STRINGSTRING
ymdA ymdA 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 ydiV ydiV ynjH ynjH flhE flhE flhA flhA flhB flhB cheZ cheZ cheY cheY cheB cheB cheR cheR tap tap tar tar cheW cheW cheA cheA motB motB motA motA flhC flhC flhD flhD yecR yecR 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 aer aer crfC crfC yjcZ yjcZ proP proP tsr tsr
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.
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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:
ymdAUncharacterized protein. (103 aa)
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)
ydiVanti-FlhD4C2 factor, inactive EAL family phosphodiesterase; Upon overexpression acts as a novel anti-FlhC(2)FlhD(4) factor, decreasing its DNA-binding activity, able to negatively regulate expression of flagellar class II operons including FliC. (237 aa)
ynjHDUF1496 family protein. (90 aa)
flhEProton seal during flagellar secretion; Not essential for flagellar formation and function. (130 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)
cheZChemotaxis regulator, protein phosphatase for CheY; Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P); Belongs to the CheZ family. (214 aa)
cheYChemotaxis regulator transmitting signal to flagellar motor component; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from counterclockwise to clockwise flagellar rotation. Overexpression of CheY in association with MotA and MotB improves motility of a ycgR disruption, suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein and th [...] (129 aa)
cheBProtein-glutamate methylesterase/protein-glutamine glutaminase; Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid. Catalyzes its own deactivation by removing the activating phosphoryl group. Belongs to the CheB family. (349 aa)
cheRChemotaxis regulator, protein-glutamate methyltransferase; Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. (286 aa)
tapMethyl-accepting protein IV; Mediates taxis toward dipeptides via an interaction with the periplasmic dipeptide-binding protein. (533 aa)
tarMethyl-accepting chemotaxis protein II; Receptor for the attractant L-aspartate and related amino and dicarboxylic acids. Tar also mediates taxis to the attractant maltose via an interaction with the periplasmic maltose binding protein. Tar mediates taxis away from the repellents cobalt and nickel. (553 aa)
cheWPurine-binding chemotaxis protein; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. It physically bridges CheA to the MCPs (methyl-accepting chemotaxis proteins) to allow regulated phosphotransfer to CheY and CheB. (167 aa)
cheAChemotaxis protein CheA; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheA is autophosphorylated; it can transfer its phosphate group to either CheB or CheY. (654 aa)
motBProtein that enables flagellar motor rotation; MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Probably a linker that fastens the torque-generating machinery to the cell wall. Overexpression of this protein with MotA improves motility in a pdeH disruption, (a c-di-GMP phosphodiesterase) suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein YcgR and the flagellar stator. (308 aa)
motAProton conductor component of flagella motor; MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel. Overexpression of MotA, with or without MotB, restores motility in a pdeH disruption, (a c-di-GMP phosphodiesterase) suggesting there is an interaction (direct or indirect) between the c-di-GMP-binding flagellar brake protein YcgR and the flagellar stator. (295 aa)
flhCFlagellar class II regulon transcriptional activator, with FlhD; Functions in complex with FlhD as a master transcriptional regulator that regulates transcription of several flagellar and non- flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways. (192 aa)
flhDFlagellar class II regulon transcriptional activator, with FlhC; Functions in complex with FlhC as a master transcriptional regulator that regulates transcription of several flagellar and non- flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways. (116 aa)
yecRLipoprotein, function unknown. (107 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)
aerFused signal transducer for aerotaxis sensory component/methyl accepting chemotaxis component; Signal transducer for aerotaxis. The aerotactic response is the accumulation of cells around air bubbles. The nature of the sensory stimulus detected by this protein is the proton motive force or cellular redox state. It uses a FAD prosthetic group as a redox sensor to monitor oxygen levels. (506 aa)
crfCClamp-binding sister replication fork colocalization protein, dynamin-related; Important for the colocalization of sister nascent DNA strands after replication fork passage during DNA replication, and for positioning and subsequent partitioning of sister chromosomes. Does not have GTPase activity on its own; Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family. (742 aa)
yjcZYjcZ family protein; yhjH motility defect suppressor. (292 aa)
proPProline/glycine betaine transporter; Proton symporter that senses osmotic shifts and responds by importing osmolytes such as proline, glycine betaine, stachydrine, pipecolic acid, ectoine and taurine. It is both an osmosensor and an osmoregulator which is available to participate early in the bacterial osmoregulatory response; Belongs to the major facilitator superfamily. Metabolite:H+ Symporter (MHS) family (TC 2.A.1.6) family. (500 aa)
tsrMethyl-accepting chemotaxis protein I, serine sensor receptor; Receptor for the attractant L-serine and related amino acids. Is also responsible for chemotaxis away from a wide range of repellents, including leucine, indole, and weak acids. (551 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
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