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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
rsmB16S rRNA methyltransferase; Specifically methylates the cytosine at position 967 (m5C967) of 16S rRNA. (451 aa)    
Predicted Functional Partners:
fmt
methionyl-tRNA formyltransferase; Attaches a formyl group to the free amino group of methionyl- tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus; Belongs to the Fmt family.
 
  
 0.998
trmG
23S rRNA (adenine(2503)-C2)-methyltransferase; Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity; Belongs to the radical SAM superfamily. RlmN family.
  
  
 0.918
trkA
Involved in potassium uptake; found to be peripherally associated with the inner membrane in Escherichia coli; contains an NAD-binding domain; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
   0.918
ligA
Aromatic ring-opening dioxygenase LigA; 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; Belongs to the NAD-dependent DNA ligase family. LigA subfamily.
  
  
 0.856
truB
Pseudouridine synthase; Responsible for synthesis of pseudouridine from uracil-55 in the psi GC loop of transfer RNAs; Belongs to the pseudouridine synthase TruB family. Type 1 subfamily.
 
 
 0.849
pheT
phenylalanine--tRNA ligase subunit beta; Catalyzes a two-step reaction, first charging a phenylalanine molecule by linking its carboxyl group to the alpha-phosphate of ATP, followed by transfer of the aminoacyl-adenylate to its tRNA; forms a tetramer of alpha(2)beta(2); binds two magnesium ions per tetramer; type 2 subfamily; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the phenylalanyl-tRNA synthetase beta subunit family. Type 1 subfamily.
  
  
 0.846
rpsA
30S ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence.
  
 
 0.835
nusA
Transcription elongation factor NusA; Participates in both transcription termination and antitermination.
  
 
 0.825
rpsJ
30S ribosomal protein S10; Involved in the binding of tRNA to the ribosomes. Belongs to the universal ribosomal protein uS10 family.
   
 
 0.824
rrmJ
23S rRNA methyltransferase; Specifically methylates the uridine in position 2552 of 23S rRNA at the 2'-O position of the ribose in the fully assembled 50S ribosomal subunit.
 
 
 0.820
Your Current Organism:
Aggregatibacter actinomycetemcomitans
NCBI taxonomy Id: 714
Other names: A. actinomycetemcomitans, ATCC 33384, Actinobacillus (Haemophilus) actinomycetemcomitans, Actinobacillus actinomycetemcomitans, Bacterium acetinomycetum comitans, Bacterium actinomycetem comitans, Bacterium comitans, CCUG 13227, CIP 52.106, DSM 8324, Haemophilus actinomycetemcomitans, Haemophilus actinomyceticomitans, NCTC 9710
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