| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| Patl_0288 | Patl_1058 | Patl_0288 | Patl_1058 | Hypothetical protein. | PFAM: iron permease FTR1; KEGG: ilo:IL0111 high-affinity Fe2+/Pb2+ permease. | 0.852 |
| Patl_0288 | Patl_2221 | Patl_0288 | Patl_2221 | Hypothetical protein. | PFAM: Rhodanese-like; KEGG: vch:VCA0620 thiosulfate sulfurtransferase SseA, putative. | 0.527 |
| Patl_0288 | Patl_3910 | Patl_0288 | Patl_3910 | Hypothetical protein. | KEGG: cps:CPS_1881 hypothetical protein. | 0.833 |
| Patl_0288 | Patl_4246 | Patl_0288 | Patl_4246 | Hypothetical protein. | 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). | 0.992 |
| Patl_0288 | msrP | Patl_0288 | Patl_2014 | Hypothetical protein. | Oxidoreductase, molybdopterin binding 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. The catalytic subunit MsrP is non-stereospecific, being able to [...] | 0.773 |
| Patl_1058 | Patl_0288 | Patl_1058 | Patl_0288 | PFAM: iron permease FTR1; KEGG: ilo:IL0111 high-affinity Fe2+/Pb2+ permease. | Hypothetical protein. | 0.852 |
| Patl_1058 | Patl_4246 | Patl_1058 | Patl_4246 | PFAM: iron permease FTR1; KEGG: ilo:IL0111 high-affinity Fe2+/Pb2+ permease. | 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). | 0.651 |
| Patl_1058 | msrP | Patl_1058 | Patl_2014 | PFAM: iron permease FTR1; KEGG: ilo:IL0111 high-affinity Fe2+/Pb2+ permease. | Oxidoreductase, molybdopterin binding 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. The catalytic subunit MsrP is non-stereospecific, being able to [...] | 0.461 |
| Patl_2012 | Patl_2015 | Patl_2012 | Patl_2015 | Hypothetical protein. | KEGG: vpa:VP0925 deoxyguanosinetriphosphate triphosphohydrolase; TIGRFAM: putative deoxyguanosinetriphosphate triphosphohydrolase; PFAM: metal-dependent phosphohydrolase, HD subdomain; SMART: Metal-dependent phosphohydrolase, HD region; Belongs to the dGTPase family. Type 2 subfamily. | 0.420 |
| Patl_2012 | msrP | Patl_2012 | Patl_2014 | Hypothetical protein. | Oxidoreductase, molybdopterin binding 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. The catalytic subunit MsrP is non-stereospecific, being able to [...] | 0.580 |
| Patl_2012 | msrQ | Patl_2012 | Patl_2013 | Hypothetical protein. | Ferric reductase-like protein transmembrane component-like 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 t [...] | 0.580 |
| Patl_2015 | Patl_2012 | Patl_2015 | Patl_2012 | KEGG: vpa:VP0925 deoxyguanosinetriphosphate triphosphohydrolase; TIGRFAM: putative deoxyguanosinetriphosphate triphosphohydrolase; PFAM: metal-dependent phosphohydrolase, HD subdomain; SMART: Metal-dependent phosphohydrolase, HD region; Belongs to the dGTPase family. Type 2 subfamily. | Hypothetical protein. | 0.420 |
| Patl_2015 | Patl_2016 | Patl_2015 | Patl_2016 | KEGG: vpa:VP0925 deoxyguanosinetriphosphate triphosphohydrolase; TIGRFAM: putative deoxyguanosinetriphosphate triphosphohydrolase; PFAM: metal-dependent phosphohydrolase, HD subdomain; SMART: Metal-dependent phosphohydrolase, HD region; Belongs to the dGTPase family. Type 2 subfamily. | KEGG: xac:XAC3992 hypothetical protein. | 0.718 |
| Patl_2015 | msrP | Patl_2015 | Patl_2014 | KEGG: vpa:VP0925 deoxyguanosinetriphosphate triphosphohydrolase; TIGRFAM: putative deoxyguanosinetriphosphate triphosphohydrolase; PFAM: metal-dependent phosphohydrolase, HD subdomain; SMART: Metal-dependent phosphohydrolase, HD region; Belongs to the dGTPase family. Type 2 subfamily. | Oxidoreductase, molybdopterin binding 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. The catalytic subunit MsrP is non-stereospecific, being able to [...] | 0.545 |
| Patl_2015 | msrQ | Patl_2015 | Patl_2013 | KEGG: vpa:VP0925 deoxyguanosinetriphosphate triphosphohydrolase; TIGRFAM: putative deoxyguanosinetriphosphate triphosphohydrolase; PFAM: metal-dependent phosphohydrolase, HD subdomain; SMART: Metal-dependent phosphohydrolase, HD region; Belongs to the dGTPase family. Type 2 subfamily. | Ferric reductase-like protein transmembrane component-like 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 t [...] | 0.545 |
| Patl_2016 | Patl_2015 | Patl_2016 | Patl_2015 | KEGG: xac:XAC3992 hypothetical protein. | KEGG: vpa:VP0925 deoxyguanosinetriphosphate triphosphohydrolase; TIGRFAM: putative deoxyguanosinetriphosphate triphosphohydrolase; PFAM: metal-dependent phosphohydrolase, HD subdomain; SMART: Metal-dependent phosphohydrolase, HD region; Belongs to the dGTPase family. Type 2 subfamily. | 0.718 |
| Patl_2016 | msrP | Patl_2016 | Patl_2014 | KEGG: xac:XAC3992 hypothetical protein. | Oxidoreductase, molybdopterin binding 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. The catalytic subunit MsrP is non-stereospecific, being able to [...] | 0.510 |
| Patl_2016 | msrQ | Patl_2016 | Patl_2013 | KEGG: xac:XAC3992 hypothetical protein. | Ferric reductase-like protein transmembrane component-like 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 t [...] | 0.517 |
| Patl_2221 | Patl_0288 | Patl_2221 | Patl_0288 | PFAM: Rhodanese-like; KEGG: vch:VCA0620 thiosulfate sulfurtransferase SseA, putative. | Hypothetical protein. | 0.527 |
| Patl_2221 | msrP | Patl_2221 | Patl_2014 | PFAM: Rhodanese-like; KEGG: vch:VCA0620 thiosulfate sulfurtransferase SseA, putative. | Oxidoreductase, molybdopterin binding 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. The catalytic subunit MsrP is non-stereospecific, being able to [...] | 0.461 |