node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
ClpA | ClpP | TTE2327 | TTE0625 | ATPases with chaperone activity, ATP-binding subunit; Best Blastp hit = gi|10172715|dbj|BAB03822.1| (AP001507) class III stress response-related ATPase [Bacillus halodurans], score 973, E-value 0; Belongs to the ClpA/ClpB family. | Protease subunit of ATP-dependent Clp proteases; 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. | 0.960 |
ClpA | DnaJ | TTE2327 | TTE0956 | ATPases with chaperone activity, ATP-binding subunit; Best Blastp hit = gi|10172715|dbj|BAB03822.1| (AP001507) class III stress response-related ATPase [Bacillus halodurans], score 973, E-value 0; Belongs to the ClpA/ClpB family. | Molecular chaperones (contain C-terminal Zn finger domain); 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-de [...] | 0.960 |
ClpA | DnaK | TTE2327 | TTE0955 | ATPases with chaperone activity, ATP-binding subunit; Best Blastp hit = gi|10172715|dbj|BAB03822.1| (AP001507) class III stress response-related ATPase [Bacillus halodurans], score 973, E-value 0; Belongs to the ClpA/ClpB family. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.980 |
ClpA | GroL | TTE2327 | TTE0580 | ATPases with chaperone activity, ATP-binding subunit; Best Blastp hit = gi|10172715|dbj|BAB03822.1| (AP001507) class III stress response-related ATPase [Bacillus halodurans], score 973, E-value 0; Belongs to the ClpA/ClpB family. | Chaperonin GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.815 |
ClpA | GroS | TTE2327 | TTE0579 | ATPases with chaperone activity, ATP-binding subunit; Best Blastp hit = gi|10172715|dbj|BAB03822.1| (AP001507) class III stress response-related ATPase [Bacillus halodurans], score 973, E-value 0; Belongs to the ClpA/ClpB family. | Co-chaperonin GroES (HSP10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.816 |
ClpA | GrpE | TTE2327 | TTE0954 | ATPases with chaperone activity, ATP-binding subunit; Best Blastp hit = gi|10172715|dbj|BAB03822.1| (AP001507) class III stress response-related ATPase [Bacillus halodurans], score 973, E-value 0; Belongs to the ClpA/ClpB family. | Molecular chaperone GrpE (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. [...] | 0.955 |
ClpA | HrcA | TTE2327 | TTE0953 | ATPases with chaperone activity, ATP-binding subunit; Best Blastp hit = gi|10172715|dbj|BAB03822.1| (AP001507) class III stress response-related ATPase [Bacillus halodurans], score 973, E-value 0; Belongs to the ClpA/ClpB family. | Transcriptional regulator of heat shock gene; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.841 |
ClpA | TTE1799 | TTE2327 | TTE1799 | ATPases with chaperone activity, ATP-binding subunit; Best Blastp hit = gi|10172715|dbj|BAB03822.1| (AP001507) class III stress response-related ATPase [Bacillus halodurans], score 973, E-value 0; Belongs to the ClpA/ClpB family. | Hypothetical protein. | 0.453 |
ClpP | ClpA | TTE0625 | TTE2327 | Protease subunit of ATP-dependent Clp proteases; 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. | ATPases with chaperone activity, ATP-binding subunit; Best Blastp hit = gi|10172715|dbj|BAB03822.1| (AP001507) class III stress response-related ATPase [Bacillus halodurans], score 973, E-value 0; Belongs to the ClpA/ClpB family. | 0.960 |
ClpP | DnaJ | TTE0625 | TTE0956 | Protease subunit of ATP-dependent Clp proteases; 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. | Molecular chaperones (contain C-terminal Zn finger domain); 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-de [...] | 0.642 |
ClpP | DnaK | TTE0625 | TTE0955 | Protease subunit of ATP-dependent Clp proteases; 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. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.864 |
ClpP | GroL | TTE0625 | TTE0580 | Protease subunit of ATP-dependent Clp proteases; 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. | Chaperonin GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.815 |
ClpP | GroS | TTE0625 | TTE0579 | Protease subunit of ATP-dependent Clp proteases; 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. | Co-chaperonin GroES (HSP10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.833 |
ClpP | GrpE | TTE0625 | TTE0954 | Protease subunit of ATP-dependent Clp proteases; 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. | Molecular chaperone GrpE (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. [...] | 0.821 |
ClpP | HrcA | TTE0625 | TTE0953 | Protease subunit of ATP-dependent Clp proteases; 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. | Transcriptional regulator of heat shock gene; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.883 |
DnaJ | ClpA | TTE0956 | TTE2327 | Molecular chaperones (contain C-terminal Zn finger domain); 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-de [...] | ATPases with chaperone activity, ATP-binding subunit; Best Blastp hit = gi|10172715|dbj|BAB03822.1| (AP001507) class III stress response-related ATPase [Bacillus halodurans], score 973, E-value 0; Belongs to the ClpA/ClpB family. | 0.960 |
DnaJ | ClpP | TTE0956 | TTE0625 | Molecular chaperones (contain C-terminal Zn finger domain); 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-de [...] | Protease subunit of ATP-dependent Clp proteases; 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. | 0.642 |
DnaJ | DnaK | TTE0956 | TTE0955 | Molecular chaperones (contain C-terminal Zn finger domain); 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-de [...] | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
DnaJ | GroL | TTE0956 | TTE0580 | Molecular chaperones (contain C-terminal Zn finger domain); 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-de [...] | Chaperonin GroEL (HSP60 family); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.968 |
DnaJ | GroS | TTE0956 | TTE0579 | Molecular chaperones (contain C-terminal Zn finger domain); 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-de [...] | Co-chaperonin GroES (HSP10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.897 |