| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| BirA | DnaK | PTH_0255 | PTH_0878 | biotin-(acetyl-CoA carboxylase) ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor; Belongs to the biotin--protein ligase family. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.551 |
| BirA | GrpE | PTH_0255 | PTH_0877 | biotin-(acetyl-CoA carboxylase) ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor; Belongs to the biotin--protein ligase family. | Molecular chaperone 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 of ATP [...] | 0.417 |
| BirA | HrcA | PTH_0255 | PTH_0875 | biotin-(acetyl-CoA carboxylase) ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor; Belongs to the biotin--protein ligase 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. | 0.528 |
| BirA | LepA | PTH_0255 | PTH_0873 | biotin-(acetyl-CoA carboxylase) ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor; Belongs to the biotin--protein ligase family. | Membrane GTPase LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner. | 0.520 |
| BirA | PTH_0881 | PTH_0255 | PTH_0881 | biotin-(acetyl-CoA carboxylase) ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor; Belongs to the biotin--protein ligase family. | Uncharacterized protein conserved in bacteria; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | 0.511 |
| CbpA | DnaK | PTH_2123 | PTH_0878 | DnaJ-class molecular chaperone. | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.995 |
| CbpA | GroL | PTH_2123 | PTH_0876 | DnaJ-class molecular chaperone. | Chaperonin GroEL; HSP60 family. | 0.740 |
| CbpA | GrpE | PTH_2123 | PTH_0877 | DnaJ-class molecular chaperone. | Molecular chaperone 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 of ATP [...] | 0.970 |
| CbpA | HrcA | PTH_2123 | PTH_0875 | DnaJ-class molecular chaperone. | 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. | 0.661 |
| CbpA | PTH_0881 | PTH_2123 | PTH_0881 | DnaJ-class molecular chaperone. | Uncharacterized protein conserved in bacteria; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | 0.481 |
| CbpA | PrmA | PTH_2123 | PTH_0880 | DnaJ-class molecular chaperone. | Ribosomal protein L11 methylase; Methylates ribosomal protein L11; Belongs to the methyltransferase superfamily. PrmA family. | 0.735 |
| DnaJ | DnaK | PTH_0879 | PTH_0878 | DnaJ-class 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 between [...] | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.998 |
| DnaJ | GroL | PTH_0879 | PTH_0876 | DnaJ-class 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 between [...] | Chaperonin GroEL; HSP60 family. | 0.834 |
| DnaJ | GrpE | PTH_0879 | PTH_0877 | DnaJ-class 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 between [...] | Molecular chaperone 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 of ATP [...] | 0.994 |
| DnaJ | HrcA | PTH_0879 | PTH_0875 | DnaJ-class 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 between [...] | 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. | 0.825 |
| DnaJ | PTH_0881 | PTH_0879 | PTH_0881 | DnaJ-class 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 between [...] | Uncharacterized protein conserved in bacteria; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | 0.832 |
| DnaJ | PrmA | PTH_0879 | PTH_0880 | DnaJ-class 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 between [...] | Ribosomal protein L11 methylase; Methylates ribosomal protein L11; Belongs to the methyltransferase superfamily. PrmA family. | 0.947 |
| DnaK | BirA | PTH_0878 | PTH_0255 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | biotin-(acetyl-CoA carboxylase) ligase; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a repressor; Belongs to the biotin--protein ligase family. | 0.551 |
| DnaK | CbpA | PTH_0878 | PTH_2123 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | DnaJ-class molecular chaperone. | 0.995 |
| DnaK | DnaJ | PTH_0878 | PTH_0879 | Molecular chaperone; Acts as a chaperone; Belongs to the heat shock protein 70 family. | DnaJ-class 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 between [...] | 0.998 |
