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
lutAIron-sulfur oxidase component; Is essential for L-lactate degradation and allows cells to grow with lactate as the sole carbon source. May also allow cells to utilize an alternative carbon source during biofilm formation, since it contributes to the formation of architecturally complex communities when lactate is present. (238 aa)    
Predicted Functional Partners:
lutC
Component of an iron-sulfur oxidase; Is essential for L-lactate degradation and allows cells to grow with lactate as the sole carbon source. May also allow cells to utilize an alternative carbon source during biofilm formation, since it contributes to the formation of architecturally complex communities when lactate is present.
 
 0.999
lutB
Component of an iron-sulfur oxidase; Is essential for L-lactate degradation and allows cells to grow with lactate as the sole carbon source. Has probably a role as an electron transporter during oxidation of L-lactate. May also allow cells to utilize an alternative carbon source during biofilm formation, since it contributes to the formation of architecturally complex communities when lactate is present.
 
 0.999
glcD
Glycolate oxidase subunit; Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is also able to oxidize D-lactate ((R)- lactate). Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown. Belongs to the FAD-binding oxidoreductase/transferase type 4 family.
  
 0.912
ytbE
Putative aldo/keto reductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the aldo/keto reductase family.
      
 0.845
yvfH
Putative lactate permease; Is the principal permease for the uptake of L-lactate in B.subtilis.
 
  
 0.726
yvfI
Putative transcriptional regulator (GntR family); Negatively regulates the transcription of the lutABC operon, which is required for L-lactate utilization. LutR activity is regulated by lactate, since presence of L-lactate, that probably binds to LutR, leads to derepression of the operon. Also appears to be essential for bacilysin biosynthesis.
 
  
 0.677
lctP
L-lactate permease; May play a role in L-lactate transport.
 
  
 0.658
maeA
NAD-dependent malic enzyme (conversion of malate into pyruvate); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.
     
 0.577
ydaD
Putative dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
   
  
 0.485
oxdC
Oxalate decarboxylase; Converts oxalate to formate and CO(2) in an O(2)-dependent reaction. Can also catalyze minor side reactions: oxalate oxidation to produce H(2)O(2), and oxalate-dependent, H(2)O(2)-independent dye oxidations.
      
 0.482
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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