node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
clpA | clpP | STM0945 | STM0448 | Similar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 97% identity in aa 1 - 758; Belongs to the ClpA/ClpB family. | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. | 0.989 |
clpA | clpX | STM0945 | STM0449 | Similar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 97% identity in aa 1 - 758; Belongs to the ClpA/ClpB family. | Specificity component of clpA-clpP ATP-dependent serine protease, chaperone; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.932 |
clpA | dnaK | STM0945 | STM0012 | Similar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 97% identity in aa 1 - 758; Belongs to the ClpA/ClpB family. | Chaperone Hsp70; Acts as a chaperone. | 0.835 |
clpA | grpE | STM0945 | STM2681 | Similar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 97% identity in aa 1 - 758; Belongs to the ClpA/ClpB family. | Molecular chaparone; 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-depe [...] | 0.741 |
clpA | htpG | STM0945 | STM0487 | Similar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 97% identity in aa 1 - 758; Belongs to the ClpA/ClpB family. | Chaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity. | 0.671 |
clpA | ibpA | STM0945 | STM3809 | Similar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 97% identity in aa 1 - 758; Belongs to the ClpA/ClpB family. | Small heat shock protein; Associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. | 0.697 |
clpA | ibpB | STM0945 | STM3808 | Similar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 97% identity in aa 1 - 758; Belongs to the ClpA/ClpB family. | Small heat shock protein; Associates with aggregated proteins, together with IbpA, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. | 0.748 |
clpA | mopA | STM0945 | STM4330 | Similar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 97% identity in aa 1 - 758; Belongs to the ClpA/ClpB family. | Chaperone Hsp60 with peptide-dependent ATPase activity; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.666 |
clpA | rpoS | STM0945 | STM2924 | Similar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 97% identity in aa 1 - 758; Belongs to the ClpA/ClpB family. | Sigma S (sigma 38) 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 the master transcriptional regulator of the stationary phase and the general stress response. | 0.525 |
clpB | clpP | STM2660 | STM0448 | 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 [...] | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. | 0.976 |
clpB | clpX | STM2660 | STM0449 | 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 [...] | Specificity component of clpA-clpP ATP-dependent serine protease, chaperone; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. | 0.932 |
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 | grpE | STM2660 | STM2681 | 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 [...] | Molecular chaparone; 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-depe [...] | 0.975 |
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. | 0.978 |
clpB | ibpA | STM2660 | STM3809 | 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 [...] | Small heat shock protein; Associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. | 0.922 |
clpB | ibpB | STM2660 | STM3808 | 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 [...] | Small heat shock protein; Associates with aggregated proteins, together with IbpA, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. | 0.912 |
clpB | mopA | STM2660 | STM4330 | 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 Hsp60 with peptide-dependent ATPase activity; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.984 |
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. | 0.748 |
clpB | rpoS | STM2660 | STM2924 | 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 S (sigma 38) 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 the master transcriptional regulator of the stationary phase and the general stress response. | 0.524 |
clpP | clpA | STM0448 | STM0945 | Proteolytic subunit of clpA-clpP ATP-dependent serine protease; 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. | Similar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 97% identity in aa 1 - 758; Belongs to the ClpA/ClpB family. | 0.989 |