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flgL | Flagellar hook-associated protein FlgL. (417 aa) | ||||
fliF | Flagellar MS-ring protein. (542 aa) | ||||
fliG | Flagellar motor switch protein G; 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. (343 aa) | ||||
fliI | Flagellar biosynthesis/type III secretory pathway ATPase. (484 aa) | ||||
ACN83159.1 | Hypothetical protein. (150 aa) | ||||
ACN83046.1 | Flagellar protein; Component of the core of the flagella. Belongs to the bacterial flagellin family. (267 aa) | ||||
fliR | Flagellar biosynthetic protein fliR; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family. (253 aa) | ||||
fliQ | Flagellar biosynthetic protein (fliQ); Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. (89 aa) | ||||
fliP | Flagellar biosynthesis protein FliP; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. (257 aa) | ||||
flaA-2 | Putative flagellar filament outer layer protein FlaA. (241 aa) | ||||
flgC | Flagellar basal body rod protein FlgC; Belongs to the flagella basal body rod proteins family. (153 aa) | ||||
flaA-3 | Flagellar filament outer layer protein FlaA; Might be part of the flagella. (216 aa) | ||||
flgB | Flagellar basal body rod protein FlgB; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. (142 aa) | ||||
flgG | Flagellar basal body rod protein FlgG. (264 aa) | ||||
ACN83465.1 | Flagellar protein; Component of the core of the flagella. Belongs to the bacterial flagellin family. (262 aa) | ||||
flaA | Flagellar filament outer layer protein FlaA. (320 aa) | ||||
fliN | Flagellar motor switch 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. Belongs to the FliN/MopA/SpaO family. (84 aa) | ||||
fliN-2 | Flagellar motor switch 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. Belongs to the FliN/MopA/SpaO family. (360 aa) | ||||
fliM | Flagellar motor switch protein FliM; 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. (343 aa) | ||||
fliL | Putative flagellar basal body-associated protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. (181 aa) | ||||
flgE | Flagellar hook protein FlgE. (423 aa) | ||||
flaB3 | Periplasmic flagellar filament protein FlaB3; Component of the core of the flagella. Belongs to the bacterial flagellin family. (256 aa) | ||||
flaB | Flagellar filament core protein flaB2; Component of the core of the flagella. Belongs to the bacterial flagellin family. (259 aa) | ||||
flgK | Flagellar hook-associated protein FlgK. (672 aa) | ||||
flgG-2 | Flagellar basal body rod protein. (282 aa) | ||||
fliK | Flagellar hook-length control domain containing protein. (535 aa) | ||||
fliE | Putative flagellar hook-basal body protein FliE. (123 aa) | ||||
fliD | Flagellar hook-associated 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. (733 aa) |