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
rlmA23S rRNA m(1)G745 methyltransferase, SAM-dependent; Specifically methylates the guanosine in position 745 of 23S rRNA. (269 aa)    
Predicted Functional Partners:
rlmB
23S rRNA mG2251 2'-O-ribose methyltransferase, SAM-dependent; Specifically methylates the ribose of guanosine 2251 in 23S rRNA.
      
 0.815
trmH
tRNA mG18-2'-O-methyltransferase, SAM-dependent; Catalyzes the 2'-O methylation of guanosine at position 18 in tRNA. Type II methylase, which methylates only a subset of tRNA species; Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family.
   
  
 0.796
trmL
tRNA Leu mC34,mU34 2'-O-methyltransferase, SAM-dependent; Methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNA(Leu)(CmAA) and tRNA(Leu)(cmnm5UmAA). Catalyzes the methyl transfer from S-adenosyl-L-methionine to the 2'-OH of the wobble nucleotide. Recognition of the target requires a pyridine at position 34 and N(6)-(isopentenyl)-2-methylthioadenosine at position 37.
     
 0.765
ftsI
Transpeptidase involved in septal peptidoglycan synthesis; Essential cell division protein that catalyzes cross-linking of the peptidoglycan cell wall at the division septum. Required for localization of FtsN. Belongs to the transpeptidase family. FtsI subfamily.
 
  
 0.707
cspC
Stress protein, member of the CspA-family; Cold shock protein; Protein involved in transcription activator activity, transcription and response to temperature stimulus.
    
 0.706
rlmH
23S rRNA m(3)Psi1915 pseudouridine methyltransferase, SAM-dependent; Specifically methylates the pseudouridine at position 1915 (m3Psi1915) in 23S rRNA. Specific for fully assembled 70S ribosomes. Belongs to the RNA methyltransferase RlmH family.
   
  
 0.674
rlmJ
23S rRNA m(6)A2030 methyltransferase, SAM-dependent; Specifically methylates the adenine in position 2030 of 23S rRNA. Nascent 23S rRNA seems to be the natural substrate. Appears to be not necessary for ribosome assembly. Required for the utilization of extracellular DNA as the sole source of carbon and energy. Belongs to the RlmJ family.
      
 0.594
yobF
DUF2527 family heat-induced protein.
     
 0.588
rlmL
23S rRNA m(2)G2445 and m(7)G2069 methyltransferases, SAM-dependent; Specifically methylates the guanine in position 2445 (m2G2445) and the guanine in position 2069 (m7G2069) of 23S rRNA. Methylation occurs before assembly of 23S rRNA into 50S subunits. Belongs to the methyltransferase superfamily. RlmKL family.
   
  
 0.547
rsmE
16S rRNA m(3)U1498 methyltransferase, SAM-dependent; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
     
 0.547
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.