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
ylmAPutative ABC transporter (ATP-binding protein); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative transporter. (264 aa)    
Predicted Functional Partners:
ycbM
Two-component sensor histidine kinase [YcbL]; Member of the two-component regulatory system YcbM/YcbL. Probably activates YcbL by phosphorylation.
      
 0.916
dppA
D-alanyl-aminopeptidase; Hydrolyzes N-terminal residues in D-amino acid containing peptides. Among the tested substrates, the highest activities are with D-Ala-D-Ala and D-Ala-Gly-Gly. The physiological role is not clear; Belongs to the peptidase M55 family.
   
  
 0.767
frlB
fructoselysine-6-P-deglycase; Catalyzes the conversion of a range of fructosamine 6- phosphates to glucose 6-phosphate and a free amino acid.
   
  
 0.764
kapB
Factor required for KinB signal transduction and activation of the phosphorelay to sporulation; May play a role in the activation or the expression of KinB.
   
  
 0.687
ilvA
Threonine dehydratase; Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2- ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA (By similarity).
 
    0.619
ecfA
Energizing coupling factor of ABC influx transporter (ATP-binding protein); ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
  
 
 
0.581
ilvD
Dihydroxy-acid dehydratase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the IlvD/Edd family.
 
    0.572
ecfAB
Energizing coupling factor of ABC influx transporter (ATP-binding protein); ATP-binding (A) component of a common energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates.
  
 
 
0.569
yobR
Putative acetyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the acetyltransferase family.
  
    0.568
thiW
Thiamine ABC transporter (ATP-binding protein); Part of the ABC transporter complex YkoCDEF that could transport hydroxymethylpyrimidine (HMP) and/or thiamine. Could also transport other HMP-containing products. Responsible for energy coupling to the transport system (Probable).
  
 
 
0.566
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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