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hslV hslV hslU hslU Daro_0231 Daro_0231 groS groS groL groL Daro_0630 Daro_0630 dnaJ dnaJ dnaK dnaK grpE grpE htpG htpG lon lon clpX clpX clpP clpP Daro_1926 Daro_1926 Daro_2058 Daro_2058 Daro_2290 Daro_2290 dnaJ-2 dnaJ-2 Daro_2530 Daro_2530 clpB clpB Daro_3428 Daro_3428 Daro_3636 Daro_3636 Daro_3951 Daro_3951
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:
hslVHslV component of HslUV peptidase, Threonine peptidase, MEROPS family T01B; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (178 aa)
hslUHeat shock protein 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. (446 aa)
Daro_0231ClpX, ATPase regulatory subunit; Belongs to the ClpX chaperone family. (360 aa)
groSChaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (96 aa)
groLChaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (550 aa)
Daro_0630Heat shock protein Hsp20; Belongs to the small heat shock protein (HSP20) family. (138 aa)
dnaJHeat shock 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, [...] (378 aa)
dnaKHeat shock protein Hsp70; 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 [...] (184 aa)
htpGHeat shock protein Hsp90:ATP-binding region, ATPase-like protein; Molecular chaperone. Has ATPase activity. (636 aa)
lonATP-dependent proteinase, Serine peptidase, MEROPS family S16; 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. (804 aa)
clpXClpX, ATPase regulatory subunit; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. (420 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. (209 aa)
Daro_1926Conserved hypothetical protein. (207 aa)
Daro_2058Heat shock protein DnaJ, N-terminal. (108 aa)
Daro_2290ATP-binding region, ATPase-like protein. (546 aa)
dnaJ-2DnaJ central region:Heat shock protein DnaJ, N-terminal:Chaperone DnaJ, C-terminal; 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. [...] (335 aa)
Daro_2530Plasmid segregation actin-type ATPase ParM. (354 aa)
clpBAAA ATPase, central region:Clp, N terminal; 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. (863 aa)
Daro_3428Molecular chaperone-like protein. (148 aa)
Daro_3636Heat shock protein DnaJ, N-terminal. (92 aa)
Daro_3951AAA ATPase, central region. (326 aa)
Your Current Organism:
Dechloromonas aromatica
NCBI taxonomy Id: 159087
Other names: D. aromatica RCB, Dechloromonas aromatica RCB, Dechloromonas aromatica str. RCB, Dechloromonas sp. RCB
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