| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| cheD | flgC | ABC2245 | ABC2271 | Chemotaxis protein CheD; Deamidates glutamine residues to glutamate on methyl- accepting chemotaxis receptors (MCPs). CheD-mediated MCP deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase (By similarity). | Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. | 0.636 |
| cheD | flgK | ABC2245 | ABC3079 | Chemotaxis protein CheD; Deamidates glutamine residues to glutamate on methyl- accepting chemotaxis receptors (MCPs). CheD-mediated MCP deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase (By similarity). | Flagellar hook-associated protein 1 FlgK; Belongs to the flagella basal body rod proteins family. | 0.563 |
| cheD | flhA | ABC2245 | ABC2250 | Chemotaxis protein CheD; Deamidates glutamine residues to glutamate on methyl- accepting chemotaxis receptors (MCPs). CheD-mediated MCP deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase (By similarity). | Flagellar biosynthesis protein FlhA; Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin; Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family. | 0.954 |
| cheD | fliF | ABC2245 | ABC2269 | Chemotaxis protein CheD; Deamidates glutamine residues to glutamate on methyl- accepting chemotaxis receptors (MCPs). CheD-mediated MCP deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase (By similarity). | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.679 |
| cheD | fliG | ABC2245 | ABC2268 | Chemotaxis protein CheD; Deamidates glutamine residues to glutamate on methyl- accepting chemotaxis receptors (MCPs). CheD-mediated MCP deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase (By similarity). | Flagellar motor switch protein FliG; One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation; Belongs to the FliG family. | 0.826 |
| cheD | fliH | ABC2245 | ABC2267 | Chemotaxis protein CheD; Deamidates glutamine residues to glutamate on methyl- accepting chemotaxis receptors (MCPs). CheD-mediated MCP deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase (By similarity). | Flagellar assembly protein FliH. | 0.728 |
| cheD | fliI | ABC2245 | ABC2266 | Chemotaxis protein CheD; Deamidates glutamine residues to glutamate on methyl- accepting chemotaxis receptors (MCPs). CheD-mediated MCP deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase (By similarity). | Flagellum-specific ATP synthase. | 0.770 |
| cheD | fliM | ABC2245 | ABC2258 | Chemotaxis protein CheD; Deamidates glutamine residues to glutamate on methyl- accepting chemotaxis receptors (MCPs). CheD-mediated MCP deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase (By similarity). | Flagellar motor switch protein FliM; One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation; Belongs to the FliM family. | 0.934 |
| cheD | fliP | ABC2245 | ABC2254 | Chemotaxis protein CheD; Deamidates glutamine residues to glutamate on methyl- accepting chemotaxis receptors (MCPs). CheD-mediated MCP deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase (By similarity). | Flagellar biosynthetic protein FliP; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. | 0.824 |
| cheD | fliY | ABC2245 | ABC2257 | Chemotaxis protein CheD; Deamidates glutamine residues to glutamate on methyl- accepting chemotaxis receptors (MCPs). CheD-mediated MCP deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase (By similarity). | Flagellar motor switch protein FliN/FliY; FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. Belongs to the FliN/MopA/SpaO family. | 0.999 |
| flgC | cheD | ABC2271 | ABC2245 | Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. | Chemotaxis protein CheD; Deamidates glutamine residues to glutamate on methyl- accepting chemotaxis receptors (MCPs). CheD-mediated MCP deamidation is required for productive communication of the conformational signals of the chemoreceptors to the CheA kinase (By similarity). | 0.636 |
| flgC | flgK | ABC2271 | ABC3079 | Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. | Flagellar hook-associated protein 1 FlgK; Belongs to the flagella basal body rod proteins family. | 0.986 |
| flgC | flhA | ABC2271 | ABC2250 | Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. | Flagellar biosynthesis protein FlhA; Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin; Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family. | 0.970 |
| flgC | fliF | ABC2271 | ABC2269 | Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.999 |
| flgC | fliG | ABC2271 | ABC2268 | Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. | Flagellar motor switch protein FliG; One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation; Belongs to the FliG family. | 0.997 |
| flgC | fliH | ABC2271 | ABC2267 | Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. | Flagellar assembly protein FliH. | 0.989 |
| flgC | fliI | ABC2271 | ABC2266 | Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. | Flagellum-specific ATP synthase. | 0.994 |
| flgC | fliM | ABC2271 | ABC2258 | Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. | Flagellar motor switch protein FliM; One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation; Belongs to the FliM family. | 0.996 |
| flgC | fliP | ABC2271 | ABC2254 | Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. | Flagellar biosynthetic protein FliP; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. | 0.995 |
| flgC | fliY | ABC2271 | ABC2257 | Flagellar basal-body rod protein FlgC; Belongs to the flagella basal body rod proteins family. | Flagellar motor switch protein FliN/FliY; FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. Belongs to the FliN/MopA/SpaO family. | 0.999 |