node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
flgM | fliA | b1071 | b1922 | Anti-sigma factor for FliA (sigma 28); Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of FliA by directly binding to FliA; Belongs to the FlgM family. | RNA polymerase, sigma 28 (sigma F) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes. | 0.999 |
flgM | fliD | b1071 | b1924 | Anti-sigma factor for FliA (sigma 28); Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of FliA by directly binding to FliA; Belongs to the FlgM family. | Flagellar filament capping protein; Required for the 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; Belongs to the FliD family. | 0.996 |
flgM | fliG | b1071 | b1939 | Anti-sigma factor for FliA (sigma 28); Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of FliA by directly binding to FliA; Belongs to the FlgM family. | Flagellar motor switching and energizing component; 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. | 0.858 |
flgM | fliM | b1071 | b1945 | Anti-sigma factor for FliA (sigma 28); Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of FliA by directly binding to FliA; Belongs to the FlgM family. | Flagellar motor switching and energizing component; 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. | 0.957 |
flgM | fliS | b1071 | b1925 | Anti-sigma factor for FliA (sigma 28); Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of FliA by directly binding to FliA; Belongs to the FlgM family. | Flagellar biosynthesis; repressor of class 3a and 3b operons (RflA activity); Protein involved in flagellum assembly and taxis. | 0.996 |
flgM | motB | b1071 | b1889 | Anti-sigma factor for FliA (sigma 28); Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of FliA by directly binding to FliA; Belongs to the FlgM family. | Protein that enables flagellar motor rotation; MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Probably a linker that fastens the torque-generating machinery to the cell wall. Overexpression of this protein with MotA improves motility in a pdeH disruption, (a c-di-GMP phosphodiesterase) suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein YcgR and the flagellar stator. | 0.971 |
flgM | ycgR | b1071 | b1194 | Anti-sigma factor for FliA (sigma 28); Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of FliA by directly binding to FliA; Belongs to the FlgM family. | Flagellar velocity braking protein, c-di-GMP-regulated; Acts as a flagellar brake, regulating swimming and swarming in a bis-(3'-5') cyclic diguanylic acid (c-di-GMP)-dependent manner. When bound to c-di-GMP it binds to elements of the flagellar motor (MotA and/or FliG and FliM , binding to FliM also occurs in the absence of c-di-GMP), causing the motor to slow down. Thus, increasing levels of c-di-GMP lead to decreased motility. Probably binds 1 c-di-GMP dimer per subunit. | 0.900 |
flgM | yhjH | b1071 | b3525 | Anti-sigma factor for FliA (sigma 28); Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of FliA by directly binding to FliA; Belongs to the FlgM family. | cyclic-di-GMP phosphodiesterase, FlhDC-regulated; Involved in the control of the switch from cell motility to adhesion via regulation of cellular levels of cyclic-di-GMP (c-di-GMP). Part of a signaling cascade that regulates curli biosynthesis. The cascade is composed of two c-di-GMP control modules, in which c-di-GMP controlled by the DgcE/PdeH pair (module I) regulates the activity of the DgcM/PdeR pair (module II), which in turn regulates activity of the transcription factor MlrA and expression of the master biofilm regulator csgD. Effect on flagella is controlled via the c-di-GMP-b [...] | 0.622 |
fliA | flgM | b1922 | b1071 | RNA polymerase, sigma 28 (sigma F) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes. | Anti-sigma factor for FliA (sigma 28); Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of FliA by directly binding to FliA; Belongs to the FlgM family. | 0.999 |
fliA | fliD | b1922 | b1924 | RNA polymerase, sigma 28 (sigma F) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes. | Flagellar filament capping protein; Required for the 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; Belongs to the FliD family. | 0.996 |
fliA | fliG | b1922 | b1939 | RNA polymerase, sigma 28 (sigma F) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes. | Flagellar motor switching and energizing component; 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. | 0.990 |
fliA | fliM | b1922 | b1945 | RNA polymerase, sigma 28 (sigma F) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes. | Flagellar motor switching and energizing component; 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. | 0.995 |
fliA | fliS | b1922 | b1925 | RNA polymerase, sigma 28 (sigma F) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes. | Flagellar biosynthesis; repressor of class 3a and 3b operons (RflA activity); Protein involved in flagellum assembly and taxis. | 0.986 |
fliA | motB | b1922 | b1889 | RNA polymerase, sigma 28 (sigma F) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes. | Protein that enables flagellar motor rotation; MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Probably a linker that fastens the torque-generating machinery to the cell wall. Overexpression of this protein with MotA improves motility in a pdeH disruption, (a c-di-GMP phosphodiesterase) suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein YcgR and the flagellar stator. | 0.987 |
fliA | ycgR | b1922 | b1194 | RNA polymerase, sigma 28 (sigma F) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes. | Flagellar velocity braking protein, c-di-GMP-regulated; Acts as a flagellar brake, regulating swimming and swarming in a bis-(3'-5') cyclic diguanylic acid (c-di-GMP)-dependent manner. When bound to c-di-GMP it binds to elements of the flagellar motor (MotA and/or FliG and FliM , binding to FliM also occurs in the absence of c-di-GMP), causing the motor to slow down. Thus, increasing levels of c-di-GMP lead to decreased motility. Probably binds 1 c-di-GMP dimer per subunit. | 0.912 |
fliA | yhjH | b1922 | b3525 | RNA polymerase, sigma 28 (sigma F) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes. | cyclic-di-GMP phosphodiesterase, FlhDC-regulated; Involved in the control of the switch from cell motility to adhesion via regulation of cellular levels of cyclic-di-GMP (c-di-GMP). Part of a signaling cascade that regulates curli biosynthesis. The cascade is composed of two c-di-GMP control modules, in which c-di-GMP controlled by the DgcE/PdeH pair (module I) regulates the activity of the DgcM/PdeR pair (module II), which in turn regulates activity of the transcription factor MlrA and expression of the master biofilm regulator csgD. Effect on flagella is controlled via the c-di-GMP-b [...] | 0.896 |
fliD | flgM | b1924 | b1071 | Flagellar filament capping protein; Required for the 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; Belongs to the FliD family. | Anti-sigma factor for FliA (sigma 28); Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of FliA by directly binding to FliA; Belongs to the FlgM family. | 0.996 |
fliD | fliA | b1924 | b1922 | Flagellar filament capping protein; Required for the 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; Belongs to the FliD family. | RNA polymerase, sigma 28 (sigma F) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes. | 0.996 |
fliD | fliG | b1924 | b1939 | Flagellar filament capping protein; Required for the 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; Belongs to the FliD family. | Flagellar motor switching and energizing component; 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 |
fliD | fliM | b1924 | b1945 | Flagellar filament capping protein; Required for the 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; Belongs to the FliD family. | Flagellar motor switching and energizing component; 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. | 0.998 |