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 trg trg ycgR ycgR flhA flhA flhB flhB cheZ cheZ cheY cheY cheB cheB cheR cheR cheM cheM cheW cheW cheA cheA motB motB motA motA 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 STM2314 STM2314 STM3152 STM3152 aer aer tcp tcp 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.
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:
flgNFlagellar biosynthesis protein; Required for the efficient initiation of filament assembly. (140 aa)
flgManti-FliA factor; 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)
flgAFlagellar biosynthesis protein; 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 biosynthesis protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. (138 aa)
flgCFlagellar biosynthesis protein; Cell-proximal portion of basal-body rod; flagellar basal-body rod protein FLGC (putative proximal rod protein). (SW:FLGC_SALTY); Belongs to the flagella basal body rod proteins family. (134 aa)
flgDFlagellar biosynthesis protein; Required for flagellar hook formation. May act as a scaffolding protein; Belongs to the FlgD family. (232 aa)
flgEHook protein; Flagellar biosynthesis; flagellar hook protein flge. (SW:FLGE_SALTY); Belongs to the flagella basal body rod proteins family. (403 aa)
flgFFlagellar biosynthesis protein; Cell-proximal portion of basal-body rod; flagellar basal-body rod protein flgf (putative proximal rod protein). (SW:FLGF_SALTY); Belongs to the flagella basal body rod proteins family. (251 aa)
flgGFlagellar biosynthesis protein; Cell-distal portion of basal-body rod; flagellar basal-body rod protein flgg (distal rod protein). (SW:FLGG_SALTY); Belongs to the flagella basal body rod proteins family. (260 aa)
flgHFlagellar biosynthesis protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (232 aa)
flgIPutative flagella 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 biosynthesis protein; 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. (316 aa)
flgKHook-filament junction protein 1; Flagellar biosynthesis protein; flagellar hook-associated protein 1 (HAP1). (SW:FLGK_SALTY); Belongs to the flagella basal body rod proteins family. (553 aa)
flgLHook-filament junction protein; Flagellar biosynthesis protein; flagellar hook-associated protein 3 (HAP3) (hook-filament junctionprotein). (SW:FLGL_SALTY). (317 aa)
trgMethyl-accepting chemotaxis protein III; Ribose and galactose sensor receptor; similar to E. coli methyl-accepting chemotaxis protein III, ribose sensor receptor (AAC74503.1); Blastp hit to AAC74503.1 (546 aa), 79% identity in aa 6 - 526. (541 aa)
ycgRPutative inner membrane protein; Acts as a flagellar brake, regulating swimming and swarming in a bis-(3'-5') cyclic diguanylic acid (c-di-GMP)-dependent manner. Overexpression of this gene decreases swimming and swarming motility; those cells that are motile turn predominantly counterclockwise. The D- 118 mutant is still able to bind FliM but no longer affects motility upon overexpression. Binds 1 c-di-GMP dimer per subunit. (244 aa)
flhAFlagellar biosynthesis protein; Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin. (692 aa)
flhBPutative part of export apparatus for flagellar proteins; 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. (383 aa)
cheZChemotactic response protein; Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P). Acts on free CheY-P. Belongs to the CheZ family. (214 aa)
cheYChemotaxis regulator protein; 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. Shows autophosphatase activity which is enhanced by CheZ. (129 aa)
cheBMethyl esterase; 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 (By similarity). Belongs to the CheB family. (349 aa)
cheRGlutamate methyltransferase; Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. (288 aa)
cheMMethyl accepting chemotaxis protein II; Receptor for the attractant L-aspartate and related amino and dicarboxylic acids. Tar mediates taxis away from the repellents cobalt and nickel. Unlike in E.coli tar, it does not mediates maltose taxis. (553 aa)
cheWPurine-binding chemotaxis protein; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. (167 aa)
cheASensory histitine protein kinase; 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. (671 aa)
motBEnables flagellar motor rotation; MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity). (309 aa)
motAProton conductor component of motor; MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity). (295 aa)
fliZPutative regulator of FliA; May regulate sigma factor activity. (183 aa)
fliASigma F (sigma 28) factor of RNA polymerase; 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. May regulate the expression of genes involved in virulence. (239 aa)
fliCFlagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (495 aa)
fliDFilament 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. (467 aa)
fliSRepressor of class 3a and 3b operons (RflA activity); Flagellar biosynthesis; flagellar protein FLIS. (SW:FLIS_SALTY); Belongs to the FliS family. (135 aa)
fliTPossible export chaperone for FliD; 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. Belongs to the FliT family. (122 aa)
fliEFlagellar hook-basal body complex protein FLIE. (SW:FLIE_SALTY). (104 aa)
fliFBasal-body MS (membrane and supramembrane)-ring and collar protein; The M ring may be actively involved in energy transduction. (560 aa)
fliGFlagellar biosynthesis 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 (By similarity). (331 aa)
fliHFlagellar biosynthesis protein; Needed for flagellar regrowth and assembly. (235 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. (456 aa)
fliJFlagellar FliJ protein; Flagellar protein that affects chemotactic events. (147 aa)
fliKFlagellar hook-length control protein; Controls the length of the flagellar hook. (405 aa)
fliLFlagellar biosynthesis; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. (155 aa)
fliMFlagellar biosynthesis 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 (By similarity). (334 aa)
fliNFlagellar biosynthesis 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 (By similarity). Belongs to the FliN/MopA/SpaO family. (137 aa)
fliOFlagellar protein FLIO. (SW:FLIO_SALTY). (125 aa)
fliPFlagellar biosynthesis protein; Plays a role in the flagellum-specific transport system. (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)
fliRPutative flagellar biosynthetic protein; Role in flagellar biosynthesis; Belongs to the FliR/MopE/SpaR family. (264 aa)
STM2314Putative chemotaxis signal transduction protein; Similar to E. coli positive regulator of CheA protein activity (AAC74957.1); Blastp hit to AAC74957.1 (167 aa), 25% identity in aa 18 - 151. (333 aa)
STM3152Similar to E. coli methyl-accepting chemotaxis protein I, serine sensor receptor (AAC77311.1); Blastp hit to AAC77311.1 (551 aa), 43% identity in aa 1 - 551. (547 aa)
aerAerotaxis sensor receptor; Senses cellular redox state or proton motive force; similar to E. coli aerotaxis sensor receptor, flavoprotein (AAC76107.1); Blastp hit to AAC76107.1 (506 aa), 83% identity in aa 1 - 506. (506 aa)
tcpMethyl-accepting transmembrane citrate/phenol chemoreceptor; Acts as a receptor for citrate and mediates taxis away from phenol. Also mediates an attractant response to metal-citrate complexes. (547 aa)
tsrSerine sensor receptor; similar to E. coli methyl-accepting chemotaxis protein I, serine sensor receptor (AAC77311.1); Blastp hit to AAC77311.1 (551 aa), 86% identity in aa 1 - 551. (553 aa)
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
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