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.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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[Homology]
Score
yerHPutative lipoprotein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; lipoprotein. (396 aa)    
Predicted Functional Partners:
pcrA
ATP-dependent DNA helicase; DNA helicase used for plasmid rolling-circle replication and also involved in UV repair.
  
  
 0.985
ligA
DNA ligase; DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
  
  
 0.983
pcrB
Heptaprenylglyceryl-phosphate synthase; Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond- formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales. To a much lesser extent, is also able to use geranyl diphosphate (GPP; C10) and geranylgeranyl diphosphate (GGPP; C20) as the prenyl donors, but not farnesyl pyrophosphate (FPP; C15). Ca [...]
 
  
 0.974
dnaB
Helicase loading protein; Probable component of primosome involved in the initiation of DNA replication. It is essential for both replication initiation and membrane attachment of the origin region of the chromosome and plasmid pUB110.
  
  
 0.887
gatA
glutamyl-tRNA(Gln) amidotransferase (subunit A); Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu- tRNA(Gln).
  
    0.818
gatC
glutamyl-tRNA(Gln) amidotransferase (subunit C); Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity); Belongs to the GatC family.
  
    0.810
gatB
glutamyl-tRNA(Gln) amidotransferase (subunit B); Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl- tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp- tRNA(Asn) or phospho-Glu-tRNA(Gln); Belongs to the GatB/GatE family. GatB subfamily.
  
    0.784
pbpA
Transpeptidase (penicillin-binding protein 2A); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.
  
    0.766
ezrA
Negative regulator of FtsZ ring formation; Negative regulator of FtsZ ring formation; modulates the frequency and position of FtsZ ring formation. Inhibits FtsZ ring formation at polar sites. Interacts either with FtsZ or with one of its binding partners to promote depolymerization.
  
     0.765
pbpH
Penicillin-binding enzyme for formation of rod-shaped peptidoglycan cell wall; Involved in the polymerization of peptidoglycan. Plays a redundant role with PBP2a in determining the rod shape of the cell during vegetative growth and spore outgrowth. Belongs to the transpeptidase family.
  
     0.761
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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