| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| LP43_0828 | LP43_1212 | LP43_0828 | LP43_1212 | Cytochrome c family protein. | Methane monooxygenase component C. | 0.652 |
| LP43_0828 | LP43_1870 | LP43_0828 | LP43_1870 | Cytochrome c family protein. | Cytochrome c oxidase polypeptide 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). | 0.912 |
| LP43_0828 | LP43_2245 | LP43_0828 | LP43_2245 | Cytochrome c family protein. | Adenylylsulfate kinase; Catalyzes the synthesis of activated sulfate. | 0.813 |
| LP43_0828 | yedY | LP43_0828 | LP43_2022 | Cytochrome c family protein. | Putative sulfite oxidase 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 reduce [...] | 0.780 |
| LP43_0858 | LP43_1212 | LP43_0858 | LP43_1212 | Hypothetical protein. | Methane monooxygenase component C. | 0.956 |
| LP43_0858 | LP43_1870 | LP43_0858 | LP43_1870 | Hypothetical protein. | Cytochrome c oxidase polypeptide 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). | 0.887 |
| LP43_0858 | yedY | LP43_0858 | LP43_2022 | Hypothetical protein. | Putative sulfite oxidase 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 reduce [...] | 0.666 |
| LP43_1212 | LP43_0828 | LP43_1212 | LP43_0828 | Methane monooxygenase component C. | Cytochrome c family protein. | 0.652 |
| LP43_1212 | LP43_0858 | LP43_1212 | LP43_0858 | Methane monooxygenase component C. | Hypothetical protein. | 0.956 |
| LP43_1212 | LP43_1870 | LP43_1212 | LP43_1870 | Methane monooxygenase component C. | Cytochrome c oxidase polypeptide 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). | 0.622 |
| LP43_1212 | yedY | LP43_1212 | LP43_2022 | Methane monooxygenase component C. | Putative sulfite oxidase 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 reduce [...] | 0.764 |
| LP43_1870 | LP43_0828 | LP43_1870 | LP43_0828 | Cytochrome c oxidase polypeptide 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). | Cytochrome c family protein. | 0.912 |
| LP43_1870 | LP43_0858 | LP43_1870 | LP43_0858 | Cytochrome c oxidase polypeptide 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). | Hypothetical protein. | 0.887 |
| LP43_1870 | LP43_1212 | LP43_1870 | LP43_1212 | Cytochrome c oxidase polypeptide 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). | Methane monooxygenase component C. | 0.622 |
| LP43_1870 | soxD | LP43_1870 | LP43_0398 | Cytochrome c oxidase polypeptide 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). | Sulfite dehydrogenase cytochrome subunit SoxD. | 0.946 |
| LP43_1870 | soxD-2 | LP43_1870 | LP43_2405 | Cytochrome c oxidase polypeptide 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). | Sulfite dehydrogenase cytochrome subunit SoxD. | 0.946 |
| LP43_1870 | yedY | LP43_1870 | LP43_2022 | Cytochrome c oxidase polypeptide 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). | Putative sulfite oxidase 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 reduce [...] | 0.593 |
| LP43_2020 | LP43_2021 | LP43_2020 | LP43_2021 | Hypothetical protein. | Hypothetical protein. | 0.961 |
| LP43_2020 | yedY | LP43_2020 | LP43_2022 | Hypothetical protein. | Putative sulfite oxidase 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 reduce [...] | 0.571 |
| LP43_2020 | yedZ | LP43_2020 | LP43_2023 | Hypothetical protein. | Membrane protein 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 catalytic subunit MsrP, using th [...] | 0.631 |