| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| cheW1 | flgB | TP_0364 | TP_0396 | Purine-binding chemotaxis protein (cheW-1); Similar to GP:1765974 percent identity: 99.78; identified by sequence similarity; putative. | Flagellar basal-body rod protein (flgB); Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | 0.973 |
| cheW1 | flgE | TP_0364 | TP_0727 | Purine-binding chemotaxis protein (cheW-1); Similar to GP:1765974 percent identity: 99.78; identified by sequence similarity; putative. | Flagellar hook protein (flgE); Similar to GP:2196893 percent identity: 100.00; identified by sequence similarity; putative. | 0.914 |
| cheW1 | flgK | TP_0364 | TP_0660 | Purine-binding chemotaxis protein (cheW-1); Similar to GP:1765974 percent identity: 99.78; identified by sequence similarity; putative. | Flagellar hook-associated protein 1 (flgK); Similar to SP:P70859 PID:1518046 GB:AE000783 percent identity: 39.78; identified by sequence similarity; putative. | 0.991 |
| cheW1 | flgL | TP_0364 | TP_0659 | Purine-binding chemotaxis protein (cheW-1); Similar to GP:1765974 percent identity: 99.78; identified by sequence similarity; putative. | Flagellar hook-associated protein 3 (flgL); Similar to GP:1518047 percent identity: 29.50; identified by sequence similarity; putative. | 0.920 |
| cheW1 | fliD | TP_0364 | TP_0872 | Purine-binding chemotaxis protein (cheW-1); Similar to GP:1765974 percent identity: 99.78; identified by sequence similarity; putative. | Flagellar filament cap protein (fliD); Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end (By similarity). | 0.977 |
| cheW1 | fliF | TP_0364 | TP_0399 | Purine-binding chemotaxis protein (cheW-1); Similar to GP:1765974 percent identity: 99.78; identified by sequence similarity; putative. | Flagellar basal-body M ring protein (fliF); The M ring may be actively involved in energy transduction. | 0.953 |
| cheW1 | fliM | TP_0364 | TP_0721 | Purine-binding chemotaxis protein (cheW-1); Similar to GP:1765974 percent identity: 99.78; identified by sequence similarity; putative. | Flagellar motor switch protein (fliM); FliM is one of three proteins (FliG, FliN, FliM) that forms 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 (By similarity). | 0.966 |
| cheW1 | fliS | TP_0364 | TP_0943 | Purine-binding chemotaxis protein (cheW-1); Similar to GP:1765974 percent identity: 99.78; identified by sequence similarity; putative. | Flagellar protein (fliS); Similar to GB:Z31376 SP:P39739 PID:499382 PID:1762346 GB:AL009126 percent identity: 34.48; identified by sequence similarity; putative. | 0.994 |
| cheW1 | fliW | TP_0364 | TP_0658 | Purine-binding chemotaxis protein (cheW-1); Similar to GP:1765974 percent identity: 99.78; identified by sequence similarity; putative. | Transmembrane protein, putative; Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin and participates in the assembly of the flagellum. Belongs to the FliW family. | 0.496 |
| cheW1 | fliY | TP_0364 | TP_0720 | Purine-binding chemotaxis protein (cheW-1); Similar to GP:1765974 percent identity: 99.78; identified by sequence similarity; putative. | Flagellar motor switch protein (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 |
| flgB | cheW1 | TP_0396 | TP_0364 | Flagellar basal-body rod protein (flgB); Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Purine-binding chemotaxis protein (cheW-1); Similar to GP:1765974 percent identity: 99.78; identified by sequence similarity; putative. | 0.973 |
| flgB | flgE | TP_0396 | TP_0727 | Flagellar basal-body rod protein (flgB); Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar hook protein (flgE); Similar to GP:2196893 percent identity: 100.00; identified by sequence similarity; putative. | 0.994 |
| flgB | flgK | TP_0396 | TP_0660 | Flagellar basal-body rod protein (flgB); Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar hook-associated protein 1 (flgK); Similar to SP:P70859 PID:1518046 GB:AE000783 percent identity: 39.78; identified by sequence similarity; putative. | 0.972 |
| flgB | flgL | TP_0396 | TP_0659 | Flagellar basal-body rod protein (flgB); Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar hook-associated protein 3 (flgL); Similar to GP:1518047 percent identity: 29.50; identified by sequence similarity; putative. | 0.925 |
| flgB | fliD | TP_0396 | TP_0872 | Flagellar basal-body rod protein (flgB); Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar filament cap protein (fliD); Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end (By similarity). | 0.970 |
| flgB | fliF | TP_0396 | TP_0399 | Flagellar basal-body rod protein (flgB); Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar basal-body M ring protein (fliF); The M ring may be actively involved in energy transduction. | 0.998 |
| flgB | fliM | TP_0396 | TP_0721 | Flagellar basal-body rod protein (flgB); Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar motor switch protein (fliM); FliM is one of three proteins (FliG, FliN, FliM) that forms 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 (By similarity). | 0.977 |
| flgB | fliS | TP_0396 | TP_0943 | Flagellar basal-body rod protein (flgB); Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar protein (fliS); Similar to GB:Z31376 SP:P39739 PID:499382 PID:1762346 GB:AL009126 percent identity: 34.48; identified by sequence similarity; putative. | 0.966 |
| flgB | fliW | TP_0396 | TP_0658 | Flagellar basal-body rod protein (flgB); Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Transmembrane protein, putative; Acts as an anti-CsrA protein, binds CsrA and prevents it from repressing translation of its target genes, one of which is flagellin. Binds to flagellin and participates in the assembly of the flagellum. Belongs to the FliW family. | 0.644 |
| flgB | fliY | TP_0396 | TP_0720 | Flagellar basal-body rod protein (flgB); Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | Flagellar motor switch protein (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. | 0.984 |