node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
acuC | htpG | BSU29710 | BSU39820 | Protein deacetylase; Role in growth and sporulation on acetoin or butanediol. Involved in the breakdown of these compounds used as a carbon source; Belongs to the histone deacetylase family. | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.846 |
clpQ | clpY | BSU16150 | BSU16160 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | 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. | 0.999 |
clpQ | dnaJ | BSU16150 | BSU25460 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | 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 [...] | 0.761 |
clpQ | dnaK | BSU16150 | BSU25470 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.884 |
clpQ | groEL | BSU16150 | BSU06030 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.904 |
clpQ | groES | BSU16150 | BSU06020 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | 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. | 0.897 |
clpQ | grpE | BSU16150 | BSU25480 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | 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 [...] | 0.928 |
clpQ | htpG | BSU16150 | BSU39820 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.963 |
clpQ | rtpA | BSU16150 | BSU02530 | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | anti-TRAP regulator; By forming a complex with tryptophan-activated TRAP, and masking its RNA binding site, it inhibits TRAP's RNA binding ability, thereby abolishing TRAP regulation of gene expression, leading to antitermination and increased trp operon expression. AT acts by competing with messenger RNA for the RNA binding domain of TRAP. | 0.582 |
clpY | clpQ | BSU16160 | BSU16150 | 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. | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | 0.999 |
clpY | dnaJ | BSU16160 | BSU25460 | 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. | 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 [...] | 0.882 |
clpY | dnaK | BSU16160 | BSU25470 | 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. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.927 |
clpY | groEL | BSU16160 | BSU06030 | 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. | Chaperonin large subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.938 |
clpY | groES | BSU16160 | BSU06020 | 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. | 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. | 0.949 |
clpY | grpE | BSU16160 | BSU25480 | 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. | 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 [...] | 0.959 |
clpY | htpG | BSU16160 | BSU39820 | 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. | Class III heat-shock protein (molecular chaperone); Molecular chaperone. Has ATPase activity. | 0.962 |
clpY | rtpA | BSU16160 | BSU02530 | 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. | anti-TRAP regulator; By forming a complex with tryptophan-activated TRAP, and masking its RNA binding site, it inhibits TRAP's RNA binding ability, thereby abolishing TRAP regulation of gene expression, leading to antitermination and increased trp operon expression. AT acts by competing with messenger RNA for the RNA binding domain of TRAP. | 0.727 |
dnaJ | clpQ | BSU25460 | BSU16150 | 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 [...] | Two-component ATP-dependent protease (N-terminal serine protease); Protease subunit of a proteasome-like degradation complex. Belongs to the peptidase T1B family. HslV subfamily. | 0.761 |
dnaJ | clpY | BSU25460 | BSU16160 | 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 [...] | 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. | 0.882 |
dnaJ | dnaK | BSU25460 | BSU25470 | 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 [...] | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |