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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
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Cooccurrence
Coexpression
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[Homology]
Score
ADR36694.1Heat shock protein HslVU, ATPase subunit HslU; COGs: COG1220 ATP-dependent protease HslVU (ClpYQ) ATPase subunit; InterPro IPR003593: IPR011704: IPR013093: IPR004491; KEGG: msv:Mesil_1659 heat shock protein HslVU, ATPase subunit HslU; PFAM: ATPase AAA-2 domain protein; ATPase associated with various cellular activities AAA_5; SMART: AAA ATPase; SPTR: Heat shock protein HslVU, ATPase subunit HslU; TIGRFAM: heat shock protein HslVU, ATPase subunit HslU; PFAM: AAA domain (Cdc48 subfamily); C-terminal, D2-small domain, of ClpB protein; ATPase family associated with various cellular activit [...] (419 aa)    
Predicted Functional Partners:
ADR36695.1
ATP dependent peptidase CodWX, CodW component; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
 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 [...]
   
  
 0.917
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
  
 0.886
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
   
  
 0.879
lon
ATP-dependent proteinase; 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.
  
  
 0.837
lon-2
ATP-dependent proteinase; 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.
  
  
 0.837
hslO
Hsp33 protein; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
   
  
 0.811
ADR36693.1
Tetratricopeptide TPR_1 repeat-containing protein; COGs: COG3063 Tfp pilus assembly protein PilF; InterPro IPR019734: IPR013026: IPR001440; KEGG: ttj:TTHA0629 TPR repeat-containing O-linked GlcNAc transferase; PFAM: Tetratricopeptide TPR_1 repeat-containing protein; SMART: Tetratricopeptide repeat; SPTR: TPR repeat-containing protein; PFAM: Tetratricopeptide repeat.
       0.777
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 [...]
   
 
 0.763
ADR37340.1
COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623: IPR018253: IPR002939: IPR003095; KEGG: msv:Mesil_0426 chaperone DnaJ domain protein; PFAM: chaperone DnaJ domain protein; heat shock protein DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Chaperone DnaJ domain protein; PFAM: DnaJ domain; DnaJ C terminal region; TIGRFAM: chaperone protein DnaJ.
   
 
 0.763
Your Current Organism:
Oceanithermus profundus
NCBI taxonomy Id: 670487
Other names: O. profundus DSM 14977, Oceanithermus profundus DSM 14977, Oceanithermus profundus str. DSM 14977, Oceanithermus profundus strain DSM 14977
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