding subunit 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; Belongs to the ClpA/ClpB family. | Conserved hypothetical protein; Negative regulator of clpC, clpB and clpP transcription by binding directly and specifically to their promoter region. | 0.716 |
| clpB | dnaK | SAOUHSC_00912 | SAOUHSC_01683 | ATP-dependent Clp protease, ATP-binding subunit 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; Belongs to the ClpA/ClpB family. | DNAk protein, putative; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.960 |
| clpB | groL | SAOUHSC_00912 | SAOUHSC_02254 | ATP-dependent Clp protease, ATP-binding subunit 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; Belongs to the ClpA/ClpB family. | Chaperonin, 60 kDa, GrpEL, putative; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.774 |
| clpB | groS | SAOUHSC_00912 | SAOUHSC_02255 | ATP-dependent Clp protease, ATP-binding subunit 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; Belongs to the ClpA/ClpB family. | Chaperonin, 10 kDa, GroES, putative; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.757 |
| clpB | grpE | SAOUHSC_00912 | SAOUHSC_01684 | ATP-dependent Clp protease, ATP-binding subunit 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; Belongs to the ClpA/ClpB family. | Co-chaperone 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-depend [...] | 0.863 |
| clpB | hrcA | SAOUHSC_00912 | SAOUHSC_01685 | ATP-dependent Clp protease, ATP-binding subunit 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; Belongs to the ClpA/ClpB family. | Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.575 |
| clpB | mcsA | SAOUHSC_00912 | SAOUHSC_00503 | ATP-dependent Clp protease, ATP-binding subunit 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; Belongs to the ClpA/ClpB family. | UvrB/uvrC motif domain protein; Activates the phosphorylation activity of the protein- arginine kinase McsB (By similarity). May function as an important molecule for oxidative tolerance in various types of stress including that of heavy metals. Binds to Cu(2+), Zn(2+), Co(2+) and Cd(2+) via its CXXC metal binding motifs. | 0.648 |
| clpB | mcsB | SAOUHSC_00912 | SAOUHSC_00504 | ATP-dependent Clp protease, ATP-binding subunit 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; Belongs to the ClpA/ClpB family. | ATP:guanido phosphotransferase, C-terminal catalytic domain protein; Catalyzes the specific phosphorylation of arginine residues in proteins (By similarity). Is required for stress tolerance and virulence in S.aureus. Acts as a modulator of the repressor activity of CtsR upon heavy metal and oxidative stress caused by these metal ions. | 0.806 |
| clpC | clpX | SAOUHSC_00505 | SAOUHSC_01778 | Endopeptidase, putative; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. | 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. | 0.731 |
| clpC | ctsR | SAOUHSC_00505 | SAOUHSC_00502 | Endopeptidase, putative; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. | Conserved hypothetical protein; Negative regulator of clpC, clpB and clpP transcription by binding directly and specifically to their promoter region. | 0.945 |
| clpC | dnaK | SAOUHSC_00505 | SAOUHSC_01683 | Endopeptidase, putative; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. | DNAk protein, putative; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.945 |
| clpC | groL | SAOUHSC_00505 | SAOUHSC_02254 | Endopeptidase, putative; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. | Chaperonin, 60 kDa, GrpEL, putative; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.739 |
| clpC | groS | SAOUHSC_00505 | SAOUHSC_02255 | Endopeptidase, putative; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. | Chaperonin, 10 kDa, GroES, putative; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.800 |
| clpC | grpE | SAOUHSC_00505 | SAOUHSC_01684 | Endopeptidase, putative; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. | Co-chaperone 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-depend [...] | 0.834 |
| clpC | hrcA | SAOUHSC_00505 | SAOUHSC_01685 | Endopeptidase, putative; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. | Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.645 |
| clpC | mcsA | SAOUHSC_00505 | SAOUHSC_00503 | Endopeptidase, putative; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. | UvrB/uvrC motif domain protein; Activates the phosphorylation activity of the protein- arginine kinase McsB (By similarity). May function as an important molecule for oxidative tolerance in various types of stress including that of heavy metals. Binds to Cu(2+), Zn(2+), Co(2+) and Cd(2+) via its CXXC metal binding motifs. | 0.962 |
| clpC | mcsB | SAOUHSC_00505 | SAOUHSC_00504 | Endopeptidase, putative; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. | ATP:guanido phosphotransferase, C-terminal catalytic domain protein; Catalyzes the specific phosphorylation of arginine residues in proteins (By similarity). Is required for stress tolerance and virulence in S.aureus. Acts as a modulator of the repressor activity of CtsR upon heavy metal and oxidative stress caused by these metal ions. | 0.983 |
| clpX | clpB | SAOUHSC_01778 | SAOUHSC_00912 | 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 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; Belongs to the ClpA/ClpB family. | 0.708 |
| clpX | clpC | SAOUHSC_01778 | SAOUHSC_00505 | 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. | Endopeptidase, putative; Required for growth at high temperatures, probably by acting as a chaperone during heat shock and targeting heat-denatured proteins for degradation by ClpP. Required for biofilm formation. May act as a chaperone regulating CtsR activity. | 0.731 |
