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
clpCClpC may interact with a clpP-like protease involved in degradation of denatured proteins and could be required for cell growth at high temperature; Contains 2 Clp amino terminal domains that function as a substrate-discriminating domain, 2 AAA ATPase domains and 1 UVR domain; Localized in the cytoplasm; High confidence in function and specificity; Belongs to the ClpA/ClpB family. (848 aa)    
Predicted Functional Partners:
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 
 0.949
clpS
ClpS is involved in the modulation of the specificity of the clpAP-mediated ATP-dependent protein degradation. It binds to the N-terminal domain of the chaperone ClpA. Localized in the cytoplasm; High confidence in function and specificity.
  
 
 0.839
clpP2
Endopeptidase Clp, peptidase subunit, family S14; 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.
 
 
 0.819
clpP1
Endopeptidase Clp, peptidase subunit, family S14; 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.
 
 
 0.816
grpE
Co-chaperone HSP-70 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 [...]
 
 
 0.785
CAZ97207.1
Hypothetical protein; Contains a N-terminal J domain present in the DnaJ protein; Localized in the cytoplasm.
 
 
 0.718
htpG
Chaperone protein htpG; Molecular chaperone. Has ATPase activity.
  
 
 0.689
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.648
CAZ97023.1
Heat shock protein belonging to the HSP20 family. Acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation. Hsp20 proteins seem to form large heterooligomeric aggregates. Localized in the cytoplasm; Family membership.
  
 
 0.638
CAZ97977.1
Heat shock protein acts as chaperone that can protect other proteins against heat-induced denaturation and aggregation; Belongs to the HSP20 family. Hsp20 proteins seem to form large heterooligomeric aggregates; Localized in the cytoplasm; Family membership.
  
 
 0.638
Your Current Organism:
Zobellia galactanivorans
NCBI taxonomy Id: 63186
Other names: CCUG 47099, CIP 106680, Cytophaga drobachiensis, DSM 12802, Flavobacterium droebachense, Pseudomonas droebachense, Z. galactanivorans, Zobellia galactanivorans corrig. Barbeyron et al. 2001, Zobellia galactanovorans, strain Dsij
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