| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| KEZ52138.1 | KEZ52145.1 | GS18_0213730 | GS18_0213775 | 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. | 0.956 |
| KEZ52138.1 | KEZ52214.1 | GS18_0213730 | GS18_0214200 | 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.829 |
| KEZ52138.1 | KEZ52215.1 | GS18_0213730 | GS18_0214205 | 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 basal body rod protein FlgC; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.880 |
| KEZ52138.1 | KEZ53481.1 | GS18_0213730 | GS18_0200350 | 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.748 |
| KEZ52138.1 | KEZ54247.1 | GS18_0213730 | GS18_0204795 | 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. | 0.982 |
| KEZ52138.1 | KEZ54258.1 | GS18_0213730 | GS18_0204850 | 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; 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. | 0.982 |
| KEZ52138.1 | KEZ54259.1 | GS18_0213730 | GS18_0204855 | 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 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. | 0.999 |
| KEZ52138.1 | fliE | GS18_0213730 | GS18_0204790 | 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. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.965 |
| KEZ52138.1 | fliI | GS18_0213730 | GS18_0204810 | 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. | ATP synthase; Involved in type III protein export during flagellum assembly; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.969 |
| KEZ52145.1 | KEZ52138.1 | GS18_0213775 | GS18_0213730 | Flagellar hook protein FlgL; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.956 |
| KEZ52145.1 | KEZ52214.1 | GS18_0213775 | GS18_0214200 | Flagellar hook protein FlgL; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.890 |
| KEZ52145.1 | KEZ52215.1 | GS18_0213775 | GS18_0214205 | Flagellar hook protein FlgL; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar basal body rod protein FlgC; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.913 |
| KEZ52145.1 | KEZ53481.1 | GS18_0213775 | GS18_0200350 | Flagellar hook protein FlgL; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.822 |
| KEZ52145.1 | KEZ54247.1 | GS18_0213775 | GS18_0204795 | Flagellar hook protein FlgL; 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. | 0.931 |
| KEZ52145.1 | KEZ54258.1 | GS18_0213775 | GS18_0204850 | Flagellar hook protein FlgL; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar motor switch protein FliM; 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. | 0.961 |
| KEZ52145.1 | KEZ54259.1 | GS18_0213775 | GS18_0204855 | Flagellar hook protein FlgL; 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. | 0.977 |
| KEZ52145.1 | fliE | GS18_0213775 | GS18_0204790 | Flagellar hook protein FlgL; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.895 |
| KEZ52145.1 | fliI | GS18_0213775 | GS18_0204810 | Flagellar hook protein FlgL; 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. | 0.960 |
| KEZ52214.1 | KEZ52138.1 | GS18_0214200 | GS18_0213730 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 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. | 0.829 |
| KEZ52214.1 | KEZ52145.1 | GS18_0214200 | GS18_0213775 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar hook protein FlgL; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.890 |
STRING v12.5 is now available!
