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
yrpGPutative oxidoreductase; 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. Aldo/keto reductase 2 subfamily. (326 aa)    
Predicted Functional Partners:
ydeA
Putative enzyme; 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 peptidase C56 family.
  
  
 0.788
sigZ
RNA polymerase ECF(extracytoplasmic function)-type sigma factor (sigma-Z); Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released.
  
  
 0.751
yhaU
Transporter involved in K+ efflux; Potassium/proton antiporter that mediates the efflux of potassium ions from the cell. Can also mediate rubidium/proton antiport, but has no permeability for sodium or lithium ions. In the absence of KhtT, does not have antiport activity, but can catalyze potassium efflux. Involved in protection of the cell from methylglyoxal, a toxic by-product of glycolysis, via activation by S-lactoyl-BSH of the antiporter activity, leading to cytoplasmic acidification and methylglyoxal resistance ; Belongs to the monovalent cation:proton antiporter 2 (CPA2) transpo [...]
      
 0.680
pksJ
Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism.
  
 0.517
yvgN
Glyoxal/methylglyoxal reductase; Reduces glyoxal and methylglyoxal (2-oxopropanal). Is not involved in the vitamin B6 biosynthesis; Belongs to the aldo/keto reductase family.
 
 
0.515
yqkF
NADPH-dependent aldo-keto reductase; Evidence 2b: Function of strongly homologous gene; Product type e: enzyme; Belongs to the aldo/keto reductase family. Aldo/keto reductase 2 subfamily.
  
   
0.449
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.
 
 
0.437
gsiB
General stress protein; Involved in an adaptive response to nutrient deprivation other than sporulation.
      
 0.424
iolS
Aldo-keto reductase; In vitro, is able to reduce the standard aldo-keto reductase (AKR) substrates DL-glyceraldehyde, D-erythrose and methylglyoxal in the presence of NADPH, albeit with poor efficiency. Shows only trace activity with benzaldehyde and butyraldehyde. Is unable to oxidize myo- inositol with either NADP(+) or NAD(+) as a cosubstrate and also does not use glucose, 2-pyridine carboxyaldehyde, fructose, xylose and succinyl semialdehyde as a substrate. The physiological function of this enzyme is not clear. Does not seem to be necessary for inositol catabolism ; Belongs to the [...]
 
   
0.421
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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