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.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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grpEHeat shock 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-depen [...] (195 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 [...]
 
 
 0.996
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.994
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.994
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.989
hslU
ATP-dependent Hsl protease ATP-binding subunit (heat shock protein); 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.
 
  
 0.968
hslV
ATP-dependent protease (heat shock protein); Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
  
  
 0.962
hscA
Chaperone protein; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU.
 
 0.936
ECA1220
Similar to Yersinia pestis putative thioredoxin ypo3082 or y1097 SWALL:Q8ZCB1 (EMBL:AJ414155) (289 aa) fasta scores: E(): 1e-69, 71.93% id in 285 aa, and to Escherichia coli hypothetical protein ybbn or b0492 SWALL:YBBN_ECOLI (SWALL:P77395) (284 aa) fasta scores: E(): 3.8e-68, 70.96% id in 279 aa.
  
  
 0.914
ECA1820
Conserved hypothetical protein; Similar to Salmonella typhimurium putative heat shock protein yegd or stm2125 SWALL:Q8ZNQ4 (EMBL:AE008794) (450 aa) fasta scores: E(): 1.2e-121, 68.22% id in 450 aa, and to Escherichia coli hypothetical chaperone protein yegd yegd or b2069 SWALL:YEGD_ECOLI (SWALL:P36928) (450 aa) fasta scores: E(): 1.6e-121, 69.33% id in 450 aa.
  
 0.907
htpG
Chaperone protein; Molecular chaperone. Has ATPase activity.
  
 
 0.889
Your Current Organism:
Pectobacterium atrosepticum
NCBI taxonomy Id: 218491
Other names: Erwinia carotovora subsp. atroseptica SCRI1043, Erwinia carotovora subsp. atroseptica str. SCRI1043, P. atrosepticum SCRI1043, Pectobacterium atrosepticum SCRI1043, Pectobacterium atrosepticum str. SCRI1043, Pectobacterium atrosepticum strain SCRI1043, Pectobacterium carotovora subsp. atroseptica SCRI1043, Pectobacterium carotovora subsp. atroseptica str. SCRI1043
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