STRINGSTRING
hslU hslU hslV hslV clpX clpX clpP clpP hrcA hrcA grpE grpE dnaK dnaK dnaJ dnaJ AEA33910.1 AEA33910.1 clpB clpB groS groS groL groL
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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
co-expression
protein homology
Your Input:
hslUATP-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. (450 aa)
hslVATP-dependent protease hslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (179 aa)
clpXATP-dependent Clp protease ATP-binding subunit clpX; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. (418 aa)
clpPATP-dependent Clp protease proteolytic subunit; Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins. Belongs to the peptidase S14 family. (205 aa)
hrcAHeat-inducible transcription repressor HrcA; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. (336 aa)
grpEProtein 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 [...] (186 aa)
dnaKChaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (638 aa)
dnaJChaperone 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 [...] (365 aa)
AEA33910.1Heat shock protein DnaJ domain protein; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623; IPR019734; IPR001440; KEGG: ddf:DEFDS_1649 hypothetical protein; PFAM: Heat shock protein DnaJ, N-terminal; Tetratricopeptide TPR-1; SMART: Heat shock protein DnaJ, N-terminal; Tetratricopeptide repeat; SPTR: Putative uncharacterized protein; PFAM: DnaJ domain; Tetratricopeptide repeat. (204 aa)
clpBATP-dependent chaperone ClpB; 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; Belongs to the ClpA/ClpB family. (868 aa)
groS10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (88 aa)
groL60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (546 aa)
Your Current Organism:
Hippea maritima
NCBI taxonomy Id: 760142
Other names: H. maritima DSM 10411, Hippea maritima DSM 10411, Hippea maritima MS2, Hippea maritima MS[subscript]2, Hippea maritima str. DSM 10411, Hippea maritima strain DSM 10411
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