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Ppro_0013 Ppro_0013 Ppro_0157 Ppro_0157 clpX clpX clpP clpP htpG htpG dnaJ dnaJ dnaK dnaK grpE grpE hrcA hrcA clpB clpB Ppro_2145 Ppro_2145 ftsH ftsH groL groL groS groS ftsH-2 ftsH-2 lon-2 lon-2
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
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:
Ppro_0013PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: gme:Gmet_3550 heat shock protein DnaJ-like. (302 aa)
Ppro_0157PFAM: Heat shock protein 70; KEGG: cdi:DIP2120 chaperone protein DnaK. (533 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 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. (199 aa)
htpGHeat shock protein Hsp90; Molecular chaperone. Has ATPase activity. (645 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 [...] (384 aa)
dnaKChaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (636 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 [...] (190 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. (343 aa)
clpBATPase AAA-2 domain protein; 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. (873 aa)
Ppro_2145KEGG: ade:Adeh_2261 molecular chaperone-like. (423 aa)
ftsHMembrane protease FtsH catalytic subunit; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; Belongs to the AAA ATPase family. In the central section; belongs to the AAA ATPase family. (621 aa)
groLChaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (554 aa)
groSChaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (95 aa)
ftsH-2ATP-dependent metalloprotease FtsH; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; In the central section; belongs to the AAA ATPase family. (623 aa)
lon-2ATP-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. (771 aa)
Your Current Organism:
Pelobacter propionicus
NCBI taxonomy Id: 338966
Other names: P. propionicus DSM 2379, Pelobacter propionicus DSM 2379, Pelobacter propionicus str. DSM 2379, Pelobacter propionicus strain DSM 2379
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