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.
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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
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[Homology]
Score
hscAFe-S protein assembly chaperone; Belongs to the heat shock protein 70 family. (565 aa)    
Predicted Functional Partners:
dnaJ
Chaperone DnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. 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 interactions between DnaJ, DnaK and [...]
 0.997
grpE
Chaperone 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 [...]
  
 0.980
dnaK
Chaperone DnaK; Acts as a chaperone.
  
  
0.918
FAD_1468
Thermosome subunit; Belongs to the TCP-1 chaperonin family.
  
 0.889
FAD_1525
Thermosome subunit; Belongs to the TCP-1 chaperonin family.
  
 0.889
fusA
Elongation factor EF-2; 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 subfamily.
 
 
 0.807
rpl10e
50S ribosomal protein L10e; Belongs to the universal ribosomal protein uL16 family.
   
 
 0.798
FAD_0005
Peptidyl-prolyl cis-trans isomerase.
  
 0.794
gap
Glyceraldehyde-3-phosphate dehydrogenase.
  
 0.788
gyrA
DNA gyrase subunit A.
   
 
 0.779
Your Current Organism:
Ferroplasma acidiphilum
NCBI taxonomy Id: 74969
Other names: DSM 12658, F. acidiphilum, Ferromonas metallovorans, Ferroplasma acidiphilum Golyshina et al. 2000, JCM 10970
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