| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ADP14874.1 | msrP | AXYL_01536 | AXYL_01537 | IndB protein. | Oxidoreductase molybdopterin binding domain protein 3; 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-stereospecific, being [...] | 0.487 |
| ADP14874.1 | msrQ | AXYL_01536 | AXYL_01538 | IndB protein. | Ferric reductase like transmembrane component family protein; 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 red [...] | 0.557 |
| ADP14874.1 | rluC | AXYL_01536 | AXYL_01535 | IndB protein. | Ribosomal large subunit pseudouridine synthase C; Responsible for synthesis of pseudouridine from uracil. Belongs to the pseudouridine synthase RluA family. | 0.886 |
| ADP18485.1 | moaE | AXYL_05185 | AXYL_05183 | Molybdenum cofactor synthesis domain protein; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | Molybdopterin-converting factor subunit 2. | 0.976 |
| ADP18485.1 | msrP | AXYL_05185 | AXYL_01537 | Molybdenum cofactor synthesis domain protein; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | Oxidoreductase molybdopterin binding domain protein 3; 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-stereospecific, being [...] | 0.410 |
| coxB | msrP | AXYL_00215 | AXYL_01537 | Cytochrome c oxidase, subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Oxidoreductase molybdopterin binding domain protein 3; 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-stereospecific, being [...] | 0.427 |
| moaE | ADP18485.1 | AXYL_05183 | AXYL_05185 | Molybdopterin-converting factor subunit 2. | Molybdenum cofactor synthesis domain protein; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | 0.976 |
| moaE | msrP | AXYL_05183 | AXYL_01537 | Molybdopterin-converting factor subunit 2. | Oxidoreductase molybdopterin binding domain protein 3; 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-stereospecific, being [...] | 0.415 |
| msrP | ADP14874.1 | AXYL_01537 | AXYL_01536 | Oxidoreductase molybdopterin binding domain protein 3; 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-stereospecific, being [...] | IndB protein. | 0.487 |
| msrP | ADP18485.1 | AXYL_01537 | AXYL_05185 | Oxidoreductase molybdopterin binding domain protein 3; 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-stereospecific, being [...] | Molybdenum cofactor synthesis domain protein; Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. Belongs to the MoeA family. | 0.410 |
| msrP | coxB | AXYL_01537 | AXYL_00215 | Oxidoreductase molybdopterin binding domain protein 3; 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-stereospecific, being [...] | Cytochrome c oxidase, subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.427 |
| msrP | moaE | AXYL_01537 | AXYL_05183 | Oxidoreductase molybdopterin binding domain protein 3; 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-stereospecific, being [...] | Molybdopterin-converting factor subunit 2. | 0.415 |
| msrP | msrQ | AXYL_01537 | AXYL_01538 | Oxidoreductase molybdopterin binding domain protein 3; 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-stereospecific, being [...] | Ferric reductase like transmembrane component family protein; 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 red [...] | 0.994 |
| msrP | rluC | AXYL_01537 | AXYL_01535 | Oxidoreductase molybdopterin binding domain protein 3; 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-stereospecific, being [...] | Ribosomal large subunit pseudouridine synthase C; Responsible for synthesis of pseudouridine from uracil. Belongs to the pseudouridine synthase RluA family. | 0.481 |
| msrQ | ADP14874.1 | AXYL_01538 | AXYL_01536 | Ferric reductase like transmembrane component family protein; 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 red [...] | IndB protein. | 0.557 |
| msrQ | msrP | AXYL_01538 | AXYL_01537 | Ferric reductase like transmembrane component family protein; 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 red [...] | Oxidoreductase molybdopterin binding domain protein 3; 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-stereospecific, being [...] | 0.994 |
| msrQ | rluC | AXYL_01538 | AXYL_01535 | Ferric reductase like transmembrane component family protein; 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 red [...] | Ribosomal large subunit pseudouridine synthase C; Responsible for synthesis of pseudouridine from uracil. Belongs to the pseudouridine synthase RluA family. | 0.547 |
| rluC | ADP14874.1 | AXYL_01535 | AXYL_01536 | Ribosomal large subunit pseudouridine synthase C; Responsible for synthesis of pseudouridine from uracil. Belongs to the pseudouridine synthase RluA family. | IndB protein. | 0.886 |
| rluC | msrP | AXYL_01535 | AXYL_01537 | Ribosomal large subunit pseudouridine synthase C; Responsible for synthesis of pseudouridine from uracil. Belongs to the pseudouridine synthase RluA family. | Oxidoreductase molybdopterin binding domain protein 3; 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-stereospecific, being [...] | 0.481 |
| rluC | msrQ | AXYL_01535 | AXYL_01538 | Ribosomal large subunit pseudouridine synthase C; Responsible for synthesis of pseudouridine from uracil. Belongs to the pseudouridine synthase RluA family. | Ferric reductase like transmembrane component family protein; 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 red [...] | 0.547 |
