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hslO hslO TMO_0337 TMO_0337 clpB clpB TMO_0518 TMO_0518 hspB hspB groL groL groS groS lon lon clpX clpX clpP clpP cbpA cbpA TMO_2185 TMO_2185 htpG htpG trxA trxA trxA-2 trxA-2 yegD yegD hslU hslU hslV hslV ytzA ytzA hrcA hrcA grpE grpE dnaK dnaK dnaJ dnaJ
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
Your Input:
hslOMolecular chaperone Hsp33; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress; Belongs to the HSP33 family. (328 aa)
TMO_0337Heat shock protein DnaJ. (203 aa)
clpBATP-dependent Clp protease ATP-binding subunit; 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. (865 aa)
TMO_0518Thioredoxin reductase. (368 aa)
hspBSmall heat shock protein; Belongs to the small heat shock protein (HSP20) family. (146 aa)
groLGroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (548 aa)
groSChaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (96 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. (827 aa)
clpXATP-dependent protease ATP-binding 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. (422 aa)
clpPProtease subunit of ATP-dependent Clp proteases; 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)
cbpACurved DNA-binding protein. (332 aa)
TMO_2185FAD-dependent pyridine nucleotide-disulfide oxidoreductase. (431 aa)
htpGChaperone protein htpG; Molecular chaperone. Has ATPase activity. (648 aa)
trxAThioredoxin. (305 aa)
trxA-2Thioredoxin 1; Belongs to the thioredoxin family. (107 aa)
yegDChaperone protein yegD. (432 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. (437 aa)
hslVATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (186 aa)
ytzAFxsA. (174 aa)
hrcATranscriptional regulator of heat shock gene; Negative regulator of class I heat shock genes (grpE-dnaK- dnaJ and groELS operons). Prevents heat-shock induction of these operons. (376 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 [...] (206 aa)
dnaKMolecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (642 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 [...] (393 aa)
Your Current Organism:
Tistrella mobilis
NCBI taxonomy Id: 1110502
Other names: T. mobilis KA081020-065, Tistrella mobilis KA081020-065, Tistrella mobilis str. KA081020-065, Tistrella mobilis strain KA081020-065
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