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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
hslU_1HslU--HslV peptidase ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. (445 aa)    
Predicted Functional Partners:
hslV
HslU--HslV peptidase proteolytic subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
 0.999
AOE40166.1
Molecular chaperone DnaJ; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.901
grpE_2
Nucleotide exchange factor 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 [...]
   
  
 0.895
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
  
 0.875
groES
10 kDa chaperonin; Cpn10; GroES; forms homoheptameric ring; binds to one or both ends of the GroEL double barrel in the presence of adenine nucleotides capping it; folding of unfolded substrates initiates in a GroEL-substrate bound and capped by GroES; release of the folded substrate is dependent on ATP binding and hydrolysis in the trans ring; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  
 0.858
htpG
Molecular chaperone HtpG; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
  
 0.856
lon_3
Endopeptidase La; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.831
ybbN
Co-chaperone YbbN; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.814
ftsN_1
Cell division protein FtsN; Derived by automated computational analysis using gene prediction method: Protein Homology.
      0.800
dnaK_3
Molecular chaperone DnaK; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.777
Your Current Organism:
Pantoea agglomerans
NCBI taxonomy Id: 549
Other names: ATCC 27155, Bacillus milletiae, Bacterium herbicola, CCUG 539, CFBP 3845, CIP 57.51, DSM 3493, Enterobacter agglomerans, Erwinia herbicola, Erwinia milletiae, ICMP 12534, ICPB 3435, NBRC 102470, NCTC 9381, P. agglomerans, Pantoea herbicola, Pantoea sp. SL1_M5, Pseudomonas herbicola, bacterium G33-1
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