| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| cheD | flgB | BL01247 | BL01275 | CheD chemotaxis protein; 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; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | 0.577 |
| cheD | flgC | BL01247 | BL01274 | CheD chemotaxis protein; 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; Belongs to the flagella basal body rod proteins family. | 0.593 |
| cheD | flhA | BL01247 | BL01254 | CheD chemotaxis protein; 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). | Flagella-associated protein; 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. | 0.966 |
| cheD | flhB | BL01247 | BL01255 | CheD chemotaxis protein; 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). | Flagella-associated protein; Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin; Belongs to the type III secretion exporter family. | 0.964 |
| cheD | fliM | BL01247 | BL01262 | CheD chemotaxis protein; 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; 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. | 0.955 |
| cheD | fliQ | BL01247 | BL01257 | CheD chemotaxis protein; 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 protein; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. | 0.898 |
| cheD | fliR | BL01247 | BL01256 | CheD chemotaxis protein; 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 protein; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family. | 0.896 |
| cheD | fliY | BL01247 | BL01261 | CheD chemotaxis protein; 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 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. | 0.998 |
| cheD | sigD | BL01247 | BL01246 | CheD chemotaxis protein; 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). | RNA polymerase sigma-28 factor (sigma-D); Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. | 0.956 |
| flgB | cheD | BL01275 | BL01247 | Flagellar basal-body rod protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | CheD chemotaxis protein; 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). | 0.577 |
| flgB | flgC | BL01275 | BL01274 | Flagellar basal-body rod protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar basal-body rod protein; Belongs to the flagella basal body rod proteins family. | 0.999 |
| flgB | flgM | BL01275 | BL03367 | Flagellar basal-body rod protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Anti-sigma factor repressor of sigma-D-dependent transcription. | 0.907 |
| flgB | flhA | BL01275 | BL01254 | Flagellar basal-body rod protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagella-associated protein; 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. | 0.969 |
| flgB | flhB | BL01275 | BL01255 | Flagellar basal-body rod protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagella-associated protein; Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin; Belongs to the type III secretion exporter family. | 0.996 |
| flgB | fliM | BL01275 | BL01262 | Flagellar basal-body rod protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar motor switch protein; 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. | 0.998 |
| flgB | fliQ | BL01275 | BL01257 | Flagellar basal-body rod protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar protein; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. | 0.998 |
| flgB | fliR | BL01275 | BL01256 | Flagellar basal-body rod protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar protein; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family. | 0.993 |
| flgB | fliY | BL01275 | BL01261 | Flagellar basal-body rod protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar motor switch protein; 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. | 0.998 |
| flgB | sigD | BL01275 | BL01246 | Flagellar basal-body rod protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | RNA polymerase sigma-28 factor (sigma-D); Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. | 0.978 |
| flgC | cheD | BL01274 | BL01247 | Flagellar basal-body rod protein; Belongs to the flagella basal body rod proteins family. | CheD chemotaxis protein; 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). | 0.593 |