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
yqxHPutative holin; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (140 aa)    
Predicted Functional Partners:
yqxG
Putative phage-related lytic exoenzyme; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; To B.subtilis XkdY/XepA.
  
  
 0.963
cwlA
N-acetylmuramoyl-L-alanine amidase; Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation; Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
  
  
 0.945
xlyB
N-acetylmuramoyl-L-alanine amidase; Autolysins are involved in some important biological processes such as cell separation, cell-wall turnover, competence for genetic transformation, formation of the flagella and sporulation.
 
  
 0.859
rttM
Antitoxin inhibiting Rnase RttL; Antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the RNase activity of cognate toxin YobL, as well as its ability to inhibit growth upon expression in E.coli. Does not have antitoxin activity on other toxins with the LXG toxin domain.
      
 0.686
rttL
Phage toxin ribonuclease; Toxic component of a type II toxin-antitoxin (TA) system. The C-terminus (residues 449-600) has RNase activity, and inhibits growth upon expression in E.coli. In vitro RNase activity and in vivo growth inhibition are neutralized by cognate antitoxin YobK, but not by antitoxins specific to other toxins with the LXG domain.
      
 0.685
yqbO
Putative lytic transglycosylase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; To B.subtilis XkdO.
 
    0.685
rttG
Phage ribonuclease toxin; Toxic component of a type II toxin-antitoxin (TA) system. The C-terminus (residues 379-531) has RNase activity, and inhibits growth upon expression in E.coli. In vitro RNase activity and in vivo growth inhibition are neutralized by cognate antitoxin YqcF, but not by antitoxins specific to other toxins with the LXG domain.
      
 0.681
yqbP
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
 
     0.675
rttF
Antitoxin factor of ribonuclease toxin RttG; Antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the RNase activity of cognate toxin YqcG, as well as its ability to inhibit growth upon expression in E.coli. Does not have antitoxin activity on other toxins with the LXG toxin domain.
      
 0.633
yqbQ
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; To B.subtilis XkdQ.
 
    0.623
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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