STRINGSTRING
flgN flgN flgM flgM flgA flgA flgB flgB flgC flgC flgD flgD flgE flgE flgF flgF flgG flgG flgH flgH flgI flgI flgJ flgJ flgK flgK flgL flgL flhA flhA flhB flhB fliZ fliZ fliA fliA fliC fliC fliD fliD fliS fliS fliT fliT fliE fliE fliF fliF fliG fliG fliH fliH fliI fliI fliJ fliJ fliK fliK fliL fliL fliM fliM fliN fliN fliO fliO fliP fliP fliQ fliQ fliR fliR
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:
flgNExport chaperone for FlgK and FlgL; Required for the efficient initiation of filament assembly. (138 aa)
flgMAnti-sigma factor for FliA (sigma 28); Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of FliA by directly binding to FliA; Belongs to the FlgM family. (97 aa)
flgAAssembly protein for flagellar basal-body periplasmic P ring; Involved in the assembly process of the P-ring formation. It may associate with FlgF on the rod constituting a structure essential for the P-ring assembly or may act as a modulator protein for the P- ring assembly; Belongs to the FlgA family. (219 aa)
flgBFlagellar component of cell-proximal portion of basal-body rod; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body (By similarity). (138 aa)
flgCFlagellar biosynthesis, cell-proximal portion of basal-body rod; Protein involved in flagellum assembly and taxis. (134 aa)
flgDFlagellar hook assembly protein; Required for flagellar hook formation. May act as a scaffolding protein. (231 aa)
flgEFlagellar biosynthesis, hook protein; Protein involved in flagellum assembly and taxis. (402 aa)
flgFFlagellar biosynthesis, cell-proximal portion of basal-body rod; Protein involved in flagellum assembly and taxis. (251 aa)
flgGFlagellar biosynthesis, cell-distal portion of basal-body rod; Protein involved in flagellum assembly and taxis. (260 aa)
flgHFlagellar protein of basal-body outer-membrane L ring; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (232 aa)
flgIPutative flagellar 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)
flgJFlagellar rod assembly protein and murein hydrolase; Flagellum-specific muramidase which hydrolyzes the peptidoglycan layer to assemble the rod structure in the periplasmic space; In the C-terminal section; belongs to the glycosyl hydrolase 73 family. (313 aa)
flgKFlagellar biosynthesis, hook-filament junction protein 1; Protein involved in flagellum assembly, protein folding and taxis; Belongs to the flagella basal body rod proteins family. (547 aa)
flgLFlagellar biosynthesis; hook-filament junction protein; Protein involved in flagellum assembly, protein folding and taxis. (317 aa)
flhAPutative flagellar export pore 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. (692 aa)
flhBFlagellin export apparatus, substrate specificity 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. (382 aa)
fliZRpoS antagonist; During the post-exponential growth phase transiently interferes with RpoS (sigma S) activity without affecting expression of RpoS itself. It is probably not an anti-sigma factor as its overexpression is detrimental in rapidly growing cells where there is almost no sigma S factor. There is a strong overlap between Crl- activated genes and FliZ-down-regulated genes. FliZ acts as a timing device for expression of the genes for the adhesive curli fimbriae by indirectly decreasing expression of the curli regulator CsgD. (183 aa)
fliARNA polymerase, sigma 28 (sigma F) factor; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes. (239 aa)
fliCFlagellar filament structural protein (flagellin); Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (498 aa)
fliDFlagellar 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. (468 aa)
fliSFlagellar biosynthesis; repressor of class 3a and 3b operons (RflA activity); Protein involved in flagellum assembly and taxis. (136 aa)
fliTPutative flagellar synthesis and assembly chaperone; Dual-function protein that regulates the transcription of class 2 flagellar operons and that also acts as an export chaperone for the filament-capping protein FliD. As a transcriptional regulator, acts as an anti-FlhDC factor; it directly binds FlhC, thus inhibiting the binding of the FlhC/FlhD complex to class 2 promoters, resulting in decreased expression of class 2 flagellar operons. As a chaperone, effects FliD transition to the membrane by preventing its premature polymerization, and by directing it to the export apparatus. Belo [...] (121 aa)
fliEFlagellar hook-basal body complex protein FliE; Pseudogene, phage integrase family. (104 aa)
fliFFlagellar basal-body MS-ring and collar protein; The M ring may be actively involved in energy transduction; Belongs to the FliF family. (552 aa)
fliGFlagellar motor switching and energizing component; 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. (331 aa)
fliHNegative regulator of FliI ATPase activity; Needed for flagellar regrowth and assembly; Belongs to the FliH family. (228 aa)
fliIFlagellum-specific ATP synthase; Probable catalytic subunit of a protein translocase for flagellum-specific export, or a proton translocase involved in local circuits at the flagellum. May be involved in a specialized protein export pathway that proceeds without signal peptide cleavage; Belongs to the ATPase alpha/beta chains family. (457 aa)
fliJFlagellar protein; The FliJ protein is a flagellar protein that affects chemotactic events. Mutations in FliJ results in failure to respond to chemotactic stimuli. (147 aa)
fliKFlagellar hook-length control protein; Controls the length of the flagellar hook; Belongs to the FliK family. (375 aa)
fliLFlagellar biosynthesis protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. (154 aa)
fliMFlagellar motor switching and energizing component; 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. (334 aa)
fliNFlagellar motor switching and energizing component; FliN is one of three proteins (FliG, FliN, FliM) that form a switch complex that is proposed to be 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. (137 aa)
fliOFlagellar biosynthesis; Protein involved in flagellum assembly and taxis. (121 aa)
fliPFlagellar biosynthesis protein; Plays a role in the flagellum-specific transport system; Belongs to the FliP/MopC/SpaP family. (245 aa)
fliQFlagellar 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)
fliRFlagellar export pore protein; Role in flagellar biosynthesis; Belongs to the FliR/MopE/SpaR family. (261 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
Server load: low (12%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.