STRINGSTRING
STRING protein interaction network
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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
motBFlagellar motor protein MotB; Derived by automated computational analysis using gene prediction method: Protein Homology. (339 aa)    
Predicted Functional Partners:
motA
Flagellar motor stator protein MotA; With MotB forms the ion channels that couple flagellar rotation to proton/sodium motive force across the membrane and forms the stator elements of the rotary flagellar machine; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.990
AOI81130.1
Chemotaxis protein CheA; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.966
flhC
Transcriptional regulator; 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; Belongs to the FlhC family.
  
 0.955
cheZ
Protein phosphatase CheZ; Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P).
 
  
 0.955
AOI84565.1
Flagellar motor stator protein MotA; With MotB forms the ion channels that couple flagellar rotation to proton/sodium motive force across the membrane and forms the stator elements of the rotary flagellar machine; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.953
flgK
Flagellar biosynthesis protein FlgK; With FlgL acts as a hook filament junction protein to join the flagellar filament to the hook; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.940
cheW
Chemotaxis protein CheW; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.926
flgH
Flagellar biosynthesis protein FlgH; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
 
  
 0.901
FliF
Flagellar M-ring protein FliF; The M ring may be actively involved in energy transduction. Belongs to the FliF family.
 
  
 0.898
flhD
Transcriptional regulator; 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; Belongs to the FlhD family.
 
  
 0.888
Your Current Organism:
Burkholderia cepacia
NCBI taxonomy Id: 292
Other names: ATCC 25416, B. cepacia, Burkholderia cepacia genomovar I, Burkholderia sp. Bp7081, Burkholderia sp. Bp7091, Burkholderia sp. Bp7098, Burkholderia sp. Bp7108, Burkholderia sp. Bp7432, Burkholderia sp. LK29, Burkholderia sp. NCIM 5465, CCUG 12691, CCUG 13226, CFBP 2227, CIP 80.24, DSM 7288, ICMP 5796, IFO 14074, JCM 5964, NBRC 14074, NCCB 76047, NCPPB 2993, NCTC 10743, NRRL B-14810, Pseudomonas cepacia, Pseudomonas kingii, Pseudomonas multivorans, strain 717-ICPB 25, strain Ballard 717
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