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
htpGMolecular chaperone HtpG; Molecular chaperone. Has ATPase activity. (634 aa)    
Predicted Functional Partners:
dnaJ
Molecular 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, [...]
 
 0.981
ARQ76442.1
DNA-binding protein; Functional analog of DnaJ; co-chaperone with DnaK, molecular chaperone in an adaptive response to environmental stresses other than heat shock; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.961
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 0.960
hscA
Fe-S protein assembly chaperone HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.
  
 0.959
ARQ76443.1
Heat-shock protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.950
groL
Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 
 0.904
ARQ73412.1
Flavodoxin; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.893
ARQ73737.1
InaA protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.858
ARQ76522.1
Polymerase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.858
ARQ76534.1
Lipopolysaccharide kinase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.858
Your Current Organism:
Pseudomonas fragi
NCBI taxonomy Id: 296
Other names: ATCC 4973, Bacterium fragi, CCUG 556, CFBP 4556, CIP 55.4, DSM 3456, HAMBI 28, IFO 3458, LMG 2191, LMG:2191, NBRC 3458, NCCB 69033, NCIB 8542, NCIB:8542, NCTC 10689, NRRL B-25, NRRL B-727, NRRL:B:25, P. fragi, Pseudomonas fragariae, VKM B-898, VKM:B:898
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