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
Dret_1856PFAM: chaperone DnaJ domain protein; heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; KEGG: dma:DMR_30690 curved DNA-binding protein. (328 aa)    
Predicted Functional Partners:
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 0.987
grpE
GrpE protein; 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 [...]
 
 
 0.939
Dret_1036
TIGRFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; Pyruvate/ketoisovalerate oxidoreductase; 4Fe-4S ferredoxin iron-sulfur binding domain protein; Pyruvate-flavodoxin oxidoreductase, EKR domain; KEGG: dvl:Dvul_0348 pyruvate flavodoxin/ferredoxin oxidoreductase domain-containing protein.
   
 
 0.832
Dret_1857
KEGG: dvm:DvMF_0568 hypothetical protein.
  
 
 0.832
htpG
Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity.
  
 0.765
clpB
ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family.
  
 
 0.728
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.705
rplO
Ribosomal protein L15; Binds to the 23S rRNA; Belongs to the universal ribosomal protein uL15 family.
  
   0.683
Dret_2254
PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; pyridine nucleotide-disulphide oxidoreductase dimerisation region; SMART: Rhodanese domain protein; KEGG: ppd:Ppro_1974 FAD-dependent pyridine nucleotide-disulphide oxidoreductase.
  
 
 0.652
Dret_1243
Peptidyl-prolyl cis-trans isomerase cyclophilin type; 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.
  
 
 0.651
Your Current Organism:
Desulfohalobium retbaense
NCBI taxonomy Id: 485915
Other names: D. retbaense DSM 5692, Desulfohalobium retbaense DSM 5692, Desulfohalobium retbaense str. DSM 5692, Desulfohalobium retbaense strain DSM 5692
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