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
groL260 kDa chaperonin 2; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (539 aa)    
Predicted Functional Partners:
groS
10 kD chaperonin cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 0.999
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.992
grpE
GrpE heat shock 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 ATP- [...]
 
 0.979
dnaJ
Chaperone protein DnaJ.
 
 0.794
dnaJ-2
DnaJ chaperone protein; 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, D [...]
 
 0.784
rpoB
DNA-directed RNA polymerase beta chain; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
  
 
 0.728
guaB
Inosine-5'-monophosphate dehydrogenase; Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Belongs to the IMPDH/GMPR family.
  
 0.724
sodB
Superoxide dismutase [Fe-Zn]; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family.
  
 
 0.724
tig
Putative cell division trigger factor; Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase; Belongs to the FKBP-type PPIase family. Tig subfamily.
  
  
 0.718
recA
Recombinase A; Can catalyze the hydrolysis of ATP in the presence of single- stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage; Belongs to the RecA family.
   
 
 0.717
Your Current Organism:
Clavibacter michiganensis sepedonicus
NCBI taxonomy Id: 31964
Other names: ATCC 33113, Aplanobacter sepedonicum, Bacterium sepedonicum, C. michiganensis subsp. sepedonicus, CCUG 23908, CFBP 2049, CIP 104844, Clavibacter michiganense sepedonicum, Clavibacter michiganensis sepedonicum, Clavibacter michiganensis subsp. sepedonicus, Clavibacter sepedonicus nom. illegit., Corynebacterium michiganense subsp. sepedonicum, Corynebacterium sepedonicum, DSM 20744, ICMP 2535, JCM 9667, LMG 2889, LMG:2889, Mycobacterium sepedonicum, NCPPB 2137, Phytomonas sepedonica, Pseudobacterium sepedonicum
Server load: medium (42%) [HD]