| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AJR22794.1 | AJR22795.1 | TZ53_02425 | TZ53_02430 | Flagellar protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar hook protein; 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. | 0.996 |
| AJR22794.1 | AJR22801.1 | TZ53_02425 | TZ53_02465 | Flagellar protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.963 |
| AJR22794.1 | AJR22807.1 | TZ53_02425 | TZ53_02500 | Flagellar protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar motor switch protein FliG; FliG 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. | 0.933 |
| AJR22794.1 | AJR22808.1 | TZ53_02425 | TZ53_02505 | Flagellar protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.962 |
| AJR22794.1 | AJR22811.1 | TZ53_02425 | TZ53_02520 | Flagellar protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 0.991 |
| AJR22794.1 | AJR22824.1 | TZ53_02425 | TZ53_02590 | Flagellar protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar basal-body rod protein FlgG; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.804 |
| AJR22794.1 | AJR22827.1 | TZ53_02425 | TZ53_02615 | Flagellar protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar P-ring protein FlgI; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.881 |
| AJR22794.1 | AJR22828.1 | TZ53_02425 | TZ53_02620 | Flagellar protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar hook protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the flagella basal body rod proteins family. | 0.985 |
| AJR22794.1 | AJR22829.1 | TZ53_02425 | TZ53_02625 | Flagellar protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 0.994 |
| AJR22794.1 | fliI | TZ53_02425 | TZ53_02490 | Flagellar protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | ATP synthase; Involved in type III protein export during flagellum assembly; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.968 |
| AJR22795.1 | AJR22794.1 | TZ53_02430 | TZ53_02425 | Flagellar hook protein; 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.996 |
| AJR22795.1 | AJR22801.1 | TZ53_02430 | TZ53_02465 | Flagellar hook protein; 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. | 0.985 |
| AJR22795.1 | AJR22807.1 | TZ53_02430 | TZ53_02500 | Flagellar hook protein; 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 FliG; FliG 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. | 0.979 |
| AJR22795.1 | AJR22808.1 | TZ53_02430 | TZ53_02505 | Flagellar hook protein; 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. | 0.986 |
| AJR22795.1 | AJR22811.1 | TZ53_02430 | TZ53_02520 | Flagellar hook protein; 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. | 0.995 |
| AJR22795.1 | AJR22824.1 | TZ53_02430 | TZ53_02590 | Flagellar hook protein; 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 basal-body rod protein FlgG; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.992 |
| AJR22795.1 | AJR22827.1 | TZ53_02430 | TZ53_02615 | Flagellar hook protein; 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 P-ring protein FlgI; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.909 |
| AJR22795.1 | AJR22828.1 | TZ53_02430 | TZ53_02620 | Flagellar hook protein; 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 hook protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the flagella basal body rod proteins family. | 0.997 |
| AJR22795.1 | AJR22829.1 | TZ53_02430 | TZ53_02625 | Flagellar hook protein; 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. | 0.993 |
| AJR22795.1 | fliI | TZ53_02430 | TZ53_02490 | Flagellar hook protein; 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. | 0.984 |
