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
yhxAHypothetical protein; Essential for glycerol catabolism; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (450 aa)    
Predicted Functional Partners:
glpP
Glycerol-3-phosphate responding transcription antiterminator; Regulates expression of the glpD operon. In the presence of glycerol 3-phosphate (G3P) causes antitermination of transcription of glpD at the inverted repeat of the leader region to enhance its transcription. Binds and stabilizes glpD leader mRNA. May also regulate expression of the glpFK operon.
  
  
 0.974
bioB
Biotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism; Belongs to the radical SAM superfamily. Biotin synthase family.
 
  
 0.792
bioD
Dethiobiotin synthetase; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring.
  
 0.778
yhaR
Putative dehydratase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
   
  
 0.755
ycbU
Putative cysteine desulfurase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
   
  
 0.699
argB
N-acetylglutamate 5-phosphotransferase (acetylglutamate kinase); Catalyzes the ATP-dependent phosphorylation of N-acetyl-L- glutamate; Belongs to the acetylglutamate kinase family. ArgB subfamily.
   
 0.570
pksH
Dehydratase for polyketide biosynthesis; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. Probably catalyzes the dehydration of the (S)-3-hydroxy-3- methylglutaryl group attached to PksL.
      
 0.483
rnjA
Ribonuclease J1; An RNase that has endonuclease and 5'-3' exonuclease activity, playing a role in both rRNA and mRNA stability and degradation. Endonuclease activity can cleave within 4 nucleotides of the 5'-end of a triphosphorylated RNA. Endonuclease digestion by the RNase J1/J2 complex occurs at a different site and in some cases more efficiently than J1 or J2 alone. The exonuclease activity of the J1/J2 complex is highly processive on substrates longer than 5 nucleotides, on shorter substrates is distributive. Preferentially cleaves ssRNA, possibly in AU-rich regions. The 5'-exonuc [...]
      
 0.482
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.
  
  
 0.454
pksN
Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism.
  
  
 0.454
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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