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
liaFIntegral inner membrane protein; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type m: membrane component. (241 aa)    
Predicted Functional Partners:
liaR
Two-component response regulator [YvqE] responding to cell wall stress; Member of the two-component regulatory system LiaS/LiaR probably involved in response to a subset of cell wall-active antibiotics that interfere with the lipid II cycle in the cytoplasmic membrane (bacitracin, nisin, ramoplanin and vancomycin). Seems also involved in response to cationic antimicrobial peptides and secretion stress. LiaR regulates the transcription of the liaIHGFSR operon.
 
  
 0.999
liaS
Two-component sensor histidine kinase [YvqC] sensing cell wall stress; Member of the two-component regulatory system LiaS/LiaR probably involved in response to a subset of cell wall-active antibiotics that interfere with the lipid II cycle in the cytoplasmic membrane (bacitracin, nisin, ramoplanin and vancomycin). Seems also involved in response to cationic antimicrobial peptides and secretion stress. Activates probably LiaR by phosphorylation.
 
  
 0.999
liaG
Conserved hypothetical protein (response to antibiotic stress); Evidence 1a: Function experimentally demonstrated in the studied strain; PubMedId: 15273097, 16816187.
 
  
 0.999
liaH
Modulator of liaIHGFSR (yvqIHGFEC) operon expression; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type f: factor.
 
  
 0.994
liaI
Permease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type t: transporter.
  
  
 0.985
yhdW
Putative glycerophosphodiester phosphodiesterase; Glycerophosphoryl diester phosphodiesterase hydrolyzes deacylated phospholipids to sn-glycerol 3-phosphate (G3P) and the corresponding alcohols.
   
  
 0.888
yqiK
Putative glycerophosphodiester phosphodiesterase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme.
      
 0.849
yvlB
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
 
  
 0.820
mprF
Phosphatidylglycerol lysyltransferase involved in lysinylation of phospholipids; Catalyzes the transfer of a lysyl group from L-lysyl- tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects B.subtilis against its own CAMPs and against those produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with po [...]
   
  
 0.767
glpQA
Glycerophosphoryl diester phosphodiesterase; Glycerophosphoryl diester phosphodiesterase hydrolyzes deacylated phospholipids to G3P and the corresponding alcohols.
      
 0.752
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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