STRINGSTRING
fliD fliD fliC fliC flgL flgL flgK flgK cheZ cheZ flgI flgI flgH flgH flgG flgG flgF flgF flgE flgE flgC flgC flgB flgB fliR fliR fliQ fliQ fliP fliP fliO fliO fliN fliN fliM fliM fliL_2 fliL_2 fliK fliK fliJ fliJ fliH_1 fliH_1 fliG fliG fliF fliF fliE fliE IL1259 IL1259 IL1519 IL1519 IL2319 IL2319 IL1107 IL1107 fliL_1 fliL_1
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:
fliDFlagellar capping 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. (463 aa)
fliCFlagellin; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (471 aa)
flgLFlagellin; Hook-filament junction protein. (404 aa)
flgKFlagellar hook-associated protein. (671 aa)
cheZChemotaxis protein CheZ; Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P). (249 aa)
flgIFlagellar basal-body P-ring protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (366 aa)
flgHFlagellar basal body L-ring protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (224 aa)
flgGFlagella basal body rod protein; Belongs to the flagella basal body rod proteins family. (262 aa)
flgFFlagella basal body rod protein. (247 aa)
flgEFlagellar hook protein FlgE. (449 aa)
flgCFlagellar basal body rod protein; Belongs to the flagella basal body rod proteins family. (150 aa)
flgBFlagellar basal body protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. (134 aa)
fliRFlagellar biosynthesis protein FliR; Role in flagellar biosynthesis. Belongs to the FliR/MopE/SpaR family. (261 aa)
fliQFlagellar biosynthesis protein FliQ; Role in flagellar biosynthesis. Belongs to the FliQ/MopD/SpaQ family. (89 aa)
fliPFlagellar biosynthesis protein FliP; Plays a role in the flagellum-specific transport system. Belongs to the FliP/MopC/SpaP family. (248 aa)
fliOFlagellar biosynthesis protein. (107 aa)
fliNFlagellar motor switch; 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. (151 aa)
fliMFlagellar motor switch 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_2Flagellar basal body-associated protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. (180 aa)
fliKFlagellar hook-length control protein. (588 aa)
fliJFlagellar biosynthesis chaperone. (147 aa)
fliH_1Type III secretory pathway protein. (249 aa)
fliGFlagellar motor switch 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. (348 aa)
fliFFlagellar basal body M-ring protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family. (570 aa)
fliEFlagellar hook-basal body protein. (110 aa)
IL1259Predicted glycosyltransferase. (229 aa)
IL1519Uncharacterized conserved protein. (209 aa)
IL2319Predicted glycosyltransferase. (234 aa)
IL1107Hypothetical protein. (545 aa)
fliL_1Flagellar basal body-associated protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. (132 aa)
Your Current Organism:
Idiomarina loihiensis
NCBI taxonomy Id: 283942
Other names: I. loihiensis L2TR, Idiomarina loihiensis L2TR, Idiomarina loihiensis str. L2TR, Idiomarina loihiensis strain L2TR
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