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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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[Homology]
Score
dnaKChaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (627 aa)    
Predicted Functional Partners:
dnaJ
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 between DnaJ, D [...]
 0.999
grpE
GrpE 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-dependent i [...]
 
 0.992
Lbys_0410
Histidine kinase; COGs: COG2205 Osmosensitive K+ channel histidine kinase; InterPro IPR005467:IPR003594:IPR004358; KEGG: wsu:WS1927 signal transduction histidine kinase; PFAM: ATP-binding region ATPase domain protein; SMART: ATP-binding region ATPase domain protein; SPTR: Putative uncharacterized protein; PFAM: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase.
  
 0.984
Lbys_3181
ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity.
 
 
 0.982
clpB
ATP-dependent chaperone ClpB; 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.
  
 
 0.964
Lbys_1011
ATPase AAA-2 domain protein; COGs: COG0542 ATPase with chaperone activity ATP-binding subunit; InterProIPR004176:IPR003959:IPR001943:IPR013093:IPR 019489:IPR001270:IPR018368:IPR003593; KEGG: dfe:Dfer_5019 ATPase AAA-2 domain protein; PFAM: ATPase AAA-2 domain protein; Clp domain protein; AAA ATPase central domain protein; UvrB/UvrC protein; Clp ATPase-like; SMART: AAA ATPase; SPTR: ATPase AAA-2 domain protein; PFAM: AAA domain (Cdc48 subfamily); Clp amino terminal domain; C-terminal, D2-small domain, of ClpB protein; UvrB/uvrC motif; ATPase family associated with various cellular activ [...]
  
 
 0.954
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.941
rplP
LSU ribosomal protein L16P; Binds 23S rRNA and is also seen to make contacts with the A and possibly P site tRNAs; Belongs to the universal ribosomal protein uL16 family.
   
 
 0.899
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.885
Lbys_3416
Chaperonin Cpn10; InterPro IPR020818; KEGG: sli:Slin_1082 chaperonin Cpn10; PFAM: Chaperonin Cpn10; SPTR: Chaperonin Cpn10; PFAM: Chaperonin 10 Kd subunit.
  
 
 0.837
Your Current Organism:
Leadbetterella byssophila
NCBI taxonomy Id: 649349
Other names: L. byssophila DSM 17132, Leadbetterella byssophila 4M15, Leadbetterella byssophila DSM 17132, Leadbetterella byssophila str. DSM 17132, Leadbetterella byssophila strain DSM 17132
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