| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ALO65684.1 | ALO67981.1 | AS189_03225 | AS189_17675 | NDP-hexose 4-ketoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | Molecular chaperone HtpG; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.759 |
| ALO65684.1 | dnaJ | AS189_03225 | AS189_10625 | NDP-hexose 4-ketoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | Molecular chaperone 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, [...] | 0.696 |
| ALO65684.1 | dnaK | AS189_03225 | AS189_01625 | NDP-hexose 4-ketoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | Molecular chaperone GrpE; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.952 |
| ALO65684.1 | groEL | AS189_03225 | AS189_05645 | NDP-hexose 4-ketoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.544 |
| ALO65684.1 | groEL-2 | AS189_03225 | AS189_17970 | NDP-hexose 4-ketoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.551 |
| ALO65684.1 | groS | AS189_03225 | AS189_05640 | NDP-hexose 4-ketoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.717 |
| ALO65684.1 | gyrB | AS189_03225 | AS189_02510 | NDP-hexose 4-ketoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | DNA topoisomerase IV subunit B; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner. | 0.435 |
| ALO66873.1 | dnaJ | AS189_10630 | AS189_10625 | 16S rRNA methyltransferase; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | Molecular chaperone 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, [...] | 0.935 |
| ALO66873.1 | hrcA | AS189_10630 | AS189_10620 | 16S rRNA methyltransferase; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | HrcA family transcriptional regulator; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. | 0.824 |
| ALO67981.1 | ALO65684.1 | AS189_17675 | AS189_03225 | Molecular chaperone HtpG; Derived by automated computational analysis using gene prediction method: Protein Homology. | NDP-hexose 4-ketoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | 0.759 |
| ALO67981.1 | dnaJ | AS189_17675 | AS189_10625 | Molecular chaperone HtpG; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone 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, [...] | 0.935 |
| ALO67981.1 | dnaK | AS189_17675 | AS189_01625 | Molecular chaperone HtpG; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GrpE; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.996 |
| ALO67981.1 | groEL | AS189_17675 | AS189_05645 | Molecular chaperone HtpG; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.822 |
| ALO67981.1 | groEL-2 | AS189_17675 | AS189_17970 | Molecular chaperone HtpG; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.822 |
| ALO67981.1 | groS | AS189_17675 | AS189_05640 | Molecular chaperone HtpG; Derived by automated computational analysis using gene prediction method: Protein Homology. | Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | 0.830 |
| dnaJ | ALO65684.1 | AS189_10625 | AS189_03225 | Molecular chaperone 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, [...] | NDP-hexose 4-ketoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ClpA/ClpB family. | 0.696 |
| dnaJ | ALO66873.1 | AS189_10625 | AS189_10630 | Molecular chaperone 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, [...] | 16S rRNA methyltransferase; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit. | 0.935 |
| dnaJ | ALO67981.1 | AS189_10625 | AS189_17675 | Molecular chaperone 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, [...] | Molecular chaperone HtpG; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.935 |
| dnaJ | dnaK | AS189_10625 | AS189_01625 | Molecular chaperone 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, [...] | Molecular chaperone GrpE; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.995 |
| dnaJ | groEL | AS189_10625 | AS189_05645 | Molecular chaperone 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, [...] | Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.731 |
