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
Databases
Textmining
[Homology]
Score
hrcAHeat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. (340 aa)    
Predicted Functional Partners:
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 [...]
  
  
 0.988
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
  
 0.986
dnaJ
Molecular chaperone 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, [...]
  
  
 0.915
SMB90879.1
Chaperonin GroEL (HSP60 family); InterPro IPR017998:IPR001844:IPR002423:IPR002194; COGs: COG0459 Chaperonin GroEL (HSP60 family); KEGG: t-complex protein 1, gamma subunit, putative; K09495 T-complex protein 1 subunit gamma; SPTR: A1HR08 Chaperonin Cpn60/TCP-1; PFAM: chaperonin Cpn60/TCP-1.
  
  
 0.908
clpP
ATP-dependent Clp protease proteolytic subunit ClpP; 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.
   
  
 0.886
SMB84508.1
ATP-dependent Clp protease ATP-binding subunit ClpC; InterPro IPR001270:IPR001943:IPR003959:IPR019489:IPR013093:IPR0117 04:IPR004176:IPR003593:IPR018368; COGs: COG0542 ATPase with chaperone activity ATP-binding subunit; KEGG: CLPC; CLPC (HEAT SHOCK PROTEIN 93-V); ATP binding / ATPase; SPTR: Q8EU05 Chaperone protein clpB; SMART: AAA ATPase; PFAM: ATPase AAA-2 domain protein; Clp ATPase-like; AAA ATPase central domain protein; UvrB/UvrC protein; ATPase associated with various cellular activities AAA_5; Clp domain protein; Belongs to the ClpA/ClpB family.
 
  
 0.752
clpB
ATP-dependent Clp protease ATP-binding subunit 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.
 
  
 0.741
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
  
 0.734
lepA
GTP-binding protein LepA; Required for accurate and efficient protein synthesis under certain stress conditions. May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes. Back-translocation proceeds from a post-translocation (POST) complex to a pre- translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP- dependent manner.
     
 0.716
SMB96036.1
InterPro IPR001907; COGs: COG0740 Protease subunit of ATP-dependent Clp protease; KEGG: ank:AnaeK_3435 ATP-dependent Clp protease, proteolytic subunit ClpP; SPTR: A1HSD4 Peptidase S14, ClpP; PFAM: peptidase S14 ClpP.
   
  
 0.716
Your Current Organism:
Desulfonispora thiosulfatigenes
NCBI taxonomy Id: 656914
Other names: D. thiosulfatigenes DSM 11270, Desulfonispora thiosulfatigenes DSM 11270, Desulfonispora thiosulfatigenes str. DSM 11270, Desulfonispora thiosulfatigenes strain DSM 11270
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