| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| MVIS_0201 | napE | MVIS_0201 | MVIS_0198 | Putative exported protein. | Putative periplasmic nitrate reductase protein NapE. | 0.421 |
| MVIS_0201 | torA | MVIS_0201 | MVIS_0200 | Putative exported protein. | trimethylamine-N-oxide reductase precursor. | 0.496 |
| MVIS_0201 | yedY | MVIS_0201 | MVIS_0196 | Putative exported protein. | Sulfoxide reductase catalytic subunit yedY; 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 able to re [...] | 0.443 |
| MVIS_0201 | yedZ | MVIS_0201 | MVIS_0197 | Putative exported protein. | Sulfoxide reductase heme-binding subunit yedZ; 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 reductase catalyti [...] | 0.436 |
| MVIS_0520 | yedZ | MVIS_0520 | MVIS_0197 | Putative lipoprotein. | Sulfoxide reductase heme-binding subunit yedZ; 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 reductase catalyti [...] | 0.516 |
| MVIS_1327 | yedY | MVIS_1327 | MVIS_0196 | 5-hydroxyisourate hydrolase; Belongs to the transthyretin family. 5-hydroxyisourate hydrolase subfamily. | Sulfoxide reductase catalytic subunit yedY; 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 able to re [...] | 0.684 |
| MVIS_1327 | yedZ | MVIS_1327 | MVIS_0197 | 5-hydroxyisourate hydrolase; Belongs to the transthyretin family. 5-hydroxyisourate hydrolase subfamily. | Sulfoxide reductase heme-binding subunit yedZ; 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 reductase catalyti [...] | 0.835 |
| MVIS_2203 | MVIS_2205 | MVIS_2203 | MVIS_2205 | Putative uncharacterized protein. | Putative uncharacterized protein, DoxX family. | 0.985 |
| MVIS_2203 | yedZ | MVIS_2203 | MVIS_0197 | Putative uncharacterized protein. | Sulfoxide reductase heme-binding subunit yedZ; 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 reductase catalyti [...] | 0.494 |
| MVIS_2205 | MVIS_2203 | MVIS_2205 | MVIS_2203 | Putative uncharacterized protein, DoxX family. | Putative uncharacterized protein. | 0.985 |
| MVIS_2205 | MVIS_2647 | MVIS_2205 | MVIS_2647 | Putative uncharacterized protein, DoxX family. | Putative uncharacterized protein. | 0.933 |
| MVIS_2205 | yedZ | MVIS_2205 | MVIS_0197 | Putative uncharacterized protein, DoxX family. | Sulfoxide reductase heme-binding subunit yedZ; 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 reductase catalyti [...] | 0.584 |
| MVIS_2647 | MVIS_2205 | MVIS_2647 | MVIS_2205 | Putative uncharacterized protein. | Putative uncharacterized protein, DoxX family. | 0.933 |
| MVIS_2647 | yedZ | MVIS_2647 | MVIS_0197 | Putative uncharacterized protein. | Sulfoxide reductase heme-binding subunit yedZ; 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 reductase catalyti [...] | 0.494 |
| napE | MVIS_0201 | MVIS_0198 | MVIS_0201 | Putative periplasmic nitrate reductase protein NapE. | Putative exported protein. | 0.421 |
| napE | torA | MVIS_0198 | MVIS_0200 | Putative periplasmic nitrate reductase protein NapE. | trimethylamine-N-oxide reductase precursor. | 0.754 |
| napE | yedY | MVIS_0198 | MVIS_0196 | Putative periplasmic nitrate reductase protein NapE. | Sulfoxide reductase catalytic subunit yedY; 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 able to re [...] | 0.450 |
| napE | yedZ | MVIS_0198 | MVIS_0197 | Putative periplasmic nitrate reductase protein NapE. | Sulfoxide reductase heme-binding subunit yedZ; 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 reductase catalyti [...] | 0.450 |
| topB | yedY | MVIS_0195 | MVIS_0196 | DNA topoisomerase III; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA su [...] | Sulfoxide reductase catalytic subunit yedY; 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 able to re [...] | 0.581 |
| topB | yedZ | MVIS_0195 | MVIS_0197 | DNA topoisomerase III; Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA- (5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA su [...] | Sulfoxide reductase heme-binding subunit yedZ; 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 reductase catalyti [...] | 0.542 |