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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
yqhAPutative sulphate transporter YqhA. (279 aa)    
Predicted Functional Partners:
rsbT
Switch protein/serine-threonine kinase.
 
 
 0.990
rsbX
Serine phosphatase.
 
 
 0.934
rsbW
Switch protein/serine kinase and anti-sigma factor (inhibitory sigma-B binding protein); Negative regulator of sigma-B activity. Phosphorylates and inactivates its specific antagonist protein, RsbV. Upon phosphorylation of RsbV, RsbW is released and binds to sigma-B, thereby blocking its ability to form an RNA polymerase holoenzyme (E-sigma-B).
 
 
 0.915
fliY
Flagellar motor switch 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. Belongs to the FliN/MopA/SpaO family.
  
   0.896
spoIIAB
Anti-sigma factor (antagonist of sigma-F) and serine kinase; Binds to sigma F and blocks its ability to form an RNA polymerase holoenzyme (E-sigma F). Phosphorylates SpoIIAA on a serine residue. This phosphorylation may enable SpoIIAA to act as an anti- anti-sigma factor that counteracts SpoIIAB and thus releases sigma F from inhibition.
  
 
 0.879
rsbU
Serine phosphatase.
 
 
 0.862
flgB
Flagellar basal-body rod protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body.
   
    0.738
fliG
Flagellar motor switch protein; 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 FliG family.
  
   0.731
BL05341
Conserved hypothetical protein.
  
   0.720
fliF
Flagellar basal-body M-ring protein; The M ring may be actively involved in energy transduction. Belongs to the FliF family.
  
    0.664
Your Current Organism:
Bacillus licheniformis
NCBI taxonomy Id: 279010
Other names: B. licheniformis DSM 13 = ATCC 14580, Bacillus licheniformis ATCC 14580, Bacillus licheniformis ATCC 14580 = DSM 13, Bacillus licheniformis DSM 13, Bacillus licheniformis DSM 13 = ATCC 14580
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.