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
groSChaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (91 aa)    
Predicted Functional Partners:
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.999
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 
 0.949
grpE
Molecular chaperone 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 of ATP [...]
 
 
 0.919
SFD65026.1
Molecular chaperone HtpG.
   
 
 0.827
clpP-2
ATP-dependent Clp protease, protease subunit; 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.
 
 
 0.725
clpP
ATP-dependent Clp protease, protease subunit; 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.
 
 
 0.717
rplL
LSU ribosomal protein L12P; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation; Belongs to the bacterial ribosomal protein bL12 family.
   
  
 0.691
SFD31340.1
Preprotein translocase subunit SecG; Involved in protein export. Participates in an early event of protein translocation; Belongs to the SecG family.
     
 0.641
SFD13459.1
Peptidyl-prolyl cis-trans isomerase (rotamase)-cyclophilin family.
 
 
 0.629
SFD57581.1
Peptidylprolyl isomerase.
 
 
 0.627
Your Current Organism:
Algibacter lectus
NCBI taxonomy Id: 221126
Other names: A. lectus, Algibacter lectus Nedashkovskaya et al. 2004, Bacteroidetes bacterium KMM 3902, Bacteroidetes bacterium KMM 3914, DSM 15365, JCM 21761, KCTC 12103, KMM 3902
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.