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
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. (479 aa)    
Predicted Functional Partners:
rplU
LSU ribosomal protein L21P; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family.
 
 
 0.970
rpsB
COGs: COG0052 Ribosomal protein S2; InterPro IPR001865: IPR018130: IPR005706; KEGG: psl:Psta_0952 ribosomal protein S2; PFAM: ribosomal protein S2; SPTR: Ribosomal protein S2; TIGRFAM: ribosomal protein S2; PFAM: Ribosomal protein S2; TIGRFAM: ribosomal protein S2, bacterial type; Belongs to the universal ribosomal protein uS2 family.
  
 
 0.968
rplV
LSU ribosomal protein L22P; 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.
 
 
 0.966
rplS
Ribosomal protein L19; This protein is located at the 30S-50S ribosomal subunit interface and may play a role in the structure and function of the aminoacyl-tRNA binding site.
 
 
 0.966
rpsD
SSU ribosomal protein S4P; One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit.
  
 
 0.965
rpsG
SSU ribosomal protein S7P; 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.
  
 
 0.964
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.
  
 
 0.963
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.
  
 
 0.962
rpsH
SSU ribosomal protein S8P; One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit; Belongs to the universal ribosomal protein uS8 family.
  
 
 0.962
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.
  
 
 0.961
Your Current Organism:
Isosphaera pallida
NCBI taxonomy Id: 575540
Other names: I. pallida ATCC 43644, Isosphaera pallida ATCC 43644, Isosphaera pallida DSM 9630, Isosphaera pallida IS1B, Isosphaera pallida str. ATCC 43644, Isosphaera pallida strain ATCC 43644
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.