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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
dnaJHypothetical 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 between DnaJ, Dna [...] (385 aa)    
Predicted Functional Partners:
dnaK
Hypothetical protein; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 0.999
hscA
Hypothetical 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.
 0.986
grpE
Hypothetical 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-dep [...]
 
 
 0.985
htpG
Hypothetical protein; Molecular chaperone. Has ATPase activity.
  
 0.983
CKO_01425
Hypothetical protein; KEGG: ecp:ECP_1403 0. probable pyruvate-flavodoxin oxidoreductase K03737; COG: COG1013 Pyruvate:ferredoxin oxidoreductase and related 2-oxoacid:ferredoxin oxidoreductases, beta subunit.
   
 
 0.958
CKO_00709
Hypothetical protein; KEGG: eci:UTI89_C0016 9.6e-11 dnaK; chaperone HSP70; DNA biosynthesis; autoregulated heat shock proteins K04043; COG: COG0443 Molecular chaperone.
 
 0.949
groL
Hypothetical protein; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.931
CKO_02852
Hypothetical protein; COG: NOG08675 non supervised orthologous group.
  
 0.923
lon
Hypothetical protein; 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.
 
  
 0.909
hslU
Hypothetical 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.
   
 
 0.905
Your Current Organism:
Citrobacter koseri
NCBI taxonomy Id: 290338
Other names: C. koseri ATCC BAA-895, Citrobacter (diversus) koseri ATCC BAA-895, Citrobacter koseri ATCC BAA-895, Citrobacter koseri str. ATCC BAA-895, Citrobacter koseri strain ATCC BAA-895
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