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
yoxDPutative oxido-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 short-chain dehydrogenases/reductases (SDR) family. (238 aa)    
Predicted Functional Partners:
dltA
D-alanine:D-alanyl-carrier protein ligase; Catalyzes the first step in the D-alanylation of lipoteichoic acid (LTA), the activation of D-alanine and its transfer onto the D- alanyl carrier protein (Dcp) DltC. In an ATP-dependent two-step reaction, forms a high energy D-alanyl-AMP intermediate, followed by transfer of the D-alanyl residue as a thiol ester to the phosphopantheinyl prosthetic group of the Dcp. D-alanylation of LTA plays an important role in modulating the properties of the cell wall in Gram-positive bacteria, influencing the net charge of the cell wall. Belongs to the ATP [...]
    
 0.923
srfAC
Surfactin synthetase; Probably activates a leucine.
 
  
 0.906
ppsE
Plipastatin synthetase; This protein is a multifunctional enzyme, able to activate and polymerize the amino acid Ile as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The activation sites for this amino acid consist of individual domains; Belongs to the ATP-dependent AMP-binding enzyme family.
 
  
 0.802
racX
Amino acid racemase; Amino-acid racemase able to utilize a broad range of substrates. Preferentially catalyzes the epimerization of LL- diaminopimelate, as well as the racemization of D-lysine, L-arginine, L-ornithine, L-lysine and D-arginine. Has lower activity against D- ornithine, L-histidine, L-alanine, L-tyrosine, L-phenylalanine, L- serine, L-glutamine, L-methionine, L-asparagine and L-homoserine. Has weak activity against L-norleucine, L-aminobutyric acid and L- norvaline. Has no activity toward nine L-amino acids (Thr, Glu, Asp, Val, Leu, Ile, Trp, Cit and Aad). D-amino acids m [...]
      
 0.769
ypuA
Putative exported protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative factor.
   
  
 0.759
yceH
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; Belongs to the TelA family.
      
 0.752
nadE
Ammonium-dependent NAD+ synthetase; Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
   
  
 0.694
liaH
Modulator of liaIHGFSR (yvqIHGFEC) operon expression; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor.
      
 0.680
pspA
Phage shock protein A homolog; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type h: extrachromosomal origin.
      
 0.600
yceC
Putative stress adaptation protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pf: putative factor; Belongs to the CAPAB/TerDEXZ family.
      
 0.573
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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