| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| clpB | dnaJ1 | DIP2104 | DIP2118 | Putative ATP-dependent protease regulatory 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. 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). Belong [...] | Chaperone protein cofactor 1; 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 D [...] | 0.685 |
| clpB | dnaJ2 | DIP2104 | DIP1720 | Putative ATP-dependent protease regulatory 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. 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). Belong [...] | Chaperone protein 2; 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 [...] | 0.669 |
| clpB | dnaK | DIP2104 | DIP2120 | Putative ATP-dependent protease regulatory 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. 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). Belong [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.978 |
| clpB | groEL1 | DIP2104 | DIP0576 | Putative ATP-dependent protease regulatory 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. 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). Belong [...] | 60 kDa chaperonin 1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.619 |
| clpB | groEL2 | DIP2104 | DIP2020 | Putative ATP-dependent protease regulatory 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. 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). Belong [...] | Chaperonin GroEL2; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.529 |
| clpB | groES | DIP2104 | DIP0575 | Putative ATP-dependent protease regulatory 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. 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). Belong [...] | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.811 |
| clpB | grpE | DIP2104 | DIP2119 | Putative ATP-dependent protease regulatory 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. 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). Belong [...] | Chaperone protein cofactor 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 [...] | 0.915 |
| clpB | hrcA | DIP2104 | DIP1721 | Putative ATP-dependent protease regulatory 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. 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). Belong [...] | Putative heat-inducible transcription repressor; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.469 |
| clpB | hspR | DIP2104 | DIP2117 | Putative ATP-dependent protease regulatory 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. 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). Belong [...] | Putative chaperone locus transcriptional regulator, HspR; Similar to Streptomyces coelicolor putative heat shock protein HspR or SCH44.08c SW:HSPR_STRCO (P40183) (151 aa) fasta scores: E(): 5.4e-16, 52.59% id in 135 aa, and to Mycobacterium tuberculosis HspR or Rv0353 or MTCY13E10.13 TR:O06302 (EMBL:Z95324) (126 aa) fasta scores: E(): 6.6e-23, 66.66% id in 117 aa. | 0.635 |
| clpC | dnaJ1 | DIP1983 | DIP2118 | ATP-dependent Clp protease ATP-binding subunit; Similar to Bacillus subtilis negative regulator of genetic competence ClpC SW:CLPC_BACSU (P37571) (810 aa) fasta scores: E(): 2.6e-134, 58.11% id in 826 aa, and to Mycobacterium tuberculosis probable ATP-dependent Clp protease ATP-binding subunit Rv3596c SW:CLPC_MYCTU (O06286) (848 aa) fasta scores: E(): 1.7e-186, 81.81% id in 847 aa; Belongs to the ClpA/ClpB family. | Chaperone protein cofactor 1; 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 D [...] | 0.685 |
| clpC | dnaJ2 | DIP1983 | DIP1720 | ATP-dependent Clp protease ATP-binding subunit; Similar to Bacillus subtilis negative regulator of genetic competence ClpC SW:CLPC_BACSU (P37571) (810 aa) fasta scores: E(): 2.6e-134, 58.11% id in 826 aa, and to Mycobacterium tuberculosis probable ATP-dependent Clp protease ATP-binding subunit Rv3596c SW:CLPC_MYCTU (O06286) (848 aa) fasta scores: E(): 1.7e-186, 81.81% id in 847 aa; Belongs to the ClpA/ClpB family. | Chaperone protein 2; 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 [...] | 0.683 |
