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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
Tter_2103PFAM: heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; KEGG: gsu:GSU0034 chaperone protein DnaJ. (220 aa)    
Predicted Functional Partners:
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.982
grpE
GrpE protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent i [...]
 
 
 0.916
Tter_1045
TIGRFAM: translation elongation factor G; small GTP- binding protein; PFAM: elongation factor G domain IV; protein synthesis factor GTP-binding; elongation factor G domain protein; elongation factor Tu domain 2 protein; KEGG: sat:SYN_02930 elongation factor G.
 
 0.813
fusA
Translation elongation factor G; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 s [...]
 
 0.776
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.
  
 
 0.773
rplN
Ribosomal protein L14; Binds to 23S rRNA. Forms part of two intersubunit bridges in the 70S ribosome; Belongs to the universal ribosomal protein uL14 family.
  
 
 0.722
rplO
Ribosomal protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
  
 
 0.718
Tter_2648
PFAM: helicase domain protein; type III restriction protein res subunit; SMART: helicase domain protein; DEAD-like helicase; KEGG: mgm:Mmc1_2016 helicase domain protein.
  
 
 0.707
Tter_2470
Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family.
 
 0.698
rplQ
TIGRFAM: ribosomal protein L17; PFAM: ribosomal protein L17; KEGG: bpt:Bpet4923 50S ribosomal protein L17.
  
   0.690
Your Current Organism:
Thermobaculum terrenum
NCBI taxonomy Id: 525904
Other names: T. terrenum ATCC BAA-798, Thermobaculum terrenum ATCC BAA-798, Thermobaculum terrenum YNP1, Thermobaculum terrenum str. ATCC BAA-798, Thermobaculum terrenum strain ATCC BAA-798
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