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
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:
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.
  
  
 0.973
pcrA
ATP-dependent DNA helicase; DNA helicase used for plasmid rolling-circle replication and also involved in UV repair.
  
  
 0.972
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 [...]
 
  
 0.967
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.
  
  
 0.890
pbpA
Transpeptidase (penicillin-binding protein 2A); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.
  
    0.765
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
gpsB
Cell division protein; Divisome component that associates with the complex late in its assembly, after the Z-ring is formed, and is dependent on DivIC and PBP2B for its recruitment to the divisome. Together with EzrA, is a key component of the system that regulates PBP1 localization during cell cycle progression. Its main role could be the removal of PBP1 from the cell pole after pole maturation is completed. Also contributes to the recruitment of PBP1 to the division complex. Not essential for septum formation; Belongs to the GpsB family.
  
    0.741
yslB
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
  
     0.734
yneF
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function.
  
    0.719
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
Server load: low (30%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.