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
groLChaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (539 aa)    
Predicted Functional Partners:
groS
Chaperonin GroS; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.999
grpE
Putative protein 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-de [...]
 
 0.991
DnaK
Chaperone protein DnaK family protein; KEGG: eci:UTI89_C0016 2.4e-114 dnaK; chaperone HSP70; DNA biosynthesis; autoregulated heat shock proteins K04043; Psort location: Cytoplasmic, score: 8.87.
 
 
 0.898
EEA84346.1
KEGG: mbo:Mb0358 2.3e-77 dnaK; probable chaperone protein DnaK (heat shock protein 70) (heat shock 70 kda protein) (HSP70) K04043; Psort location: Cytoplasmic, score: 9.65.
 
 
 0.896
HscC
DnaK family protein; KEGG: mbo:Mb0358 9.4e-65 dnaK; probable chaperone protein DnaK (heat shock protein 70) (heat shock 70 kda protein) (HSP70) K04043; Psort location: Cytoplasmic, score: 9.98.
 
 
 0.887
DagK
Putative lipid kinase; KEGG: eci:UTI89_C2362 5.5e-21 hypothetical protein; Psort location: Cytoplasmic, score: 8.87.
    
  0.867
dnaJ
Putative chaperone protein DnaJ; 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 betwee [...]
 
 0.827
nifJ
Pyruvate synthase; KEGG: tte:TTE0445 0. porA; Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, alpha subunit K03737; Psort location: Cytoplasmic, score: 8.87.
  
 
 0.800
EEA84091.1
Tetratricopeptide repeat protein; KEGG: rso:RS02206 0.0034 RSp1647; putative methyltransferase protein K00575; Psort location: Cytoplasmic, score: 8.87.
  
 0.770
lon
Endopeptidase La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner.
  
 0.755
Your Current Organism:
Clostridium hiranonis
NCBI taxonomy Id: 500633
Other names: Clostridium hiranonis DSM 13275, Clostridium hiranonis str. DSM 13275, Clostridium hiranonis strain DSM 13275, [. hiranonis DSM 13275, [Clostridium] hiranonis DSM 13275
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