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
groLChaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (546 aa)    
Predicted Functional Partners:
groS
Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.999
grpE
Co-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-depend [...]
 
 0.994
htpG
Hsp90 protein; Molecular chaperone. Has ATPase activity.
   
 
 0.966
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 
 0.948
EEU95353.1
DnaK family protein; KEGG: mbo:Mb0358 6.4e-114 dnaK; probable chaperone protein DnaK (heat shock protein 70) (heat shock 70 kda protein) (HSP70) K04043; Psort location: Cytoplasmic, score: 9.26; overlaps another CDS with the same product name.
 
 
 0.940
EEU95355.1
Hypothetical protein; KEGG: hpa:HPAG1_0109 3.0e-39 chaperone and heat shock protein 70 K01529; Psort location: Cytoplasmic, score: 8.96; overlaps another CDS with the same product name.
 
 
 0.936
trxA
Thioredoxin; KEGG: mbo:Mb3945 9.3e-26 trxC; thioredoxin TrxC (TRX) (MPT46) K03671; Psort location: Cytoplasmic, score: 9.26.
  
 
 0.932
EEU96302.1
Lipid kinase, YegS/Rv2252/BmrU family; KEGG: eci:UTI89_C2362 3.7e-07 hypothetical protein.
    
 0.906
EEU97365.1
Peptidase M16 inactive domain protein; KEGG: ava:Ava_3678 1.1e-11 peptidase M16-like K07263.
   
  0.905
dnaJ
Chaperone protein 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, D [...]
 
 0.893
Your Current Organism:
Faecalibacterium prausnitzii A2165
NCBI taxonomy Id: 411483
Other names: F. prausnitzii A2-165, Faecalibacterium prausnitzii A2-165
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.