STRINGSTRING
flgK flgK rplI rplI gapA gapA flhB flhB fliL fliL fliF fliF fliE fliE flgB flgB suhB suhB ohrR ohrR cspC cspC flgM flgM fliD fliD fadE fadE kinB kinB yrdQ yrdQ yqfG yqfG sodA sodA pstS pstS sodF sodF hfq hfq cheW cheW
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:
flgKFlagellar hook-filament junction; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; structure. (507 aa)
rplIRibosomal protein L9; Binds to the 23S rRNA. (149 aa)
gapAGlyceraldehyde-3-phosphate dehydrogenase; Involved in the glycolysis. Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3- bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG. (335 aa)
flhBComponent of the flagellar export machinery; May be involved in the export of flagellum proteins; Belongs to the type III secretion exporter family. (360 aa)
fliLFlagellar basal-body associated protein; Controls the rotational direction of flagella during chemotaxis; Belongs to the FliL family. (140 aa)
fliFFlagellar basal-body M-ring protein; The M ring may be actively involved in energy transduction. (536 aa)
fliEFlagellar basal body protein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type s: structure. (106 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. (129 aa)
suhBInositol monophosphatase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the inositol monophosphatase superfamily. (265 aa)
ohrRTranscriptional regulator sensing organic peroxides; Organic peroxide sensor. Represses the expression of the peroxide-inducible gene ohrA by cooperative binding to two inverted repeat elements. (147 aa)
cspCCold-shock protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor. (66 aa)
flgMAnti-sigma factor repressor of sigma(D)-dependent transcription; Allows the coupling of early and late flagellar synthesis through the repression of RNA polymerase sigma-D factor-dependent transcription. (88 aa)
fliDFlagellar hook-associated capping protein 2 (HAP2); 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 (By similarity); Belongs to the FliD family. (498 aa)
fadEacyl-CoA dehydrogenase (FAD dependent); Involved in the degradation of long-chain fatty acids. (594 aa)
kinBTwo-component sensor histidine kinase; Phosphorylates the sporulation-regulatory proteins spo0A and spo0F. Spo0F is required for the KinB activity. (428 aa)
yrdQPutative transcriptional regulator (LysR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator; Belongs to the LysR transcriptional regulatory family. (288 aa)
yqfGPutative metal-dependent hydrolase; Single strand-specific metallo-endoribonuclease involved in late-stage 70S ribosome quality control and in maturation of the 3' terminus of the 16S rRNA. (157 aa)
sodASuperoxide dismutase; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems; Belongs to the iron/manganese superoxide dismutase family. (202 aa)
pstSPhosphate ABC transporter (binding lipoprotein); Part of the ABC transporter complex PstSACB involved in phosphate import. (300 aa)
sodFSuperoxide dismutase; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. (281 aa)
hfqHfq RNA chaperone; RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs. Belongs to the Hfq family. (73 aa)
cheWModulation of CheA activity in response to attractants (chemotaxis); Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. CheV and CheW are involved in the coupling of the methyl-accepting chemoreceptors to the central two- component kinase CheA; they are both necessary for efficient chemotaxis. (156 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
Server load: low (12%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.