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
groL60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (542 aa)    
Predicted Functional Partners:
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.995
grpE
Protein 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 of ATP-dependent i [...]
 
 0.972
htpG
Chaperone protein htpG; Molecular chaperone. Has ATPase activity.
   
 
 0.932
dnaK
Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 
 0.919
AEJ60430.1
Peptidoglycan-binding lysin domain-containing protein; PFAM: LysM domain; InterPro IPR018392:IPR002482; KEGG: sta:STHERM_c01550 hypothetical protein; PFAM: Peptidoglycan-binding lysin domain; SMART: Peptidoglycan-binding Lysin subgroup; SPTR: Peptidoglycan-binding lysin domain.
  
 
 0.900
AEJ62118.1
KEGG: sta:STHERM_c17890 hypothetical protein; SPTR: Putative uncharacterized protein.
  
 
 0.900
hslU
ATP-dependent hsl protease ATP-binding subunit hslU; 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.
   
  
 0.868
AEJ61223.1
Flagellar motor switch protein FliN; FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation. Belongs to the FliN/MopA/SpaO family.
   
 
 0.822
hslV
ATP-dependent protease hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
 
 0.796
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 [...]
 
 0.768
Your Current Organism:
Spirochaeta thermophila
NCBI taxonomy Id: 869211
Other names: S. thermophila DSM 6578, Spirochaeta thermophila DSM 6578, Spirochaeta thermophila str. DSM 6578, Spirochaeta thermophila strain DSM 6578
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