STRINGSTRING
hspA hspA clpP clpP clpX clpX lon lon trxB trxB clpB clpB hslO hslO trxB_2 trxB_2 htpG htpG dnaJ dnaJ dnaK dnaK grpE grpE trxA_1 trxA_1 Lade_0850 Lade_0850 groES groES htpB htpB cbpM cbpM cbpA cbpA hslU hslU hslV hslV trxA trxA dnaJ_2 dnaJ_2 msrA msrA ahpC ahpC resA resA
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:
hspAHeat shock protein, Hsp20 family; Belongs to the small heat shock protein (HSP20) family. (146 aa)
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. (207 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. (811 aa)
trxBThioredoxin reductase. (314 aa)
clpBEndopeptidase Clp ATP-binding subunit B; 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. (858 aa)
hslOHeat shock protein 33, redox regulated chaperonin; 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. (283 aa)
trxB_2Thioredoxin reductase. (294 aa)
htpGClass III heat-shock protein HtpG(molecular chaperone); Molecular chaperone. Has ATPase activity. (620 aa)
dnaJMolecular chaperone 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, [...] (373 aa)
dnaKMolecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (642 aa)
grpEHeat-shock protein GrpE(HSP-70 cofactor); 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. Sever [...] (200 aa)
trxA_1Thioredoxin domain-containing protein; Belongs to the thioredoxin family. (121 aa)
Lade_0850Thiol:disulfide interchange protein DsbD. (577 aa)
groESCo-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (96 aa)
htpBMolecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (547 aa)
cbpMPutative chaperone-modulator protein CbpM. (104 aa)
cbpADNA-binding protein DnaJ. (295 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. (446 aa)
hslVDetoxification / adaptation, Protein fate / hydrolases / secretion; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (180 aa)
trxAThioredoxin; Belongs to the thioredoxin family. (107 aa)
dnaJ_2Molecular chaperone DnaJ. (346 aa)
msrABifunctional methionine sulfoxide reductase B/A protein; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. (287 aa)
ahpCAlkyl hydroperoxide reductase. (201 aa)
resAThiol-disulfide oxidoreductase ResA. (154 aa)
Your Current Organism:
Legionella adelaidensis
NCBI taxonomy Id: 45056
Other names: ATCC 49625, CCUG 31231 A, CIP 103645, DSM 19888, L. adelaidensis, NCTC 12735
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