| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ANB07546.1 | ANB07547.1 | SAM40697_3588 | SAM40697_3589 | Fe-S oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.748 |
| ANB07546.1 | dnaJ-2 | SAM40697_3588 | SAM40697_3592 | Fe-S oxidoreductase; 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, [...] | 0.700 |
| ANB07546.1 | dnaK | SAM40697_3588 | SAM40697_3590 | Fe-S oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Fe-S protein assembly chaperone HscA; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.694 |
| ANB07546.1 | grpE | SAM40697_3588 | SAM40697_3591 | Fe-S oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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 [...] | 0.694 |
| ANB07546.1 | hspR | SAM40697_3588 | SAM40697_3593 | Fe-S oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat-shock protein HspR; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.720 |
| ANB07547.1 | ANB07546.1 | SAM40697_3589 | SAM40697_3588 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Fe-S oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.748 |
| ANB07547.1 | dnaJ-2 | SAM40697_3589 | SAM40697_3592 | Hypothetical protein; 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, [...] | 0.760 |
| ANB07547.1 | dnaK | SAM40697_3589 | SAM40697_3590 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Fe-S protein assembly chaperone HscA; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.806 |
| ANB07547.1 | grpE | SAM40697_3589 | SAM40697_3591 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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 [...] | 0.783 |
| ANB07547.1 | hspR | SAM40697_3589 | SAM40697_3593 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Heat-shock protein HspR; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.752 |
| ANB07547.1 | murD | SAM40697_3589 | SAM40697_1981 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | UDP-N-acetylmuramoylalanine--D-glutamate ligase; Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). Belongs to the MurCDEF family. | 0.784 |
| ANB07547.1 | murE | SAM40697_3589 | SAM40697_1984 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | UDP-N-acetylmuramoylalanyl-D-glutamate--2, 6-diaminopimelate ligase; Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Belongs to the MurCDEF family. MurE subfamily. | 0.592 |
| ANB07547.1 | murF | SAM40697_3589 | SAM40697_1983 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D- alanine ligase; Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein; Belongs to the MurCDEF family. MurF subfamily. | 0.783 |
| ANB07547.1 | murG | SAM40697_3589 | SAM40697_1979 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase; Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc- (pentapeptide)GlcNAc (lipid intermediate II); Belongs to the glycosyltransferase 28 family. MurG subfamily. | 0.625 |
| ANB07547.1 | wecA | SAM40697_3589 | SAM40697_4630 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Transferase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.733 |
| dnaJ-2 | ANB07546.1 | SAM40697_3592 | SAM40697_3588 | 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, [...] | Fe-S oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.700 |
| dnaJ-2 | ANB07547.1 | SAM40697_3592 | SAM40697_3589 | 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, [...] | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.760 |
| dnaJ-2 | dnaK | SAM40697_3592 | SAM40697_3590 | 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, [...] | Fe-S protein assembly chaperone HscA; Acts as a chaperone; Belongs to the heat shock protein 70 family. | 0.999 |
| dnaJ-2 | grpE | SAM40697_3592 | SAM40697_3591 | 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; 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 [...] | 0.997 |
| dnaJ-2 | hspR | SAM40697_3592 | SAM40697_3593 | 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, [...] | Heat-shock protein HspR; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.971 |