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
yrrSConserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 14679248. (233 aa)    
Predicted Functional Partners:
pbpI
Penicillin-binding protein PBP4B; Penicillin-binding protein with an unknown catalytic activity. Penicillin-binding proteins (PBPs) function in the late steps of murein biosynthesis. Beta-lactamase inactivates the PBPs by acylating an essential serine residue in the active site of these proteins, thereby interrupting normal cell wall synthesis; Belongs to the transpeptidase family.
  
 
 0.985
ypbE
Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 16855244.
   
 
 0.949
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.
  
 
 0.890
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.
  
   
 0.812
mreD
Cell-shape determining protein; Involved in formation of the rod shape of the cell. May also contribute to regulation of formation of penicillin-binding proteins (By similarity).
  
     0.761
atpI
ATP synthase (subunit i); A possible function for this protein is to guide the assembly of the membrane sector of the ATPase enzyme complex; Belongs to the bacterial AtpI family.
  
     0.754
ysoA
Putative hydrolase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme.
  
     0.745
walH
Regulator of YycFG; Together with YycI, regulates the activity of the two- component system WalR/WalK.
  
     0.743
spoVIF
Sporulation-specific protein needed for heat resistance; Transcription factor involved in spore coat assembly and spore resistance. Regulates the transcription of at least cgeA, cotG and cotS.
  
     0.736
comN
Post-transcriptional regulator; Required for post-transcription initiation control of the comE operon. Promotes the accumulation of its target comE mRNA to septal and polar sites.
  
     0.730
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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