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
ywbIPutative transcriptional regulator (LysR family); Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pr: putative regulator; Belongs to the LysR transcriptional regulatory family. (301 aa)    
Predicted Functional Partners:
ywbF
Putative sugar permease; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pt: putative transporter.
  
  
 0.902
cidA
Holin regulator of murein hydrolases; Increases the activity of extracellular murein hydrolases possibly by mediating their export via hole formation. Inhibited by the antiholin-like proteins LrgAB. In an unstressed cell, the LrgAB products probably inhibit the function of the CidA protein. When a cell is stressed by the addition of antibiotics or by other factors in the environment, CidA possibly oligomerizes within the bacterial cell membrane, creating lesions that disrupt the proton motive force, which in turn results in loss of cell viability. These lesions are also hypothesized to [...]
 
  
 0.832
thiM
Hydroxyethylthiazole kinase; Catalyzes the phosphorylation of the hydroxyl group of 4- methyl-5-beta-hydroxyethylthiazole (THZ).
  
  
 0.817
thiE
Thiamine-phosphate pyrophosphorylase; Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Is also able to use the 2-methoxy analog MeO-HMP-PP, as substrate in vitro, but not the 2-trifluoromethyl analog CF(3)-HMP-PP. Belongs to the thiamine-phosphate synthase family.
  
    0.813
ywbG
Anti-holin factor controlling activity of murein hydrolases; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; regulator.
 
   
 0.797
yclJ
Two-component response regulator [YclK]; Could be member of the two-component regulatory system YclK/YclJ.
  
  
 0.621
lytS
Two-component sensor histidine kinase [LytT]; Member of the two-component regulatory system LytS/LytT that probably regulates genes involved in cell wall metabolism.
      
 0.560
lytT
Two-component response regulator [LytS]; Member of the two-component regulatory system LytS/LytT that probably regulates genes involved in cell wall metabolism.
      
 0.485
lrgB
Antiholin factor; Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgA, with the holin-like protein CidA. The LrgAB and CidA proteins may affect the proton motive force of the membrane. May be involved in programmed cell death (PCD), possibly triggering PCD in response to antibiotics and environmental stresses; Belongs to the CidB/LrgB family. LrgB subfamily.
      
 0.481
efeM
Lipoprotein binding ferrous or ferric iron for transport; Involved in iron uptake; Belongs to the EfeM/EfeO family.
       0.472
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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