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
tigTrigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily. (457 aa)    
Predicted Functional Partners:
rpsB
PFAM: Ribosomal protein S2; TIGRFAM: ribosomal protein S2, bacterial type; COGs: COG0052 Ribosomal protein S2; InterPro IPR018130: IPR001865: IPR005706; KEGG: tai:Taci_0742 ribosomal protein S2; PFAM: ribosomal protein S2; SPTR: 30S ribosomal protein S2; TIGRFAM: ribosomal protein S2; Belongs to the universal ribosomal protein uS2 family.
  
 
 0.986
rplC
LSU ribosomal protein L3P; One of the primary rRNA binding proteins, it binds directly near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit; Belongs to the universal ribosomal protein uL3 family.
  
 
 0.984
rplM
LSU ribosomal protein L13P; This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly.
   
 
 0.983
rplD
LSU ribosomal protein L4P; Forms part of the polypeptide exit tunnel.
 
 
 0.982
rpsG
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.
  
 
 0.980
rpsJ
SSU ribosomal protein S10P; Involved in the binding of tRNA to the ribosomes. Belongs to the universal ribosomal protein uS10 family.
  
 
 0.980
rplB
Ribosomal protein L2; One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family.
  
 
 0.979
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.
 
 
 0.978
rpsK
30S ribosomal protein S11; 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.
  
 
 0.974
rpsC
SSU ribosomal protein S3P; 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.
  
 
 0.973
Your Current Organism:
Thermovirga lienii
NCBI taxonomy Id: 580340
Other names: T. lienii DSM 17291, Thermovirga lienii DSM 17291, Thermovirga lienii str. DSM 17291, Thermovirga lienii strain DSM 17291
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.