STRINGSTRING
clpP clpP AHM58592.1 AHM58592.1 groS groS groL groL AHM59250.1 AHM59250.1 hslV hslV AHM60241.1 AHM60241.1 grpE grpE dnaJ dnaJ dnaK dnaK htpG htpG clpB clpB AHM61081.1 AHM61081.1 lon lon hslU hslU clpX clpX clpP-2 clpP-2 AHM63100.1 AHM63100.1
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.
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:
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. (210 aa)
AHM58592.1COG0234 Co-chaperonin GroES (HSP10). (131 aa)
groSCo-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (92 aa)
groLChaperonin groel; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (546 aa)
AHM59250.1COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. (178 aa)
hslVATP-dependent protease subunit HslV; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (182 aa)
AHM60241.1Hypothetical protein; COG0464 ATPases of the AAA+ class. (520 aa)
grpEMolecular chaperone 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 [...] (199 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 [...] (371 aa)
dnaKChaperone protein dnak; Acts as a chaperone; Belongs to the heat shock protein 70 family. (646 aa)
htpGHeat shock protein 90; Molecular chaperone. Has ATPase activity. (621 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. (873 aa)
AHM61081.1COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain. (268 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. (826 aa)
hslUATP-dependent 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. (470 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. (412 aa)
clpP-2Protease subunit of ATP-dependent protease; 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. (231 aa)
AHM63100.1Hypothetical protein. (1144 aa)
Your Current Organism:
Flammeovirgaceae bacterium 311
NCBI taxonomy Id: 1257021
Other names: F. bacterium 311
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