| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| clpP | clpY | BL03605 | BL01277 | ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein); 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. ClpXP1 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 transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.733 |
| clpP | dnaJ | BL03605 | BL02098 | ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein); 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. ClpXP1 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 transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | Heat-shock protein; 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 between DnaJ, DnaK [...] | 0.520 |
| clpP | dnaK | BL03605 | BL02097 | ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein); 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. ClpXP1 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 transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | Class I heat-shock protein (molecular chaperone); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.802 |
| clpP | groEL | BL03605 | BL03283 | ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein); 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. ClpXP1 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 transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | Class I heat-shock protein (chaperonin); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.892 |
| clpP | groES | BL03605 | BL03284 | ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein); 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. ClpXP1 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 transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | Class I heat-shock protein (chaperonin); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.783 |
| clpP | grpE | BL03605 | BL02095 | ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein); 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. ClpXP1 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 transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | Heat-shock protein; 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-depen [...] | 0.716 |
| clpP | htpG | BL03605 | BL00247 | ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein); 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. ClpXP1 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 transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.516 |
| clpP | lonA | BL03605 | BL00621 | ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein); 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. ClpXP1 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 transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | Class III heat-shock ATP-dependent Lon protease; 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. | 0.503 |
| clpY | clpP | BL01277 | BL03605 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein); 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. ClpXP1 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 transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | 0.733 |
| clpY | dnaJ | BL01277 | BL02098 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Heat-shock protein; 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 between DnaJ, DnaK [...] | 0.789 |
| clpY | dnaK | BL01277 | BL02097 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Class I heat-shock protein (molecular chaperone); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.810 |
| clpY | groEL | BL01277 | BL03283 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Class I heat-shock protein (chaperonin); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.911 |
| clpY | groES | BL01277 | BL03284 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Class I heat-shock protein (chaperonin); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.865 |
| clpY | grpE | BL01277 | BL02095 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Heat-shock protein; 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-depen [...] | 0.924 |
| clpY | htpG | BL01277 | BL00247 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.869 |
| clpY | lonA | BL01277 | BL00621 | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | Class III heat-shock ATP-dependent Lon protease; 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. | 0.870 |
| dnaJ | clpP | BL02098 | BL03605 | Heat-shock protein; 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 between DnaJ, DnaK [...] | ATP-dependent Clp protease proteolytic subunit (class III heat-shock protein); 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. ClpXP1 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 transcription activation of the genes under the control of the sigma-W factor (By similarity); Belongs to the peptidase S14 family. | 0.520 |
| dnaJ | clpY | BL02098 | BL01277 | Heat-shock protein; 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 between DnaJ, DnaK [...] | Two-component ATP-dependent protease (N-terminal serine protease); ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. | 0.789 |
| dnaJ | dnaK | BL02098 | BL02097 | Heat-shock protein; 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 between DnaJ, DnaK [...] | Class I heat-shock protein (molecular chaperone); Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ | fusA | BL02098 | BL01057 | Heat-shock protein; 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 between DnaJ, DnaK [...] | Elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily. | 0.598 |
