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fliH | Flagellar biosynthesis protein; Needed for flagellar regrowth and assembly. (235 aa) | ||||
fliR | Putative flagellar biosynthetic protein; Role in flagellar biosynthesis; Belongs to the FliR/MopE/SpaR family. (264 aa) | ||||
fliQ | Flagellar biosynthesis protein; Required for the assembly of the rivet at the earliest stage of flagellar biosynthesis; Belongs to the FliQ/MopD/SpaQ family. (89 aa) | ||||
fliP | Flagellar biosynthesis protein; Plays a role in the flagellum-specific transport system. (245 aa) | ||||
fliN | Flagellar biosynthesis protein; 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 (By similarity). Belongs to the FliN/MopA/SpaO family. (137 aa) | ||||
fliM | Flagellar biosynthesis protein; 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 (By similarity). (334 aa) | ||||
fliG | Flagellar biosynthesis protein; 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 (By similarity). (331 aa) | ||||
fliF | Basal-body MS (membrane and supramembrane)-ring and collar protein; The M ring may be actively involved in energy transduction. (560 aa) | ||||
fliD | 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. (467 aa) | ||||
fliC | Flagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (495 aa) | ||||
motB | Enables flagellar motor rotation; 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). (309 aa) | ||||
cheA | Sensory histitine protein kinase; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY. (671 aa) | ||||
cheW | Purine-binding chemotaxis protein; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. (167 aa) | ||||
cheR | Glutamate methyltransferase; Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. (288 aa) | ||||
cheB | Methyl esterase; Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid (By similarity). Belongs to the CheB family. (349 aa) | ||||
cheZ | Chemotactic response protein; Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P). Acts on free CheY-P. Belongs to the CheZ family. (214 aa) | ||||
flhB | Putative part of export apparatus for flagellar proteins; Required for formation of the rod structure in the basal body of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin; Belongs to the type III secretion exporter family. (383 aa) | ||||
flhA | Flagellar biosynthesis protein; Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin. (692 aa) | ||||
flgL | Hook-filament junction protein; Flagellar biosynthesis protein; flagellar hook-associated protein 3 (HAP3) (hook-filament junctionprotein). (SW:FLGL_SALTY). (317 aa) | ||||
flgK | Hook-filament junction protein 1; Flagellar biosynthesis protein; flagellar hook-associated protein 1 (HAP1). (SW:FLGK_SALTY); Belongs to the flagella basal body rod proteins family. (553 aa) | ||||
flgI | Putative flagella basal body protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (365 aa) | ||||
flgH | Flagellar biosynthesis protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (232 aa) | ||||
flgE | Hook protein; Flagellar biosynthesis; flagellar hook protein flge. (SW:FLGE_SALTY); Belongs to the flagella basal body rod proteins family. (403 aa) |