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flaA | Unannotated protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (305 aa) | ||||
flaB | Unannotated protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (303 aa) | ||||
flaG | Unannotated protein. (146 aa) | ||||
fliD | Unannotated 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. (464 aa) | ||||
fliS | Unannotated protein. (140 aa) | ||||
motB | Unannotated protein. (291 aa) | ||||
motA | Unannotated protein. (252 aa) | ||||
A4SLR2_AERS4 | Unannotated protein. (343 aa) | ||||
motB-2 | Unannotated protein. (305 aa) | ||||
motA-2 | Unannotated protein. (245 aa) | ||||
flhA | Unannotated protein; Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin; Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family. (700 aa) | ||||
flhB | Unannotated protein. (281 aa) | ||||
fliR | Unannotated protein; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family. (265 aa) | ||||
fliQ | Unannotated protein; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. (89 aa) | ||||
fliP | Unannotated protein; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. (249 aa) | ||||
fliO | Unannotated protein. (127 aa) | ||||
fliN | Unannotated 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. (121 aa) | ||||
fliM | Unannotated 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. (356 aa) | ||||
fliL | Unannotated protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. (172 aa) | ||||
fliK | Unannotated protein. (639 aa) | ||||
fliJ | Unannotated protein. (146 aa) | ||||
fliI | Unannotated protein. (443 aa) | ||||
fliH | Unannotated protein. (268 aa) | ||||
fliG | Unannotated 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. (353 aa) | ||||
fliF | Unannotated protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family. (569 aa) | ||||
fliE | Unannotated protein. (105 aa) | ||||
lfiM | Unannotated protein. (236 aa) | ||||
lfiN | Unannotated 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. (125 aa) | ||||
lfiP | Unannotated protein; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. (244 aa) | ||||
lfiQ | Unannotated protein. (89 aa) | ||||
lfiR | Unannotated protein; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family. (260 aa) | ||||
lfhB | Unannotated protein; 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. (378 aa) | ||||
lfhA | Unannotated protein; Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin; Belongs to the FHIPEP (flagella/HR/invasion proteins export pore) family. (691 aa) | ||||
lfiE | Unannotated protein. (104 aa) | ||||
lfiF | Unannotated protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family. (583 aa) | ||||
lfiG | Unannotated protein. (342 aa) | ||||
lfiH | Unannotated protein. (230 aa) | ||||
lfiI | Unannotated protein. (446 aa) | ||||
lfgB | Unannotated protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. (129 aa) | ||||
lfgC | Unannotated protein; Belongs to the flagella basal body rod proteins family. (141 aa) | ||||
GCA_000820065_03388 | Unannotated protein. (178 aa) | ||||
lfgE | Unannotated protein. (397 aa) | ||||
lfgF | Unannotated protein. (244 aa) | ||||
lfgG | Unannotated protein; Belongs to the flagella basal body rod proteins family. (261 aa) | ||||
lfgH | Unannotated protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (223 aa) | ||||
lfgI | Unannotated protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (368 aa) | ||||
lfjJ | Unannotated protein. (132 aa) | ||||
lfgK | Unannotated protein. (439 aa) | ||||
lfgL | Unannotated protein. (299 aa) | ||||
GCA_000820065_03399 | Unannotated protein. (236 aa) | ||||
GCA_000820065_04014 | Unannotated protein. (110 aa) | ||||
GCA_000820065_04015 | Unannotated protein. (313 aa) | ||||
flgK | Unannotated protein. (666 aa) | ||||
flgJ | Unannotated protein. (363 aa) | ||||
flgI | Unannotated 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 | Unannotated protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (223 aa) | ||||
flgG | Unannotated protein; Belongs to the flagella basal body rod proteins family. (262 aa) | ||||
flgF | Unannotated protein; Belongs to the flagella basal body rod proteins family. (248 aa) | ||||
flgE | Unannotated protein. (446 aa) | ||||
flgD | Unannotated protein; Required for flagellar hook formation. May act as a scaffolding protein. (242 aa) | ||||
flgC | Unannotated protein; Belongs to the flagella basal body rod proteins family. (139 aa) | ||||
flgB | Unannotated protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. (132 aa) | ||||
flgA | Unannotated protein. (227 aa) | ||||
lafB | Unannotated 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. (427 aa) | ||||
lafC | Unannotated protein. (130 aa) | ||||
lafE | Unannotated protein. (362 aa) | ||||
lafF | Unannotated protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. (152 aa) | ||||
lafT | Unannotated protein. (285 aa) | ||||
lafU | Unannotated protein. (315 aa) |