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
clpP-2ATP-dependent Clp protease proteolytic subunit 2; 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. (237 aa)    
Predicted Functional Partners:
clpX
ATP-dependent protease ATP-binding subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP.
 0.996
EAQ49418.1
ATP-dependent Clp protease, ATP-binding subunit ClpC; COG0542 ATPases with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family.
  
 
 0.911
clpB
Putative heat shock ClpB protein; 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.
  
 
 0.901
EAQ51370.1
Hypothetical protein.
   
 
 0.880
def
Peptide deformylase; Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.
 
  
 0.771
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
 
 0.725
groL
Chaperonin, 60 kDa; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.662
grpE
GrpE protein (Hsp-70 cofactor); 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 [...]
   
 
 0.662
EAQ50249.1
Hypothetical protein; Belongs to the ClpS family.
   
 
 0.661
EAQ51097.1
COG0544 FKBP-type peptidyl-prolyl cis-trans isomerase (trigger factor).
  
  
 0.649
Your Current Organism:
Leeuwenhoekiella blandensis
NCBI taxonomy Id: 398720
Other names: Flavobacterium sp. MED217, L. blandensis MED217, Leeuwenhoekiella blandensis MED217
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