STRINGSTRING
IM53_008055 IM53_008055 IM53_008040 IM53_008040 IM53_008035 IM53_008035 IM53_008030 IM53_008030 flgH flgH flgI flgI IM53_008000 IM53_008000 IM53_007995 IM53_007995 fliE fliE IM53_006045 IM53_006045 IM53_006040 IM53_006040 IM53_006035 IM53_006035 IM53_006020 IM53_006020 IM53_006015 IM53_006015 IM53_006005 IM53_006005 IM53_006010 IM53_006010 IM53_010520 IM53_010520 IM53_008840 IM53_008840 IM53_016255 IM53_016255 IM53_016260 IM53_016260 IM53_016275 IM53_016275 IM53_016300 IM53_016300 IM53_007855 IM53_007855 ycgR ycgR flhB flhB IM53_009295 IM53_009295 IM53_009290 IM53_009290 fliP fliP IM53_006000 IM53_006000 IM53_015510 IM53_015510 IM53_008050 IM53_008050
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
IM53_008055Unannotated protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. (133 aa)
IM53_008040Unannotated protein. (407 aa)
IM53_008035Unannotated protein; Belongs to the flagella basal body rod proteins family. (251 aa)
IM53_008030Unannotated protein; Belongs to the flagella basal body rod proteins family. (261 aa)
flgHUnannotated protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (230 aa)
flgIUnannotated protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (372 aa)
IM53_008000Unannotated protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (399 aa)
IM53_007995Unannotated 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. (441 aa)
fliEUnannotated protein. (123 aa)
IM53_006045Unannotated protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family. (574 aa)
IM53_006040Unannotated 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. (329 aa)
IM53_006035Unannotated protein. (206 aa)
IM53_006020Unannotated protein. (430 aa)
IM53_006015Unannotated protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. (175 aa)
IM53_006005Unannotated 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. (112 aa)
IM53_006010Unannotated 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. (337 aa)
IM53_010520Unannotated protein. (385 aa)
IM53_008840Unannotated protein. (419 aa)
IM53_016255Unannotated protein. (214 aa)
IM53_016260Unannotated protein. (334 aa)
IM53_016275Unannotated protein. (357 aa)
IM53_016300Unannotated protein. (233 aa)
IM53_007855Unannotated protein. (98 aa)
ycgRUnannotated protein; Acts as a flagellar brake, regulating swimming and swarming in a bis-(3'-5') cyclic diguanylic acid (c-di-GMP)-dependent manner. Binds 1 c-di-GMP dimer per subunit. Increasing levels of c-di-GMP lead to decreased motility. (261 aa)
flhBUnannotated 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. (376 aa)
IM53_009295Unannotated protein; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family. (263 aa)
IM53_009290Unannotated protein. (89 aa)
fliPUnannotated protein; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. (281 aa)
IM53_006000Unannotated protein. (135 aa)
IM53_015510Unannotated protein. (338 aa)
IM53_008050Unannotated protein; Belongs to the flagella basal body rod proteins family. (135 aa)
Your Current Organism:
Xanthomonas phaseoli
NCBI taxonomy Id: 1437877
Other names: X. phaseoli pv. dieffenbachiae LMG 695, Xanthomonas axonopodis pv. dieffenbachiae LMG 695, Xanthomonas phaseoli pv. dieffenbachiae LMG 695
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