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
dnaKMolecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (640 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, [...]
 0.993
htpG
Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity.
   
 0.983
OBX84043.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
  
 0.974
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.934
OBX85486.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
   
 0.896
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.
   
 
 0.880
groS
Co-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.846
OBX83258.1
Fe-S protein assembly co-chaperone HscB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the HscB family.
  
 
 0.822
OBX83422.1
ATP-dependent Clp protease ATP-binding subunit ClpA; Derived by automated computational analysis using gene prediction method: GeneMarkS+; Belongs to the ClpA/ClpB family.
   
 
 0.818
rplP
50S ribosomal protein L16; Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs; Belongs to the universal ribosomal protein uL16 family.
   
 0.816
Your Current Organism:
Moraxella nonliquefaciens
NCBI taxonomy Id: 478
Other names: ATCC 19975, Bacillus duplex non liquefaciens, CCUG 348, CIP 68.36, DSM 6327, JCM 20443, M. nonliquefaciens, NCTC 10464, strain 4663/62
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