Phosphodiesterase acting on cyclic dinucleotides; Has phosphodiesterase (PDE) activity against cyclic-di-AMP (c-di-AMP) and to a much lesser extent against cyclic-di-GMP (c-di-GMP) in the DHH/DHHA1 domains. Also has ATPase activity, probably via the GGDEF domain. Overexpression leads to increased sensitivity to methyl methanesulfonate (MMS) and H(2)O(2). Overexpression leads to extreme sensitivity to the beta-lactam antibiotic cefuroxime (CEF), probably dependent on PDE activity. May monitor cellular heme or NO levels. In B.subtilis c-di-AMP is a second messenger that mediates growth, [...]

Oligoribonuclease (nanoRNAse), 3',5'-bisphosphate nucleotidase; Bifunctional enzyme which has both oligoribonuclease and pAp- phosphatase activities. Degrades RNA and DNA oligonucleotides with a length of 5 nucleotides and shorter, with a preference for 3-mers. Directionality is controversial; shown to degrade 5-mers and less in a 3' to 5' direction , and 11-mers in a 5' to 3' direction. Converts 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP.

Phosphodiesterase acting on cyclic dinucleotides; Has phosphodiesterase (PDE) activity against cyclic-di-AMP (c-di-AMP) and to a much lesser extent against cyclic-di-GMP (c-di-GMP) in the DHH/DHHA1 domains. Also has ATPase activity, probably via the GGDEF domain. Overexpression leads to increased sensitivity to methyl methanesulfonate (MMS) and H(2)O(2). Overexpression leads to extreme sensitivity to the beta-lactam antibiotic cefuroxime (CEF), probably dependent on PDE activity. May monitor cellular heme or NO levels. In B.subtilis c-di-AMP is a second messenger that mediates growth, [...]

Putative single-strand DNA-specific exonuclease; Putative single-stranded-DNA-specific exonuclease (By similarity). RecA thread formation during DNA double-strand break repair requires RecJ or AadAB; Belongs to the RecJ family.

Flagellar hook protein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type f: factor; Belongs to the flagella basal body rod proteins family.

Flagellar hook-filament junction; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; structure.

Flagellar hook protein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type f: factor; Belongs to the flagella basal body rod proteins family.

Flagellar hook-associated capping protein 2 (HAP2); 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 (By similarity); Belongs to the FliD family.

Flagellar hook protein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type f: factor; Belongs to the flagella basal body rod proteins family.

Flagellar basal-body M-ring protein; The M ring may be actively involved in energy transduction.

Flagellar hook protein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type f: factor; Belongs to the flagella basal body rod proteins family.

Flagellar motor switching and energizing component; 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.

Flagellar hook protein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type f: factor; Belongs to the flagella basal body rod proteins family.

Motility protein B; MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity).

Flagellar hook-filament junction; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; structure.

Flagellar hook protein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type f: factor; Belongs to the flagella basal body rod proteins family.

Flagellar hook-filament junction; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; structure.

Flagellar hook-associated capping protein 2 (HAP2); 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 (By similarity); Belongs to the FliD family.

Flagellar hook-filament junction; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; structure.

Flagellar basal-body M-ring protein; The M ring may be actively involved in energy transduction.

Flagellar hook-filament junction; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; structure.

Flagellar motor switching and energizing component; 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.

Flagellar hook-filament junction; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; structure.

Motility protein B; MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity).

Flagellar hook-associated capping protein 2 (HAP2); 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 (By similarity); Belongs to the FliD family.

Flagellar hook protein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type f: factor; Belongs to the flagella basal body rod proteins family.

Flagellar hook-associated capping protein 2 (HAP2); 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 (By similarity); Belongs to the FliD family.

Flagellar hook-filament junction; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; structure.

Flagellar hook-associated capping protein 2 (HAP2); 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 (By similarity); Belongs to the FliD family.

Flagellar basal-body M-ring protein; The M ring may be actively involved in energy transduction.

Flagellar hook-associated capping protein 2 (HAP2); 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 (By similarity); Belongs to the FliD family.

Flagellar motor switching and energizing component; 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.

Flagellar hook-associated capping protein 2 (HAP2); 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 (By similarity); Belongs to the FliD family.

Motility protein B; MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity).

Flagellar hook-associated capping protein 2 (HAP2); 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 (By similarity); Belongs to the FliD family.

Putative cyclic diGMP binding protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative regulator.

Flagellar basal-body M-ring protein; The M ring may be actively involved in energy transduction.

Flagellar hook protein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type f: factor; Belongs to the flagella basal body rod proteins family.

Flagellar basal-body M-ring protein; The M ring may be actively involved in energy transduction.

Flagellar hook-filament junction; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; structure.