| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| ACO47081.2 | msrP | Deide_20615 | Deide_20380 | Putative molybdenum cofactor biosynthesis protein, small and large subunit. | Putative molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized cell envelope 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. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers [...] | 0.412 |
| ACO47081.2 | msrQ | Deide_20615 | Deide_20370 | Putative molybdenum cofactor biosynthesis protein, small and large subunit. | Putative membrane protein; Part of the MsrPQ system that repairs oxidized cell envelope 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. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory [...] | 0.443 |
| ctaC | msrP | Deide_18320 | Deide_20380 | Putative cytochrome-c oxidase, subunit 2; 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 molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized cell envelope 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. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers [...] | 0.428 |
| hslO | msrP | Deide_06260 | Deide_20380 | Putative heat shock protein 33 (HSP33) (33 kDa chaperonin); Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | Putative molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized cell envelope 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. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers [...] | 0.474 |
| hslO | msrQ | Deide_06260 | Deide_20370 | Putative heat shock protein 33 (HSP33) (33 kDa chaperonin); Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | Putative membrane protein; Part of the MsrPQ system that repairs oxidized cell envelope 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. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory [...] | 0.474 |
| msrP | ACO47081.2 | Deide_20380 | Deide_20615 | Putative molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized cell envelope 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. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers [...] | Putative molybdenum cofactor biosynthesis protein, small and large subunit. | 0.412 |
| msrP | ctaC | Deide_20380 | Deide_18320 | Putative molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized cell envelope 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. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers [...] | Putative cytochrome-c oxidase, subunit 2; 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). | 0.428 |
| msrP | hslO | Deide_20380 | Deide_06260 | Putative molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized cell envelope 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. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers [...] | Putative heat shock protein 33 (HSP33) (33 kDa chaperonin); Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.474 |
| msrP | msrQ | Deide_20380 | Deide_20370 | Putative molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized cell envelope 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. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers [...] | Putative membrane protein; Part of the MsrPQ system that repairs oxidized cell envelope 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. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory [...] | 0.985 |
| msrQ | ACO47081.2 | Deide_20370 | Deide_20615 | Putative membrane protein; Part of the MsrPQ system that repairs oxidized cell envelope 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. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory [...] | Putative molybdenum cofactor biosynthesis protein, small and large subunit. | 0.443 |
| msrQ | hslO | Deide_20370 | Deide_06260 | Putative membrane protein; Part of the MsrPQ system that repairs oxidized cell envelope 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. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory [...] | Putative heat shock protein 33 (HSP33) (33 kDa chaperonin); Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.474 |
| msrQ | msrP | Deide_20370 | Deide_20380 | Putative membrane protein; Part of the MsrPQ system that repairs oxidized cell envelope 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. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory [...] | Putative molybdopterin binding protein; Part of the MsrPQ system that repairs oxidized cell envelope 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. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers [...] | 0.985 |
