| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| AQX53219.1 | AQX53231.1 | BC359_02180 | BC359_02240 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar hook 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. | 0.886 |
| AQX53219.1 | AQX54058.1 | BC359_02180 | BC359_06855 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.836 |
| AQX53219.1 | AQX54976.1 | BC359_02180 | BC359_12100 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.773 |
| AQX53219.1 | AQX55385.1 | BC359_02180 | BC359_14450 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Chemotaxis protein CheV; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.869 |
| AQX53219.1 | BC359_06005 | BC359_02180 | BC359_06005 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Germination protein YpeB; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.791 |
| AQX53219.1 | flgK | BC359_02180 | BC359_02185 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar hook-associated protein FlgK; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.996 |
| AQX53219.1 | flgM | BC359_02180 | BC359_02175 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar biosynthesis anti-sigma factor FlgM; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.997 |
| AQX53219.1 | fliL | BC359_02180 | BC359_06835 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar basal body-associated protein FliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | 0.854 |
| AQX53219.1 | fliY | BC359_02180 | BC359_06845 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar motor switch phosphatase 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. | 0.861 |
| AQX53231.1 | AQX53219.1 | BC359_02240 | BC359_02180 | Flagellar hook 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.886 |
| AQX53231.1 | AQX54058.1 | BC359_02240 | BC359_06855 | Flagellar hook 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; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.784 |
| AQX53231.1 | AQX54976.1 | BC359_02240 | BC359_12100 | Flagellar hook 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; Derived by automated computational analysis using gene prediction method: GeneMarkS+. | 0.985 |
| AQX53231.1 | AQX55385.1 | BC359_02240 | BC359_14450 | Flagellar hook 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. | Chemotaxis protein CheV; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.971 |
| AQX53231.1 | BC359_06005 | BC359_02240 | BC359_06005 | Flagellar hook 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. | Germination protein YpeB; Frameshifted; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.835 |
| AQX53231.1 | flgK | BC359_02240 | BC359_02185 | Flagellar hook 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 hook-associated protein FlgK; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.996 |
| AQX53231.1 | flgM | BC359_02240 | BC359_02175 | Flagellar hook 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 biosynthesis anti-sigma factor FlgM; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.940 |
| AQX53231.1 | fliL | BC359_02240 | BC359_06835 | Flagellar hook 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 basal body-associated protein FliL; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. | 0.890 |
| AQX53231.1 | fliY | BC359_02240 | BC359_06845 | Flagellar hook 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 phosphatase 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. | 0.994 |
| AQX54058.1 | AQX53219.1 | BC359_06855 | BC359_02180 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.836 |
| AQX54058.1 | AQX53231.1 | BC359_06855 | BC359_02240 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | Flagellar hook 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. | 0.784 |
