| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AIA73880.1 | AIA73881.1 | FF32_03245 | FF32_03250 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Hypothetical 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. | 0.959 |
| AIA73880.1 | AIA74535.1 | FF32_03245 | FF32_06660 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Flagellar biosynthesis protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | 0.895 |
| AIA73880.1 | AIA74544.1 | FF32_03245 | FF32_06705 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Flagellar hook protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.896 |
| AIA73880.1 | AIA74545.1 | FF32_03245 | FF32_06710 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Flagellar hook protein FlgL; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.825 |
| AIA73880.1 | AIA74558.1 | FF32_03245 | FF32_06775 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.838 |
| AIA73880.1 | AIA74562.1 | FF32_03245 | FF32_06795 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Flagellar biosynthesis protein FliS; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.978 |
| AIA73880.1 | flgC | FF32_03245 | FF32_06665 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 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. | 0.925 |
| AIA73880.1 | flgE | FF32_03245 | FF32_06675 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | The hook connects flagellar basal body to the flagellar filament; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.923 |
| AIA73880.1 | fliG | FF32_03245 | FF32_06770 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | Flagellar motor switch protein G; 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. | 0.921 |
| AIA73880.1 | fliM | FF32_03245 | FF32_06740 | Flagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. | 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. | 0.862 |
| AIA73881.1 | AIA73880.1 | FF32_03250 | FF32_03245 | Hypothetical 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. | 0.959 |
| AIA73881.1 | AIA74535.1 | FF32_03250 | FF32_06660 | Hypothetical 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 biosynthesis protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. | 0.962 |
| AIA73881.1 | AIA74544.1 | FF32_03250 | FF32_06705 | Hypothetical 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. | 0.964 |
| AIA73881.1 | AIA74545.1 | FF32_03250 | FF32_06710 | Hypothetical 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 FlgL; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.969 |
| AIA73881.1 | AIA74558.1 | FF32_03250 | FF32_06775 | Hypothetical 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. | 0.960 |
| AIA73881.1 | AIA74562.1 | FF32_03250 | FF32_06795 | Hypothetical 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 biosynthesis protein FliS; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.973 |
| AIA73881.1 | flgC | FF32_03250 | FF32_06665 | Hypothetical 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. | 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. | 0.960 |
| AIA73881.1 | flgE | FF32_03250 | FF32_06675 | Hypothetical 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. | The hook connects flagellar basal body to the flagellar filament; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.963 |
| AIA73881.1 | fliG | FF32_03250 | FF32_06770 | Hypothetical 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 G; 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. | 0.962 |
| AIA73881.1 | fliM | FF32_03250 | FF32_06740 | Hypothetical 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 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. | 0.959 |
STRING v12.5 is now available!
