STRINGSTRING
dnaK dnaK dnaJ dnaJ lon lon clpX clpX clpP clpP ybaR ybaR htpG htpG ahpC ahpC ahpF ahpF grxA grxA tpx tpx sodC sodC sodB sodB yegD yegD trxB trxB aat aat clpA clpA yljA yljA grpE grpE trxC trxC clpB clpB ftsN ftsN hslV hslV hslU hslU sodA sodA trxA trxA ibpB ibpB ibpA ibpA mopB mopB mopA mopA
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:
dnaKChaperone Hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family. (638 aa)
dnaJHeat shock protein; 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, DnaK [...] (376 aa)
lonDNA-binding, ATP-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. Endogenous substrates include the regulatory proteins RcsA and SulA, the transcriptional activator SoxS, and UmuD. Its overpr [...] (812 aa)
clpXATP-dependent specificity component of clpP serine protease; ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of ClpP. (424 aa)
clpPATP-dependent proteolytic subunit of clpA-clpP serine 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. (207 aa)
ybaRPutative ATPase; Code: P; COG: COG2217. (834 aa)
htpGChaperone Hsp90; Molecular chaperone. Has ATPase activity. (624 aa)
ahpCAlkyl hydroperoxide reductase, C22 subunit; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily. (187 aa)
ahpFAlkyl hydroperoxide reductase, F52a subunit; Detoxification of hydroperoxides; Code: O; COG: COG3634. (531 aa)
grxAGlutaredoxin1 redox coenzyme for glutathione-dependent ribonucleotide reductase; Code: O; COG: COG0695. (85 aa)
tpxThiol peroxidase; Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides; Belongs to the peroxiredoxin family. Tpx subfamily. (168 aa)
sodCSuperoxide dismutase precursor (Cu-Zn); Code: P; COG: COG2032. (173 aa)
sodBSuperoxide dismutase, iron; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. (193 aa)
yegDPutative heat shock protein; Code: O; COG: COG0443. (471 aa)
trxBThioredoxin reductase; Code: O; COG: COG0492. (321 aa)
aatLeucyl, phenylalanyl-tRNA-protein transferase; Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl- tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine. (234 aa)
clpAATP-binding component of serine protease; Code: O; COG: COG0542; Belongs to the ClpA/ClpB family. (758 aa)
yljAConserved hypothetical protein; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. (106 aa)
grpEGrpE; 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 interacti [...] (197 aa)
trxCPutative thioredoxin-like protein; Code: OC; COG: COG0526; Belongs to the thioredoxin family. (139 aa)
clpBHeat shock 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. (857 aa)
ftsNEssential cell division protein; Essential cell division protein that activates septal peptidoglycan synthesis and constriction of the cell. Acts on both sides of the membrane, via interaction with FtsA in the cytoplasm and interaction with the FtsQBL complex in the periplasm. These interactions may induce a conformational switch in both FtsA and FtsQBL, leading to septal peptidoglycan synthesis by FtsI and associated synthases. (319 aa)
hslVHeat shock protein hslVU, proteasome-related peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. Belongs to the peptidase T1B family. HslV subfamily. (176 aa)
hslUHeat shock protein hslVU, ATPase subunit; 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. (443 aa)
sodASuperoxide dismutase, manganese; Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the iron/manganese superoxide dismutase family. (206 aa)
trxAThioredoxin 1; Code: OC; COG: COG0526; Belongs to the thioredoxin family. (127 aa)
ibpBHeat shock protein; Associates with aggregated proteins, together with IbpA, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. (144 aa)
ibpAHeat shock protein; Associates with aggregated proteins, together with IbpB, to stabilize and protect them from irreversible denaturation and extensive proteolysis during heat shock and oxidative stress. Aggregated proteins bound to the IbpAB complex are more efficiently refolded and reactivated by the ATP-dependent chaperone systems ClpB and DnaK/DnaJ/GrpE. Its activity is ATP-independent. (137 aa)
mopBGroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (97 aa)
mopAGroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (548 aa)
Your Current Organism:
Shigella dysenteriae
NCBI taxonomy Id: 300267
Other names: S. dysenteriae Sd197, Shigella dysenteriae Sd197, Shigella dysenteriae str. Sd197, Shigella dysenteriae strain Sd197
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