| clpC | dnaK | DIP1983 | DIP2120 | ATP-dependent Clp protease ATP-binding subunit; Similar to Bacillus subtilis negative regulator of genetic competence ClpC SW:CLPC_BACSU (P37571) (810 aa) fasta scores: E(): 2.6e-134, 58.11% id in 826 aa, and to Mycobacterium tuberculosis probable ATP-dependent Clp protease ATP-binding subunit Rv3596c SW:CLPC_MYCTU (O06286) (848 aa) fasta scores: E(): 1.7e-186, 81.81% id in 847 aa; Belongs to the ClpA/ClpB family. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.956 |
| clpC | groEL1 | DIP1983 | DIP0576 | ATP-dependent Clp protease ATP-binding subunit; Similar to Bacillus subtilis negative regulator of genetic competence ClpC SW:CLPC_BACSU (P37571) (810 aa) fasta scores: E(): 2.6e-134, 58.11% id in 826 aa, and to Mycobacterium tuberculosis probable ATP-dependent Clp protease ATP-binding subunit Rv3596c SW:CLPC_MYCTU (O06286) (848 aa) fasta scores: E(): 1.7e-186, 81.81% id in 847 aa; Belongs to the ClpA/ClpB family. | 60 kDa chaperonin 1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.633 |
| clpC | groEL2 | DIP1983 | DIP2020 | ATP-dependent Clp protease ATP-binding subunit; Similar to Bacillus subtilis negative regulator of genetic competence ClpC SW:CLPC_BACSU (P37571) (810 aa) fasta scores: E(): 2.6e-134, 58.11% id in 826 aa, and to Mycobacterium tuberculosis probable ATP-dependent Clp protease ATP-binding subunit Rv3596c SW:CLPC_MYCTU (O06286) (848 aa) fasta scores: E(): 1.7e-186, 81.81% id in 847 aa; Belongs to the ClpA/ClpB family. | Chaperonin GroEL2; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.538 |
| clpC | groES | DIP1983 | DIP0575 | ATP-dependent Clp protease ATP-binding subunit; Similar to Bacillus subtilis negative regulator of genetic competence ClpC SW:CLPC_BACSU (P37571) (810 aa) fasta scores: E(): 2.6e-134, 58.11% id in 826 aa, and to Mycobacterium tuberculosis probable ATP-dependent Clp protease ATP-binding subunit Rv3596c SW:CLPC_MYCTU (O06286) (848 aa) fasta scores: E(): 1.7e-186, 81.81% id in 847 aa; Belongs to the ClpA/ClpB family. | 10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.793 |
| clpC | grpE | DIP1983 | DIP2119 | ATP-dependent Clp protease ATP-binding subunit; Similar to Bacillus subtilis negative regulator of genetic competence ClpC SW:CLPC_BACSU (P37571) (810 aa) fasta scores: E(): 2.6e-134, 58.11% id in 826 aa, and to Mycobacterium tuberculosis probable ATP-dependent Clp protease ATP-binding subunit Rv3596c SW:CLPC_MYCTU (O06286) (848 aa) fasta scores: E(): 1.7e-186, 81.81% id in 847 aa; Belongs to the ClpA/ClpB family. | Chaperone protein cofactor 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 [...] | 0.894 |
| clpC | hrcA | DIP1983 | DIP1721 | ATP-dependent Clp protease ATP-binding subunit; Similar to Bacillus subtilis negative regulator of genetic competence ClpC SW:CLPC_BACSU (P37571) (810 aa) fasta scores: E(): 2.6e-134, 58.11% id in 826 aa, and to Mycobacterium tuberculosis probable ATP-dependent Clp protease ATP-binding subunit Rv3596c SW:CLPC_MYCTU (O06286) (848 aa) fasta scores: E(): 1.7e-186, 81.81% id in 847 aa; Belongs to the ClpA/ClpB family. | Putative heat-inducible transcription repressor; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.681 |
| dnaJ1 | clpB | DIP2118 | DIP2104 | Chaperone protein cofactor 1; 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 D [...] | Putative ATP-dependent protease regulatory 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. 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). Belong [...] | 0.685 |
| dnaJ1 | clpC | DIP2118 | DIP1983 | Chaperone protein cofactor 1; 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 D [...] | ATP-dependent Clp protease ATP-binding subunit; Similar to Bacillus subtilis negative regulator of genetic competence ClpC SW:CLPC_BACSU (P37571) (810 aa) fasta scores: E(): 2.6e-134, 58.11% id in 826 aa, and to Mycobacterium tuberculosis probable ATP-dependent Clp protease ATP-binding subunit Rv3596c SW:CLPC_MYCTU (O06286) (848 aa) fasta scores: E(): 1.7e-186, 81.81% id in 847 aa; Belongs to the ClpA/ClpB family. | 0.685 |
| dnaJ1 | dnaK | DIP2118 | DIP2120 | Chaperone protein cofactor 1; 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 D [...] | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |