| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| bisC | msrA | STM3644 | STM4408 | Similar to E. coli biotin sulfoxide reductase (AAC76575.1); Blastp hit to AAC76575.1 (739 aa), 86% identity in aa 2 - 739; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | Peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | 0.685 |
| bisC | msrP | STM3644 | STM3377 | Similar to E. coli biotin sulfoxide reductase (AAC76575.1); Blastp hit to AAC76575.1 (739 aa), 86% identity in aa 2 - 739; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | Putative nitrate reductase; 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, including the primary periplasmic chaperone SurA and the lipoprotein Pal. The cata [...] | 0.898 |
| bisC | msrQ | STM3644 | STM3378 | Similar to E. coli biotin sulfoxide reductase (AAC76575.1); Blastp hit to AAC76575.1 (739 aa), 86% identity in aa 2 - 739; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | Putative inner membrane 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, including the primary periplasmic chaperone SurA and the lipoprotein Pal. Msr [...] | 0.673 |
| bisC | yeaA | STM3644 | STM1291 | Similar to E. coli biotin sulfoxide reductase (AAC76575.1); Blastp hit to AAC76575.1 (739 aa), 86% identity in aa 2 - 739; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | Hypothetical protein; Putative domain frequently associated with peptide methionine sulfoxide reductase; similar to E. coli orf, hypothetical protein (AAC74848.1); Blastp hit to AAC74848.1 (137 aa), 85% identity in aa 1 - 137. | 0.751 |
| hiuH | msrP | STM1097 | STM3377 | Putative periplasmic or exported protein; Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo- 4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). | Putative nitrate reductase; 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, including the primary periplasmic chaperone SurA and the lipoprotein Pal. The cata [...] | 0.650 |
| hiuH | msrQ | STM1097 | STM3378 | Putative periplasmic or exported protein; Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo- 4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). | Putative inner membrane 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, including the primary periplasmic chaperone SurA and the lipoprotein Pal. Msr [...] | 0.804 |
| moaD | moaE | STM0805 | STM0806 | Similar to E. coli molybdopterin biosynthesis (AAC73871.1); Blastp hit to AAC73871.1 (81 aa), 86% identity in aa 1 - 81. | Molybdopterin converting factor, subunit 2; Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity); Belongs to the MoaE family. | 0.999 |
| moaD | msrP | STM0805 | STM3377 | Similar to E. coli molybdopterin biosynthesis (AAC73871.1); Blastp hit to AAC73871.1 (81 aa), 86% identity in aa 1 - 81. | Putative nitrate reductase; 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, including the primary periplasmic chaperone SurA and the lipoprotein Pal. The cata [...] | 0.446 |
| moaD | msrQ | STM0805 | STM3378 | Similar to E. coli molybdopterin biosynthesis (AAC73871.1); Blastp hit to AAC73871.1 (81 aa), 86% identity in aa 1 - 81. | Putative inner membrane 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, including the primary periplasmic chaperone SurA and the lipoprotein Pal. Msr [...] | 0.486 |
| moaE | moaD | STM0806 | STM0805 | Molybdopterin converting factor, subunit 2; Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity); Belongs to the MoaE family. | Similar to E. coli molybdopterin biosynthesis (AAC73871.1); Blastp hit to AAC73871.1 (81 aa), 86% identity in aa 1 - 81. | 0.999 |
| moaE | msrP | STM0806 | STM3377 | Molybdopterin converting factor, subunit 2; Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity); Belongs to the MoaE family. | Putative nitrate reductase; 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, including the primary periplasmic chaperone SurA and the lipoprotein Pal. The cata [...] | 0.569 |
| moaE | msrQ | STM0806 | STM3378 | Molybdopterin converting factor, subunit 2; Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity); Belongs to the MoaE family. | Putative inner membrane 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, including the primary periplasmic chaperone SurA and the lipoprotein Pal. Msr [...] | 0.518 |
| msrA | bisC | STM4408 | STM3644 | Peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | Similar to E. coli biotin sulfoxide reductase (AAC76575.1); Blastp hit to AAC76575.1 (739 aa), 86% identity in aa 2 - 739; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | 0.685 |
| msrA | msrP | STM4408 | STM3377 | Peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | Putative nitrate reductase; 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, including the primary periplasmic chaperone SurA and the lipoprotein Pal. The cata [...] | 0.778 |
| msrA | msrQ | STM4408 | STM3378 | Peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | Putative inner membrane 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, including the primary periplasmic chaperone SurA and the lipoprotein Pal. Msr [...] | 0.464 |
| msrA | yeaA | STM4408 | STM1291 | Peptide methionine sulfoxide reductase; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | Hypothetical protein; Putative domain frequently associated with peptide methionine sulfoxide reductase; similar to E. coli orf, hypothetical protein (AAC74848.1); Blastp hit to AAC74848.1 (137 aa), 85% identity in aa 1 - 137. | 0.999 |
| msrP | bisC | STM3377 | STM3644 | Putative nitrate reductase; 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, including the primary periplasmic chaperone SurA and the lipoprotein Pal. The cata [...] | Similar to E. coli biotin sulfoxide reductase (AAC76575.1); Blastp hit to AAC76575.1 (739 aa), 86% identity in aa 2 - 739; Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. | 0.898 |
| msrP | hiuH | STM3377 | STM1097 | Putative nitrate reductase; 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, including the primary periplasmic chaperone SurA and the lipoprotein Pal. The cata [...] | Putative periplasmic or exported protein; Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo- 4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU). | 0.650 |
| msrP | moaD | STM3377 | STM0805 | Putative nitrate reductase; 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, including the primary periplasmic chaperone SurA and the lipoprotein Pal. The cata [...] | Similar to E. coli molybdopterin biosynthesis (AAC73871.1); Blastp hit to AAC73871.1 (81 aa), 86% identity in aa 1 - 81. | 0.446 |
| msrP | moaE | STM3377 | STM0806 | Putative nitrate reductase; 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, including the primary periplasmic chaperone SurA and the lipoprotein Pal. The cata [...] | Molybdopterin converting factor, subunit 2; Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity); Belongs to the MoaE family. | 0.569 |
