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hslV hslV hslU hslU groL groL groS groS ACS17863.1 ACS17863.1 ACS18060.1 ACS18060.1 dnaJ dnaJ dnaK dnaK grpE grpE ACS18799.1 ACS18799.1 clpP clpP clpX clpX lon lon clpS clpS ACS19276.1 ACS19276.1 hrcA hrcA htpG htpG ACS21696.1 ACS21696.1
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
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
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hslV20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (181 aa)
hslUHeat shock protein HslVU, ATPase 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. (442 aa)
groLChaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (550 aa)
groSChaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (96 aa)
ACS17863.1PFAM: peptidase S14 ClpP; KEGG: bpt:Bpet3891 ATP-dependent Clp protease proteolytic component. (198 aa)
ACS18060.1KEGG: dac:Daci_1060 molecular chaperone, HSP70 class. (420 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 [...] (378 aa)
dnaKChaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (645 aa)
grpEGrpE 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-dependent i [...] (179 aa)
ACS18799.1PFAM: 20S proteasome A and B subunits; KEGG: pna:Pnap_1783 20S proteasome, A and B subunits. (197 aa)
clpPATP-dependent Clp protease, proteolytic subunit ClpP; 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. (202 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. (421 aa)
lonATP-dependent protease La; 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. (813 aa)
clpSATP-dependent Clp protease adaptor protein ClpS; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. (119 aa)
ACS19276.1KEGG: pol:Bpro_2940 ATPase AAA-2; TIGRFAM: ATP-dependent Clp protease, ATP-binding subunit clpA; PFAM: ATPase AAA-2 domain protein; AAA ATPase central domain protein; ATPase associated with various cellular activities AAA_5; Clp domain protein; SMART: AAA ATPase; Belongs to the ClpA/ClpB family. (773 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)
htpGHeat shock protein Hsp90; Molecular chaperone. Has ATPase activity. (678 aa)
ACS21696.1TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: dia:Dtpsy_3279 thioredoxin. (306 aa)
Your Current Organism:
Variovorax paradoxus S110
NCBI taxonomy Id: 543728
Other names: V. paradoxus S110, Variovorax paradoxus str. S110, Variovorax paradoxus strain S110
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