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
rnhCRibonuclease HIII; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids; Belongs to the RNase HII family. RnhC subfamily. (313 aa)    
Predicted Functional Partners:
rnhB
Ribonuclease HII; Endonuclease that specifically degrades the RNA of RNA-DNA hybrids; Belongs to the RNase HII family.
  
 
 0.992
ypdQ
Putative RNA binding protein; Not known; does not have RNase H activity; Belongs to the RNase H family. EbsB subfamily.
   
  
 0.918
ypeP
Ribonuclease; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme.
  
  
 0.806
rnmV
Ribonuclease M5; Required for correct processing of both the 5' and 3' ends of 5S rRNA precursor. Cleaves both sides of a double-stranded region yielding mature 5S rRNA in one step. Releases 5'-phosphoryl and 3'- hydroxy termini.
      
 0.796
yshB
Putative integral membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component.
  
  
 0.761
yshE
Putative integral inner membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pm: putative membrane component.
     
 0.746
ypcP
5'3'-exonuclease; 5'-3' exonuclease acting preferentially on double-stranded DNA.
   
  
 0.683
yshA
Conserved hypothetical protein; Activator of cell division through the inhibition of FtsZ GTPase activity, therefore promoting FtsZ assembly into bundles of protofilaments necessary for the formation of the division Z ring. It is recruited early at mid-cell but it is not essential for cell division (By similarity); Belongs to the ZapA family. Type 2 subfamily.
  
  
 0.672
recU
Holliday junction resolvase; Has at least 2 separable functions; Holliday junction resolution with generation of monomeric chromosomes, and modulation of RecA activity. Endonuclease that resolves Holliday junction intermediates in genetic recombination. Cleaves mobile four-strand junctions by introducing symmetrical nicks in paired strands. Promotes annealing of linear ssDNA with homologous dsDNA. Required for DNA repair, homologous recombination and chromosome segregation. Partially inhibits the hydrolysis of dATP or rATP by RecA. Holliday junction resolution is stimulated by RuvB.
  
   
 0.668
polX
DNA polymerase/3'-5' exonuclease X; Strictly DNA-template-directed DNA polymerase, preferentially acting on DNA structures containing gaps from one to a few nucleotides and bearing a phosphate group at the 5' end of the downstream DNA. The fact that PolX is able to conduct filling of a single-nucleotide gap, allowing further sealing of the resulting nick by a DNA ligase, points to a putative role in base excision repair (BER) during the B.subtilis life cycle. Moreover, also possesses a 3'-5' exonuclease activity able to edit unpaired 3'-termini in a gapped DNA substrate and likely invo [...]
  
  
 0.602
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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