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
dnaJ_1Molecular 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, [...] (396 aa)    
Predicted Functional Partners:
dnaK
Restriction endonuclease subunit M; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 0.985
hscC
Molecular chaperone HscC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family.
 0.976
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.
 0.976
grpE
Nucleotide exchange factor 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 [...]
 
 
 0.957
htpG
Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity.
   
 0.938
OBX59801.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
   
 0.910
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.870
groS
Co-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.754
OBX61223.1
Trifunctional thioredoxin/methionine sulfoxide reductase A/B protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.750
rpoH
RNA polymerase factor sigma-32; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes.
   
 
 0.749
Your Current Organism:
Moraxella lacunata
NCBI taxonomy Id: 477
Other names: ATCC 17967, Bacillus lacunatus, CCUG 4441, CIP A182, DSM 18052, Diplobacille de la conjonctivite subaigue, Diplobacillus moraxenfeld, JCM 20914, LMG 5301, LMG:5301, M. lacunata, NBRC 102154, NCTC 11011, strain Morax 260
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