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
clpBATP-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. (857 aa)    
Predicted Functional Partners:
clpP
ATP-dependent Clp endopeptidase, proteolytic subunit ClpP; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family.
  
 
 0.844
hscC
Molecular chaperone HscC; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heat shock protein 70 family.
   
 
 0.805
dnaK
Restriction endonuclease subunit M; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
 
 0.805
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 [...]
   
 
 0.718
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.
   
   0.715
clpS
Hypothetical protein; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family.
   
 
 0.698
OBX61450.1
EvpB family type VI secretion protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.687
barA
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 
 0.640
htpG
Molecular chaperone HtpG; Molecular chaperone. Has ATPase activity.
   
 
 0.613
groS
Co-chaperone GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
   
 
 0.612
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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