| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| VV0714 | VVA0294 | VV93_v1c06500 | VV93_v1c32820 | annotation not available | Catalase; Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide; Belongs to the catalase family | 0.511 |
| VV0714 | VVA1042 | VV93_v1c06500 | VV93_v1c39840 | annotation not available | annotation not available | 0.493 |
| VV0714 | bamD | VV93_v1c06500 | VV93_v1c06480 | annotation not available | Outer membrane protein assembly factor BamD; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane | 0.701 |
| VV0714 | clpB | VV93_v1c06500 | VV93_v1c06510 | annotation not available | Chaperone protein ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity); Belongs to the ClpA/ClpB family | 0.680 |
| VV0714 | ftsZ | VV93_v1c06500 | VV93_v1c05610 | annotation not available | Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity | 0.775 |
| VV0714 | kefB | VV93_v1c06500 | VV93_v1c27710 | annotation not available | Glutathione-regulated potassium-efflux system protein KefB; Pore-forming subunit of a potassium efflux system that confers protection against electrophiles. Catalyzes K(+)/H(+) antiport | 0.482 |
| VV0714 | metH | VV93_v1c06500 | VV93_v1c26820 | annotation not available | Methionine synthase; Catalyzes the transfer of a methyl group from methyl- cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate (By similarity) | 0.619 |
| VV0714 | nnrD | VV93_v1c06500 | VV93_v1c41110 | annotation not available | Multifunctional fusion protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration; Belongs to the NnrD/CARKD family | 0.532 |
| VV0714 | polA | VV93_v1c06500 | VV93_v1c01730 | annotation not available | DNA polymerase I; In addition to polymerase activity, this DNA polymerase exhibits 5’-3’ exonuclease activity | 0.604 |
| VV0714 | rluD | VV93_v1c06500 | VV93_v1c06490 | annotation not available | Pseudouridine synthase; Responsible for synthesis of pseudouridine from uracil | 0.968 |
| VVA0294 | VV0714 | VV93_v1c32820 | VV93_v1c06500 | Catalase; Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide; Belongs to the catalase family | annotation not available | 0.511 |
| VVA0294 | nnrD | VV93_v1c32820 | VV93_v1c41110 | Catalase; Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide; Belongs to the catalase family | Multifunctional fusion protein; Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration; Belongs to the NnrD/CARKD family | 0.528 |
| VVA1042 | VV0714 | VV93_v1c39840 | VV93_v1c06500 | annotation not available | annotation not available | 0.493 |
| bamD | VV0714 | VV93_v1c06480 | VV93_v1c06500 | Outer membrane protein assembly factor BamD; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane | annotation not available | 0.701 |
| bamD | clpB | VV93_v1c06480 | VV93_v1c06510 | Outer membrane protein assembly factor BamD; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane | Chaperone protein ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity); Belongs to the ClpA/ClpB family | 0.571 |
| bamD | rluD | VV93_v1c06480 | VV93_v1c06490 | Outer membrane protein assembly factor BamD; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane | Pseudouridine synthase; Responsible for synthesis of pseudouridine from uracil | 0.710 |
| clpB | VV0714 | VV93_v1c06510 | VV93_v1c06500 | Chaperone protein ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity); Belongs to the ClpA/ClpB family | annotation not available | 0.680 |
| clpB | bamD | VV93_v1c06510 | VV93_v1c06480 | Chaperone protein ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity); Belongs to the ClpA/ClpB family | Outer membrane protein assembly factor BamD; Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane | 0.571 |
| clpB | rluD | VV93_v1c06510 | VV93_v1c06490 | Chaperone protein ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein aggregates by DnaK (By similarity); Belongs to the ClpA/ClpB family | Pseudouridine synthase; Responsible for synthesis of pseudouridine from uracil | 0.730 |
| ftsZ | VV0714 | VV93_v1c05610 | VV93_v1c06500 | Cell division protein FtsZ; Essential cell division protein that forms a contractile ring structure (Z ring) at the future cell division site. The regulation of the ring assembly controls the timing and the location of cell division. One of the functions of the FtsZ ring is to recruit other cell division proteins to the septum to produce a new cell wall between the dividing cells. Binds GTP and shows GTPase activity | annotation not available | 0.775 |
