close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
EF_1978DNA-3-methyladenine glycosylase; Identified by match to PFAM protein family HMM PF02245; Belongs to the DNA glycosylase MPG family. (229 aa)    
Predicted Functional Partners:
EF_1977
Conserved hypothetical protein; Identified by Glimmer2; putative.
       0.884
prmA
Ribosomal protein L11 methyltransferase; Methylates ribosomal protein L11; Belongs to the methyltransferase superfamily. PrmA family.
     
 0.879
EF_1975
Conserved hypothetical protein TIGR00046; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
       0.875
relA
GTP pyrophosphokinase; In eubacteria ppGpp (guanosine 3'-diphosphate 5-' diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance.
  
    0.795
EF_1979
ATPase, AAA family; Similar to GP:10173873; identified by sequence similarity; putative.
     
 0.772
exoA
Exodeoxyribonuclease; Similar to GB:D10704, SP:P35790, and PID:219541; identified by sequence similarity; putative.
    
 0.718
dtd
Conserved hypothetical protein TIGR00256; An aminoacyl-tRNA editing enzyme that deacylates mischarged D-aminoacyl-tRNAs. Also deacylates mischarged glycyl-tRNA(Ala), protecting cells against glycine mischarging by AlaRS. Acts via tRNA- based rather than protein-based catalysis; rejects L-amino acids rather than detecting D-amino acids in the active site. By recycling D- aminoacyl-tRNA to D-amino acids and free tRNA molecules, this enzyme counteracts the toxicity associated with the formation of D-aminoacyl- tRNA entities in vivo and helps enforce protein L-homochirality. Belongs to the [...]
  
    0.711
EF_0659
Phage SPO1 DNA polymerase-related protein, putative; Identified by match to PFAM protein family HMM PF03167.
 
   
 0.589
nth
Endonuclease III; DNA repair enzyme that has both DNA N-glycosylase activity and AP-lyase activity. The DNA N-glycosylase activity releases various damaged pyrimidines from DNA by cleaving the N-glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The AP-lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'- phosphate.
  
  
 0.449
EF_0796
Type 2 phosphatidic acid phosphatase family protein; Similar to SP:Q05384, and PID:581543; identified by sequence similarity; putative.
 
  
 0.423
Your Current Organism:
Enterococcus faecalis V583
NCBI taxonomy Id: 226185
Other names: E. faecalis V583, Enterococcus faecalis str. V583, Enterococcus faecalis strain V583
Server load: medium (48%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.