node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AFL74589.1 | AFL75151.1 | Thivi_2669 | Thivi_3277 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. | 0.939 |
AFL74589.1 | clpP | Thivi_2669 | Thivi_0628 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | ATP-dependent Clp protease, proteolytic subunit ClpP; 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. | 0.528 |
AFL74589.1 | dnaK | Thivi_2669 | Thivi_4597 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.939 |
AFL74589.1 | grpE | Thivi_2669 | Thivi_4596 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | 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. [...] | 0.885 |
AFL74589.1 | hrcA | Thivi_2669 | Thivi_4595 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.685 |
AFL74972.1 | AFL75151.1 | Thivi_3092 | Thivi_3277 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DnaJ C terminal region. | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. | 0.941 |
AFL74972.1 | clpP | Thivi_3092 | Thivi_0628 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DnaJ C terminal region. | ATP-dependent Clp protease, proteolytic subunit ClpP; 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. | 0.533 |
AFL74972.1 | dnaK | Thivi_3092 | Thivi_4597 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DnaJ C terminal region. | Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.988 |
AFL74972.1 | grpE | Thivi_3092 | Thivi_4596 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DnaJ C terminal region. | 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. [...] | 0.949 |
AFL74972.1 | hrcA | Thivi_3092 | Thivi_4595 | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DnaJ C terminal region. | Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.689 |
AFL75151.1 | AFL74589.1 | Thivi_3277 | Thivi_2669 | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain. | 0.939 |
AFL75151.1 | AFL74972.1 | Thivi_3277 | Thivi_3092 | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. | DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DnaJ C terminal region. | 0.941 |
AFL75151.1 | AFL76114.1 | Thivi_3277 | Thivi_4301 | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. | DNA segregation ATPase, FtsK/SpoIIIE family; PFAM: Ftsk gamma domain; DnaJ domain. | 0.941 |
AFL75151.1 | birA | Thivi_3277 | Thivi_0684 | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. | birA, biotin-(acetyl-CoA-carboxylase) ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. | 0.424 |
AFL75151.1 | clpP | Thivi_3277 | Thivi_0628 | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. | ATP-dependent Clp protease, proteolytic subunit ClpP; 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. | 0.766 |
AFL75151.1 | dnaJ | Thivi_3277 | Thivi_4598 | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. | Chaperone protein DnaJ; 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, D [...] | 0.984 |
AFL75151.1 | grpE | Thivi_3277 | Thivi_4596 | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 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. [...] | 0.977 |
AFL75151.1 | hrcA | Thivi_3277 | Thivi_4595 | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. | Heat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.872 |
AFL76114.1 | AFL75151.1 | Thivi_4301 | Thivi_3277 | DNA segregation ATPase, FtsK/SpoIIIE family; PFAM: Ftsk gamma domain; DnaJ domain. | Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family. | 0.941 |
AFL76114.1 | clpP | Thivi_4301 | Thivi_0628 | DNA segregation ATPase, FtsK/SpoIIIE family; PFAM: Ftsk gamma domain; DnaJ domain. | ATP-dependent Clp protease, proteolytic subunit ClpP; 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. | 0.533 |