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
tsfElongation 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. (280 aa)    
Predicted Functional Partners:
frr
Ribosome-recycling factor; Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another; Belongs to the RRF family.
 
 
 0.988
rpsB
PFAM: Ribosomal protein S2; TIGRFAM: ribosomal protein S2, bacterial type; COGs: COG0052 Ribosomal protein S2; InterPro IPR005706:IPR001865; KEGG: sta:STHERM_c13060 30S ribosomal protein S2; PFAM: Ribosomal protein S2; SPTR: 30S ribosomal protein S2; TIGRFAM: Ribosomal protein S2, bacteria/mitochondria/plastid.
 
 0.987
tuf
Translation elongation factor Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.
   
 0.984
cmk
PFAM: Cytidylate kinase; S1 RNA binding domain; TIGRFAM: ribosomal protein S1; cytidylate kinase; COGs: COG0539 Ribosomal protein S1; HAMAP: Cytidylate kinase; InterPro IPR011994:IPR003029:IPR003136; KEGG: sta:STHERM_c10970 30S ribosomal protein S1; PFAM: Cytidylate kinase region; Ribosomal protein S1, RNA binding domain; SPTR: Cytidylate kinase; TIGRFAM: Cytidylate kinase.
  
 
 0.964
tig
Trigger 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.
 
 
 0.950
rplT
50S 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.
 
 
 0.945
rpsE
Ribosomal protein S5; Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. Belongs to the universal ribosomal protein uS5 family.
  
 
 0.934
rplL
50S ribosomal protein L7/L12; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation; Belongs to the bacterial ribosomal protein bL12 family.
 
 0.933
rplJ
50S ribosomal protein L10; Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. Belongs to the universal ribosomal protein uL10 family.
 
  
 0.931
rpsC
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.
 
  
 0.931
Your Current Organism:
Spirochaeta thermophila
NCBI taxonomy Id: 869211
Other names: S. thermophila DSM 6578, Spirochaeta thermophila DSM 6578, Spirochaeta thermophila str. DSM 6578, Spirochaeta thermophila strain DSM 6578
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.