| node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
| flgJ | fliD | PSHAa0777 | PSHAa0784 | Putative flagellar biosynthesis; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; structural protein. | Putative flagellar hook-associated 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. | 0.949 |
| flgJ | fliE | PSHAa0777 | PSHAa0791 | Putative flagellar biosynthesis; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; structural protein. | Flagellar biosynthesis; Function of homologous gene experimentally demonstrated in an other organism; structural protein. | 0.996 |
| flgJ | fliF | PSHAa0777 | PSHAa0792 | Putative flagellar biosynthesis; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; structural protein. | Flagellar biosynthesis; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.997 |
| flgJ | fliG | PSHAa0777 | PSHAa0793 | Putative flagellar biosynthesis; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; structural protein. | Flagellar biosynthesis; 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. | 0.997 |
| flgJ | fliH | PSHAa0777 | PSHAa0794 | Putative flagellar biosynthesis; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; structural protein. | Putative flagellar biosynthesis; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; membrane component. | 0.995 |
| flgJ | fliI | PSHAa0777 | PSHAa0795 | Putative flagellar biosynthesis; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; structural protein. | Flagellum-specific ATP synthase; Function of strongly homologous gene; enzyme. | 0.945 |
| flgJ | fliJ | PSHAa0777 | PSHAa0796 | Putative flagellar biosynthesis; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; structural protein. | Flagellar protein; Function of strongly homologous gene; structural protein. | 0.954 |
| flgJ | fliK | PSHAa0777 | PSHAa0797 | Putative flagellar biosynthesis; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; structural protein. | Putative flagellar hook-length control protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; structural protein. | 0.993 |
| flgJ | fliM | PSHAa0777 | PSHAa0799 | Putative flagellar biosynthesis; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; structural protein. | Flagellar biosynthesis; 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. | 0.996 |
| flgJ | fliN | PSHAa0777 | PSHAa0800 | Putative flagellar biosynthesis; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; structural protein. | Flagellar biosynthesis; 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. | 0.980 |
| fliD | flgJ | PSHAa0784 | PSHAa0777 | Putative flagellar hook-associated 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. | Putative flagellar biosynthesis; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; structural protein. | 0.949 |
| fliD | fliE | PSHAa0784 | PSHAa0791 | Putative flagellar hook-associated 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; Function of homologous gene experimentally demonstrated in an other organism; structural protein. | 0.976 |
| fliD | fliF | PSHAa0784 | PSHAa0792 | Putative flagellar hook-associated 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; The M ring may be actively involved in energy transduction. Belongs to the FliF family. | 0.982 |
| fliD | fliG | PSHAa0784 | PSHAa0793 | Putative flagellar hook-associated 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; 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 |
| fliD | fliH | PSHAa0784 | PSHAa0794 | Putative flagellar hook-associated 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. | Putative flagellar biosynthesis; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; membrane component. | 0.991 |
| fliD | fliI | PSHAa0784 | PSHAa0795 | Putative flagellar hook-associated 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. | Flagellum-specific ATP synthase; Function of strongly homologous gene; enzyme. | 0.977 |
| fliD | fliJ | PSHAa0784 | PSHAa0796 | Putative flagellar hook-associated 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; Function of strongly homologous gene; structural protein. | 0.909 |
| fliD | fliK | PSHAa0784 | PSHAa0797 | Putative flagellar hook-associated 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. | Putative flagellar hook-length control protein; Function proposed based on presence of conserved amino acid motif, structural feature or limited homolgy; structural protein. | 0.873 |
| fliD | fliM | PSHAa0784 | PSHAa0799 | Putative flagellar hook-associated 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; 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. | 0.976 |
| fliD | fliN | PSHAa0784 | PSHAa0800 | Putative flagellar hook-associated 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; 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 |
