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
AEH22842.1KEGG: dak:DaAHT2_1329 chaperone DnaJ domain protein; PFAM: Heat shock protein DnaJ, N-terminal; Chaperone DnaJ, C-terminal; SMART: Heat shock protein DnaJ, N-terminal. (304 aa)    
Predicted Functional Partners:
dnaK
Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 0.981
grpE
Protein grpE; 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 [...]
 
 
 0.858
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.747
hslU
ATP-dependent hsl protease ATP-binding subunit hslU; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
   
 
 0.599
AEH22840.1
PFAM: NADPH-dependent FMN reductase; KEGG: iho:Igni_0620 NADPH-dependent FMN reductase.
  
    0.592
glyA
Glycine hydroxymethyltransferase; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
   
 
 0.592
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.592
AEH22843.1
PFAM: CMP/dCMP deaminase, zinc-binding; KEGG: ter:Tery_2084 CMP/dCMP deaminase, zinc-binding.
       0.572
AEH23522.1
Small GTP-binding protein; KEGG: ddf:DEFDS_1534 translation elongation factor G; TIGRFAM: Small GTP-binding protein; PFAM: Translation elongation factor EFG/EF2, domain IV; Protein synthesis factor, GTP-binding; Translation elongation factor EFG/EF2, C-terminal.
  
 0.567
AEH22839.1
PFAM: Nitroreductase-like; KEGG: dak:DaAHT2_0557 nitroreductase.
       0.558
Your Current Organism:
Thermodesulfobacterium geofontis
NCBI taxonomy Id: 795359
Other names: T. geofontis OPF15, Thermodesulfobacterium geofontis OPF15, Thermodesulfobacterium sp. OPF15
Server load: low (16%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.