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
tsfTranslation 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. (199 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.
 
 
 0.987
tuf
Translation elongation factor Tu; This protein promotes the GTP-dependent binding of aminoacyl- tRNA to the A-site of ribosomes during protein biosynthesis.
   
 0.987
Deba_2953
COGs: COG0050 GTPase - translation elongation factors; InterProIPR000795:IPR004161:IPR004160:IPR009001:IPR 009000:IPR004541:IPR005225; KEGG: dal:Dalk_1928 elongation factor Tu; PFAM: protein synthesis factor GTP-binding; elongation factor Tu domain 2 protein; elongation factor Tu domain protein; SPTR: B8FET7 Elongation factor Tu; TIGRFAM: translation elongation factor Tu; small GTP-binding protein; PFAM: Elongation factor Tu domain 2; Elongation factor Tu C-terminal domain; Elongation factor Tu GTP binding domain; TIGRFAM: small GTP-binding protein domain; translation elongation factor TU.
   
 0.987
rpsB
COGs: COG0052 Ribosomal protein S2; InterPro IPR005706:IPR001865:IPR018130; KEGG: gur:Gura_3733 30S ribosomal protein S2; PFAM: ribosomal protein S2; SPTR: A5G7W8 30S 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.
 
 0.979
pyrH
Uridylate kinase; Catalyzes the reversible phosphorylation of UMP to UDP.
 
  
 0.964
Deba_2714
Ribosomal protein S1; Binds mRNA; thus facilitating recognition of the initiation point. It is needed to translate mRNA with a short Shine-Dalgarno (SD) purine-rich sequence.
  
 
 0.964
rplD
Ribosomal protein L4/L1e; Forms part of the polypeptide exit tunnel.
 
 
 0.953
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.
 
 
 0.949
rplL
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.
 
 0.947
rplU
Ribosomal protein L21; This protein binds to 23S rRNA in the presence of protein L20; Belongs to the bacterial ribosomal protein bL21 family.
 
 
 0.945
Your Current Organism:
Desulfarculus baarsii
NCBI taxonomy Id: 644282
Other names: D. baarsii DSM 2075, Desulfarculus baarsii 2st 14, Desulfarculus baarsii DSM 2075, Desulfarculus baarsii str. DSM 2075, Desulfarculus baarsii strain DSM 2075
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.