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
infCTranslation initiation factor IF-3; IF-3 binds to the 30S ribosomal subunit and shifts the equilibrum between 70S ribosomes and their 50S and 30S subunits in favor of the free subunits, thus enhancing the availability of 30S subunits on which protein synthesis initiation begins. (174 aa)    
Predicted Functional Partners:
rplT
Large subunit ribosomal protein L20; Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit.
  
 0.997
rpsK
SSU ribosomal protein S11P; Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine- Dalgarno cleft in the 70S ribosome; Belongs to the universal ribosomal protein uS11 family.
  
 
 0.994
rpsG
Small subunit ribosomal protein S7; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit. Is located at the subunit interface close to the decoding center, probably blocks exit of the E-site tRNA; Belongs to the universal ribosomal protein uS7 family.
   
 
 0.994
rpsM
Small subunit ribosomal protein S13; Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. In the 70S ribosome it contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; these bridges are implicated in subunit movement. Contacts the tRNAs in the A and P-sites. Belongs to the universal ribosomal protein uS13 family.
   
 
 0.989
rpmI
Large subunit ribosomal protein L35; Belongs to the bacterial ribosomal protein bL35 family.
  
  
 0.985
rpsS
SSU ribosomal protein S19P; Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
   
 
 0.982
rpsJ
SSU ribosomal protein S10P; Involved in the binding of tRNA to the ribosomes. Belongs to the universal ribosomal protein uS10 family.
   
 
 0.979
rpsF
Small subunit ribosomal protein S6; Binds together with S18 to 16S ribosomal RNA.
  
 
 0.979
rpsC
Small subunit ribosomal protein S3; Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation; Belongs to the universal ribosomal protein uS3 family.
   
 
 0.978
rpsL
SSU ribosomal protein S12P; 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.
   
 
 0.978
Your Current Organism:
Pilibacter termitis
NCBI taxonomy Id: 263852
Other names: CCUG 49613, P. termitis, Pilibacter termitis Higashiguchi et al. 2006, gut bacterium 1 of Coptotermes formosanus, strain TI-1
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.