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
htpG_1Heat shock protein 90; Molecular chaperone. Has ATPase activity. (625 aa)    
Predicted Functional Partners:
dnaJ_1
Molecular chaperone DnaJ; Chaperone Hsp40; co-chaperone with DnaK; 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; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.983
dnaK
Molecular chaperone DnaK; Heat shock protein 70; assists in folding of nascent polypeptide chains; refolding of misfolded proteins; utilizes ATPase activity to help fold; co-chaperones are DnaJ and GrpE; multiple copies in some bacteria; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.940
hscA
Chaperone protein HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.
   
 0.932
ppiB_2
Peptidylprolyl isomerase; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.
  
 0.931
cysJ_1
Sulfite reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.925
groEL
Molecular chaperone GroEL; 60 kDa chaperone family; promotes refolding of misfolded polypeptides especially under stressful conditions; forms two stacked rings of heptamers to form a barrel-shaped 14mer; ends can be capped by GroES; misfolded proteins enter the barrel where they are refolded when GroES binds; many bacteria have multiple copies of the groEL gene which are active under different environmental conditions; the B.japonicum protein in this cluster is expressed constitutively; in Rhodobacter, Corynebacterium and Rhizobium this protein is essential for growth; Derived by autom [...]
   
 
 0.858
ACEE_05835
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.824
ACEE_05840
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.821
ACEE_03710
UDP-N-acetylglucosamine-peptide N-acetylglucosaminyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.788
groES
Molecular chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
   
 
 0.777
Your Current Organism:
Actinobacillus equuli
NCBI taxonomy Id: 202947
Other names: A. equuli subsp. equuli, Actinobacillus equuli subsp. equuli
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