| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AKL11433.1 | AKL11442.1 | AB182_09000 | AB182_09045 | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | Flagellar cap protein FliD; Required for 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. | 0.975 |
| AKL11433.1 | AKL11443.1 | AB182_09000 | AB182_09050 | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 0.896 |
| AKL11433.1 | AKL14460.1 | AB182_09000 | AB182_25695 | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | Hypothetical protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 0.884 |
| AKL11433.1 | flgC | AB182_09000 | AB182_09455 | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | With FlgF and B makes up the proximal portion of the flagellar basal body rod; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.997 |
| AKL11433.1 | flgK | AB182_09000 | AB182_09495 | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | With FlgL acts as a hook filament junction protein to join the flagellar filament to the hook; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.968 |
| AKL11433.1 | flgL | AB182_09000 | AB182_09500 | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | With FlgK acts as a hook filament junction protein to join the flagellar filament to the hook; Yersinia, Vibrio parahaemolyticus, Bradyrhizobium and other organisms have 2 copies of this and other flagellar genes; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.914 |
| AKL11433.1 | fliI | AB182_09000 | AB182_08985 | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | ATP synthase; Involved in type III protein export during flagellum assembly; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.997 |
| AKL11433.1 | fliM | AB182_09000 | AB182_08965 | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 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. | 0.997 |
| AKL11433.1 | fliN | AB182_09000 | AB182_08960 | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | Flagellar motor switch protein FliN; 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. | 0.997 |
| AKL11433.1 | fliS | AB182_09000 | AB182_09040 | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | Flagellar protein FliS; Flagellin specific chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.972 |
| AKL11442.1 | AKL11433.1 | AB182_09045 | AB182_09000 | Flagellar cap protein FliD; Required for 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. | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.975 |
| AKL11442.1 | AKL11443.1 | AB182_09045 | AB182_09050 | Flagellar cap protein FliD; Required for 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. | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 0.989 |
| AKL11442.1 | AKL14460.1 | AB182_09045 | AB182_25695 | Flagellar cap protein FliD; Required for 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. | Hypothetical protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 0.983 |
| AKL11442.1 | flgC | AB182_09045 | AB182_09455 | Flagellar cap protein FliD; Required for 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. | With FlgF and B makes up the proximal portion of the flagellar basal body rod; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.965 |
| AKL11442.1 | flgK | AB182_09045 | AB182_09495 | Flagellar cap protein FliD; Required for 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. | With FlgL acts as a hook filament junction protein to join the flagellar filament to the hook; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.997 |
| AKL11442.1 | flgL | AB182_09045 | AB182_09500 | Flagellar cap protein FliD; Required for 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. | With FlgK acts as a hook filament junction protein to join the flagellar filament to the hook; Yersinia, Vibrio parahaemolyticus, Bradyrhizobium and other organisms have 2 copies of this and other flagellar genes; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.997 |
| AKL11442.1 | fliI | AB182_09045 | AB182_08985 | Flagellar cap protein FliD; Required for 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. | ATP synthase; Involved in type III protein export during flagellum assembly; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.976 |
| AKL11442.1 | fliM | AB182_09045 | AB182_08965 | Flagellar cap protein FliD; Required for 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. | 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. | 0.966 |
| AKL11442.1 | fliN | AB182_09045 | AB182_08960 | Flagellar cap protein FliD; Required for 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. | Flagellar motor switch protein FliN; 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. | 0.964 |
| AKL11442.1 | fliS | AB182_09045 | AB182_09040 | Flagellar cap protein FliD; Required for 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. | Flagellar protein FliS; Flagellin specific chaperone; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.999 |
