| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| clpE | clpP | BSU13700 | BSU34540 | ATP-dependent Clp protease (class III stress gene); ATPase essential both for efficient CtsR-dependent gene derepression during heat stress and for rerepression. Together with ClpP, degrades the global regulator CtsR after heat shock. Is also involved in disaggregation of heat-denatured proteins. Has thus a role in overall protein quality control in response to heat stress. | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | 0.999 |
| clpE | clpY | BSU13700 | BSU16160 | ATP-dependent Clp protease (class III stress gene); ATPase essential both for efficient CtsR-dependent gene derepression during heat stress and for rerepression. Together with ClpP, degrades the global regulator CtsR after heat shock. Is also involved in disaggregation of heat-denatured proteins. Has thus a role in overall protein quality control in response to heat stress. | Two-component ATP-dependent protease (ATPase and chaperone); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity; Belongs to the ClpX chaperone family. HslU subfamily. | 0.900 |
| clpE | dnaJ | BSU13700 | BSU25460 | ATP-dependent Clp protease (class III stress gene); ATPase essential both for efficient CtsR-dependent gene derepression during heat stress and for rerepression. Together with ClpP, degrades the global regulator CtsR after heat shock. Is also involved in disaggregation of heat-denatured proteins. Has thus a role in overall protein quality control in response to heat stress. | Co-factor of molecular chaperone; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent interactions betwe [...] | 0.874 |
| clpE | dnaK | BSU13700 | BSU25470 | ATP-dependent Clp protease (class III stress gene); ATPase essential both for efficient CtsR-dependent gene derepression during heat stress and for rerepression. Together with ClpP, degrades the global regulator CtsR after heat shock. Is also involved in disaggregation of heat-denatured proteins. Has thus a role in overall protein quality control in response to heat stress. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.988 |
| clpE | groEL | BSU13700 | BSU06030 | ATP-dependent Clp protease (class III stress gene); ATPase essential both for efficient CtsR-dependent gene derepression during heat stress and for rerepression. Together with ClpP, degrades the global regulator CtsR after heat shock. Is also involved in disaggregation of heat-denatured proteins. Has thus a role in overall protein quality control in response to heat stress. | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.942 |
| clpE | groES | BSU13700 | BSU06020 | ATP-dependent Clp protease (class III stress gene); ATPase essential both for efficient CtsR-dependent gene derepression during heat stress and for rerepression. Together with ClpP, degrades the global regulator CtsR after heat shock. Is also involved in disaggregation of heat-denatured proteins. Has thus a role in overall protein quality control in response to heat stress. | Chaperonin small subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.961 |
| clpE | grpE | BSU13700 | BSU25480 | ATP-dependent Clp protease (class III stress gene); ATPase essential both for efficient CtsR-dependent gene derepression during heat stress and for rerepression. Together with ClpP, degrades the global regulator CtsR after heat shock. Is also involved in disaggregation of heat-denatured proteins. Has thus a role in overall protein quality control in response to heat stress. | Nucleotide exchange factor for DnaK activity; 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. S [...] | 0.947 |
| clpE | hrcA | BSU13700 | BSU25490 | ATP-dependent Clp protease (class III stress gene); ATPase essential both for efficient CtsR-dependent gene derepression during heat stress and for rerepression. Together with ClpP, degrades the global regulator CtsR after heat shock. Is also involved in disaggregation of heat-denatured proteins. Has thus a role in overall protein quality control in response to heat stress. | Transcriptional regulator of heat-shock genes; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.946 |
| clpE | htpG | BSU13700 | BSU39820 | ATP-dependent Clp protease (class III stress gene); ATPase essential both for efficient CtsR-dependent gene derepression during heat stress and for rerepression. Together with ClpP, degrades the global regulator CtsR after heat shock. Is also involved in disaggregation of heat-denatured proteins. Has thus a role in overall protein quality control in response to heat stress. | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.797 |
| clpP | clpE | BSU34540 | BSU13700 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | ATP-dependent Clp protease (class III stress gene); ATPase essential both for efficient CtsR-dependent gene derepression during heat stress and for rerepression. Together with ClpP, degrades the global regulator CtsR after heat shock. Is also involved in disaggregation of heat-denatured proteins. Has thus a role in overall protein quality control in response to heat stress. | 0.999 |
| clpP | clpY | BSU34540 | BSU16160 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | Two-component ATP-dependent protease (ATPase and chaperone); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity; Belongs to the ClpX chaperone family. HslU subfamily. | 0.984 |
| clpP | dnaJ | BSU34540 | BSU25460 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | Co-factor of molecular chaperone; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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-dependent interactions betwe [...] | 0.840 |
| clpP | dnaK | BSU34540 | BSU25470 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.982 |
| clpP | groEL | BSU34540 | BSU06030 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.972 |
| clpP | groES | BSU34540 | BSU06020 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | Chaperonin small subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter; Belongs to the GroES chaperonin family. | 0.924 |
| clpP | grpE | BSU34540 | BSU25480 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | Nucleotide exchange factor for DnaK activity; 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. S [...] | 0.947 |
| clpP | hrcA | BSU34540 | BSU25490 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | Transcriptional regulator of heat-shock genes; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.973 |
| clpP | htpG | BSU34540 | BSU39820 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.679 |
| clpP | tig | BSU34540 | BSU28230 | ATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a limited peptidase activity in the absence of ATP-binding subunits ClpC, ClpE or ClpX. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity). ClpXP is involved in the complete degradation of the site-2 clipped anti-sigma-W factor RsiW. This results in the release of SigW and the transcriptional activation of genes under the control of the sigma-W factor. Probably the major protease that degrades prot [...] | Prolyl isomerase (trigger factor); 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 (By similarity). Belongs to the FKBP-type PPIase family. Tig subfamily. | 0.727 |
| clpY | clpE | BSU16160 | BSU13700 | Two-component ATP-dependent protease (ATPase and chaperone); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity; Belongs to the ClpX chaperone family. HslU subfamily. | ATP-dependent Clp protease (class III stress gene); ATPase essential both for efficient CtsR-dependent gene derepression during heat stress and for rerepression. Together with ClpP, degrades the global regulator CtsR after heat shock. Is also involved in disaggregation of heat-denatured proteins. Has thus a role in overall protein quality control in response to heat stress. | 0.900 |
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