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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
ypbGPutative phosphoesterase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (259 aa)    
Predicted Functional Partners:
ypuA
Putative exported protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative factor.
   
  
 0.880
disA
Diadenylate cyclase; Participates in a DNA-damage check-point that is active prior to asymmetric division when DNA is damaged. Forms globular foci that rapidly scan along the chromosomes during sporulation, searching for lesions. Its ability to scan through the chromosome rapidly is due to its non-specific DNA- binding. When a lesion is present, DisA pauses at the lesion site. This triggers a cellular response that culminates in a temporary block in sporulation initiation. It is required, at least partially, to inhibit the activity of the transcription factor spo0A, which controls, amo [...]
   
  
 0.780
yraA
General stress protein; Functions in the protection against aldehyde-stress, possibly by degrading damaged proteins.
  
  
 0.727
ltaSA
Exported glycerol phosphate lipoteichoic acid synthetase and anion-binding protein; Catalyzes the polymerization of lipoteichoic acid (LTA) polyglycerol phosphate, a reaction that presumably uses phosphatidylglycerol (PG) as substrate.
  
  
 0.726
ydaH
Putative integral inner membrane protein; Involved in peptidoglycan biosynthesis. Transports lipid- linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane. May serve as a defense mechanism against naturally occurring MurJ antagonists.
   
  
 0.711
yqjL
Putative hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
   
    0.688
radC
Putative DNA repair protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pf: putative factor.
   
  
 0.664
spxA
Redox-sensitive regulator enzyme; Interferes with activator-stimulated transcription by interaction with the RNA polymerase alpha-CTD. May function to globally reduce transcription of genes involved in growth- and development- promoting processes and to increase transcription of genes involved in thiol homeostasis, during periods of extreme stress. Negatively affects competence and sporulation. Its degradation by the MecA/ClpXP complex is needed for competence development; Belongs to the ArsC family. Spx subfamily.
   
  
 0.659
bcrC
Undecaprenyl pyrophosphate phosphatase; Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin; Belongs to the BcrC/YbjG family.
  
  
 0.615
murB
UDP-N-acetylenolpyruvoylglucosamine reductase; Cell wall formation.
   
    0.602
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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