STRINGSTRING
qoxC qoxC yheG yheG adeC adeC flgD flgD fliM fliM cheY cheY fliR fliR flhB flhB flhA flhA cheW cheW alsT alsT cheR cheR iolG iolG
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:
qoxCCytochrome aa3-600 quinol oxidase (subunit III); Catalyzes quinol oxidation with the concomitant reduction of oxygen to water. Major component for energy conversion during vegetative growth (By similarity). (204 aa)
yheGPutative NADH-flavin oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (206 aa)
adeCAdenine deaminase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the metallo-dependent hydrolases superfamily. Adenine deaminase family. (577 aa)
flgDFlagellar hook assembly protein; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type pf: putative factor; Belongs to the FlgD family. (140 aa)
fliMFlagellar motor switching and energizing component; One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation; Belongs to the FliM family. (332 aa)
cheYRegulator of chemotaxis and motility; Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming. (120 aa)
fliRComponent of the flagellar export machinery; Role in flagellar biosynthesis; Belongs to the FliR/MopE/SpaR family. (259 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)
flhAComponent of the flagellar export machinery; Involved in the export of flagellum proteins. (677 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)
alsTAmino acid carrier protein; Evidence 2b: Function of strongly homologous gene; Product type t: transporter; Belongs to the alanine or glycine:cation symporter (AGCS) (TC 2.A.25) family. (465 aa)
cheRMethyl-accepting chemotaxis proteins (MCPs) methyltransferase; Methylation of the membrane-bound methyl-accepting chemotaxis proteins (MCP) to form gamma-glutamyl methyl ester residues in MCP. CheR is responsible for the chemotactic adaptation to repellents. (256 aa)
iolGMyo-inositol 2-dehydrogenase/D-chiro-inositol 3-dehydrogenase; Involved in the oxidation of myo-inositol (MI) and D-chiro- inositol (DCI) to 2-keto-myo-inositol (2KMI or 2-inosose) and 1-keto-D- chiro-inositol (1KDCI), respectively. Can also use D-glucose and D- xylose, and shows a trace of activity with D-ribose and D-fructose. (344 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
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