| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| DM42_6469 | msrQ | DM42_6469 | DM42_1437 | annotation not available | Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the [...] | 0.536 |
| WI67_05965 | msrQ | DM42_496 | DM42_1437 | annotation not available | Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the [...] | 0.589 |
| WL94_04790 | msrQ | DM42_6977 | DM42_1437 | annotation not available | Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the [...] | 0.450 |
| WL94_15710 | ccsB | DM42_1440 | DM42_1439 | annotation not available | cytochr_II_ccsB- cytochrome c-type biogenesis protein CcsB | 0.988 |
| WL94_15710 | msrP | DM42_1440 | DM42_1438 | annotation not available | Protein-methionine-sulfoxide reductase catalytic subunit MsrP; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecifi [...] | 0.616 |
| WL94_15710 | msrQ | DM42_1440 | DM42_1437 | annotation not available | Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the [...] | 0.593 |
| ccsB | WL94_15710 | DM42_1439 | DM42_1440 | cytochr_II_ccsB- cytochrome c-type biogenesis protein CcsB | annotation not available | 0.988 |
| ccsB | msrP | DM42_1439 | DM42_1438 | cytochr_II_ccsB- cytochrome c-type biogenesis protein CcsB | Protein-methionine-sulfoxide reductase catalytic subunit MsrP; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecifi [...] | 0.618 |
| ccsB | msrQ | DM42_1439 | DM42_1437 | cytochr_II_ccsB- cytochrome c-type biogenesis protein CcsB | Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the [...] | 0.595 |
| msrP | WL94_15710 | DM42_1438 | DM42_1440 | Protein-methionine-sulfoxide reductase catalytic subunit MsrP; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecifi [...] | annotation not available | 0.616 |
| msrP | ccsB | DM42_1438 | DM42_1439 | Protein-methionine-sulfoxide reductase catalytic subunit MsrP; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecifi [...] | cytochr_II_ccsB- cytochrome c-type biogenesis protein CcsB | 0.618 |
| msrP | msrQ | DM42_1438 | DM42_1437 | Protein-methionine-sulfoxide reductase catalytic subunit MsrP; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecifi [...] | Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the [...] | 0.982 |
| msrQ | DM42_6469 | DM42_1437 | DM42_6469 | Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the [...] | annotation not available | 0.536 |
| msrQ | WI67_05965 | DM42_1437 | DM42_496 | Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the [...] | annotation not available | 0.589 |
| msrQ | WL94_04790 | DM42_1437 | DM42_6977 | Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the [...] | annotation not available | 0.450 |
| msrQ | WL94_15710 | DM42_1437 | DM42_1440 | Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the [...] | annotation not available | 0.593 |
| msrQ | ccsB | DM42_1437 | DM42_1439 | Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the [...] | cytochr_II_ccsB- cytochrome c-type biogenesis protein CcsB | 0.595 |
| msrQ | msrP | DM42_1437 | DM42_1438 | Protein-methionine-sulfoxide reductase heme-binding subunit MsrQ; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. MsrQ provides electrons for reduction to the [...] | Protein-methionine-sulfoxide reductase catalytic subunit MsrP; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecifi [...] | 0.982 |
