STRINGSTRING
dnaJ1 dnaJ1 dnaK dnaK grpE grpE hspR hspR groEL2 groEL2 clpB clpB groEL1 groEL1 htpG htpG Rv2264c Rv2264c Rv0312 Rv0312 Rv3446c Rv3446c
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
dnaJ1Probable chaperone protein DnaJ1; 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 betwe [...] (395 aa)    
Predicted Functional Partners:
dnaK
Probable chaperone protein DnaK (heat shock protein 70) (heat shock 70 kDa protein) (HSP70); Acts as a chaperone; Belongs to the heat shock protein 70 family.
 0.999
grpE
Probable GrpE protein (HSP-70 cofactor); 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. Severa [...]
 
 
 0.999
hspR
Rv0353, (MTCY13E10.13), len: 126 aa. Probable hspR,heat shock regulatory protein (see Stewart et al., 2001),merR family, highly similar to others e.g. HspR|P40183 heat shock regulatory protein from Streptomyces coelicolor (151 aa), FASTA scores: E(): 4.9e-22, (55.7% identity in 140 aa overlap), that binds to three inverted repeats (IR1-IR3) in the promoter region of the dnaK operon. Has possible coiled coil region in C-terminal half. Belongs to the MerR family of transcriptional regulators.
  
 
 0.998
groEL2
60 kDa chaperonin 2; Prevents aggregation of substrate proteins and promotes their refolding.
 
 0.987
clpB
Probable endopeptidase ATP binding protein (chain B) ClpB (ClpB protein) (heat shock protein F84.1); Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE. Acts before DnaK, in the processing of protein aggregates. Protein binding stimulates the ATPase activity; ATP hydrolysis unfolds the denatured protein aggregates, which probably helps expose new hydrophobic binding sites on the surface of ClpB-bound aggregates, contributing to the solubilization and refolding of denatured protein [...]
  
 
 0.982
groEL1
60 kDa chaperonin 1 GroEL1 (protein CPN60-1) (GroEL protein 1); Prevents aggregation of substrate proteins and promotes their refolding. Functions in the absence of co-chaperone CH10 and ATP.
 
 0.973
htpG
Chaperone protein HtpG; Molecular chaperone. Has ATPase activity.
  
 0.965
Rv2264c
Rv2264c, (MTV022.14c), len: 592 aa. Conserved hypothetical Pro-rich protein, similar to hypothetical proteins Rv0312 (MTCY63.17, 620 aa and Rv0350) that has highly Pro-, Thr-rich C-terminus. Contains PS00343 Gram-positive cocci surface proteins 'anchoring' hexapeptide. FASTA scores: Z96800|MTCY63_17 Mycobacterium tuberculosis cosmid (620 aa) opt: 1075, E(): 8.8e-24; (38.9% identity in 627 aa overlap). Predicted to be an outer membrane protein (See Song et al., 2008).
 
 0.939
Rv0312
Rv0312, (MTCY63.17), len: 620 aa. Conserved hypothetical protein with highly Pro-, Thr-rich C-terminus. Similar to Pro-,Thr-rich region in Rv2264c|AL021925|MTV022_14 from Mycobacterium tuberculosis (592 aa), FASTA scores: opt: 1075, E(): 0, (38.9% identity in 627 aa overlap). Also some similarity with Rv0350|dnaK from Mycobacterium tuberculosis. Possibly membrane protein; has hydrophobic stetch in its middle part.
  
 0.929
Rv3446c
Rv3446c, (MTCY77.18c), len: 404 aa. Hypothetical unknown ala-, val-rich protein.
  
 0.929
Your Current Organism:
Mycobacterium tuberculosis H37Rv
NCBI taxonomy Id: 83332
Other names: M. tuberculosis H37Rv, Mycobacterium sp. H37Rv, Mycobacterium tuberculosis str. H37Rv, Mycobacterium tuberculosis strain H37Rv
Server load: low (22%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.