STRINGSTRING
hslU hslU hslV hslV dnaJ dnaJ grpE grpE htpG htpG BPSL0856 BPSL0856 groEL groEL groL groL BPSL0245 BPSL0245 lon lon groS groS
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
hslUATP-dependent Hsl protease ATP-binding subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis. (447 aa)    
Predicted Functional Partners:
hslV
ATP-dependent Hsl protease; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
 
 0.999
dnaJ
Putative 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 betwee [...]
   
 
 0.937
grpE
Conserved hypothetical protein (pseudogene); 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. Se [...]
  
  
 0.935
htpG
Chaperone protein; Molecular chaperone. Has ATPase activity.
   
  
 0.917
BPSL0856
Similar to Ralstonia solanacearum putative thioredoxin protein rsc0779 or rs05075 SWALL:Q8Y1B1 (EMBL:AL646061) (280 aa) fasta scores: E(): 2.9e-54, 55.51% id in 281 aa, and to Pseudomonas aeruginosa probable thioredoxin pa4061 SWALL:Q9HWW7 (EMBL:AE004822) (289 aa) fasta scores: E(): 1e-32, 42.1% id in 285 aa, and to Xanthomonas axonopodis thioredoxin xac2783 SWALL:AAM37628 (EMBL:AE011919) (286 aa) fasta scores: E(): 9.5e-32, 41.07% id in 280 aa.
  
 
 0.883
groEL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
  
 0.812
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
  
 0.812
BPSL0245
Putative ATPase; No significant database matches.
  
  
 0.731
lon
ATP-dependent protease; 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.
  
  
 0.731
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
   
  
 0.723
Your Current Organism:
Burkholderia pseudomallei
NCBI taxonomy Id: 272560
Other names: B. pseudomallei K96243, Burkholderia pseudomallei K96243, Burkholderia pseudomallei str. K96243, Burkholderia pseudomallei strain K96243
Server load: low (24%) [HD]