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
AEM79619.1KEGG: tbo:Thebr_0368 translation elongation factor Tu; TIGRFAM: Translation elongation factor EFTu/EF1A, bacterial/organelle; Small GTP-binding protein; PFAM: Protein synthesis factor, GTP-binding; Translation elongation factor EFTu/EF1A, C-terminal; Translation elongation factor EFTu/EF1A, domain 2. (400 aa)    
Predicted Functional Partners:
AEM78408.1
PFAM: NADH:ubiquinone oxidoreductase, 51kDa subunit; Sucraseferredoxin-like; Soluble ligand binding domain; NADH ubiquinone oxidoreductase, F subunit, iron sulphur binding; 4Fe-4S ferredoxin, iron-sulphur binding, subgroup; KEGG: tbo:Thebr_1492 NADH dehydrogenase (quinone).
   
 
 0.979
tsf
Elongation factor Ts; Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF- Tu.GTP complex up to the GTP hydrolysis stage on the ribosome. Belongs to the EF-Ts family.
   
 0.973
rplK
Ribosomal protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
 
 0.973
rpmG
PFAM: Ribosomal protein L33; manually curated; TIGRFAM: Ribosomal protein L33; KEGG: tbo:Thebr_0369 50S ribosomal protein L33; HAMAP: Ribosomal protein L33; Belongs to the bacterial ribosomal protein bL33 family.
  
 0.972
rpsJ
30S ribosomal protein S10; Involved in the binding of tRNA to the ribosomes. Belongs to the universal ribosomal protein uS10 family.
 
 0.970
rplF
Ribosomal protein L6; This protein binds to the 23S rRNA, and is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center; Belongs to the universal ribosomal protein uL6 family.
  
 
 0.968
rplA
Ribosomal protein L1; Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release.
  
 0.966
rpsL
Ribosomal protein S12; Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit.
  
 0.963
rplP
50S ribosomal protein L16; Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs; Belongs to the universal ribosomal protein uL16 family.
  
 0.962
rplV
Ribosomal protein L22; The globular domain of the protein is located near the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that lines the wall of the exit tunnel in the center of the 70S ribosome.
  
 0.962
Your Current Organism:
Thermoanaerobacter wiegelii
NCBI taxonomy Id: 697303
Other names: T. wiegelii Rt8.B1, Thermoanaerobacter wiegelii Rt8.B1, Thermoanaerobacter wiegelii str. Rt8.B1, Thermoanaerobacter wiegelii strain Rt8.B1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.