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
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[Homology]
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dnaJ-2Molecular chaperone 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, [...] (383 aa)    
Predicted Functional Partners:
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 0.991
grpE
Molecular chaperone; 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-depe [...]
 
 
 0.972
htpG
Heat shock protein 90; Molecular chaperone. Has ATPase activity.
 
 0.963
AKD96469.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.941
AKD98290.1
Ribosomal RNA small subunit methyltransferase E; Specifically methylates the N3 position of the uracil ring of uridine 1498 (m3U1498) in 16S rRNA. Acts on the fully assembled 30S ribosomal subunit.
  
 
 0.935
hrcA
HrcA family transcriptional regulator; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons.
  
  
 0.934
groEL-2
Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.908
groEL
Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.907
gyrB
DNA gyrase subunit B; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
 
  
 0.887
AKD96612.1
ATPase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the AAA ATPase family.
 
 
 0.887
Your Current Organism:
Rhodococcus erythropolis
NCBI taxonomy Id: 1833
Other names: ATCC 4277, Arthrobacter hydrocarboglutamicus, Arthrobacter oxamicetus, Arthrobacter oxamicetus subsp. propiophenicolus, Arthrobacter paraffineus, Arthrobacter picolinophilus, Brevibacterium healii, Brevibacterium ketoglutamicum, Brevibacterium paraffinoliticum, CIP 104179, Corynebacterium alkanum, Corynebacterium aurantiacum, Corynebacterium humiferum, Corynebacterium sp. WS2071, Corynebacterium sp. WS2072, DSM 43066, IEGM 7, IFO 15567, JCM 20419, JCM 3201, LMG 5359, LMG:5359, Mycobacterium erythropolis, NBRC 15567, NCIB 11148, NCIB 9158, NCIB:11148, NCIB:9158, NCIMB 9158, NCTC 13021, NRRL B-16025, Nocardia calcarea, Nocardioides simplex ATCC 13260, Nocardioides simplex ATCC 19565, Nocardioides simplex ATCC 19566, R. erythropolis, Rhodococcus NI86/21, Rhodococcus sp. (strain NI86/21), Rhodococcus sp. ATCC 15108, Rhodococcus sp. ATCC 15961, Rhodococcus sp. ATCC 21035, Rhodococcus sp. BG43, Rhodococcus sp. BZ4, Rhodococcus sp. NCIB 9646, Rhodococcus sp. NI86/21, Rhodococcus sp. strain NI86/21, VKM Ac-858, strain N11
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