STRINGSTRING
dnaK dnaK dnaJ dnaJ KPN_00354 KPN_00354 clpP clpP clpX clpX lon lon htpG htpG copA copA ybbN ybbN ahpC ahpC ahpF ahpF clpS clpS clpA clpA aat aat trxB trxB KPN_01190 KPN_01190 yeaA yeaA katE katE KPN_01401 KPN_01401 KPN_01596 KPN_01596 KPN_01805 KPN_01805 katG katG sodC sodC sodB sodB tdcC tdcC yegD yegD yfcG yfcG trxC trxC clpB clpB grpE grpE hslR hslR hslO hslO malT malT gor gor grxC grxC yibN yibN ibpB ibpB ibpA ibpA sodA sodA hslU hslU hslV hslV trxA trxA yccD yccD cbpA cbpA KPN_04510 KPN_04510 groES groES groEL-2 groEL-2 msrA msrA
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:
dnaKMolecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (638 aa)
dnaJChaperone with DnaK; 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 [...] (377 aa)
KPN_00354Putative thiol - alkyl hydroperoxide reductase. (200 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. (194 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. (424 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. (784 aa)
htpGHeat shock protein 90; Molecular chaperone. Has ATPase activity. (624 aa)
copACu(I)-translocating P-type ATPase. (851 aa)
ybbNPutative thioredoxin protein. (284 aa)
ahpCAlkyl hydroperoxide reductase, C22 subunit, thioredoxin-like protein; 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 subunit, FAD/NAD(P)-binding protein; Detoxification of hydroperoxides. (521 aa)
clpSATP-dependent Clp protease adaptor protein ClpS; Involved in the modulation of the specificity of the ClpAP- mediated ATP-dependent protein degradation; Belongs to the ClpS family. (105 aa)
clpAATP-binding component of serine protease; Belongs to the ClpA/ClpB family. (759 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. (233 aa)
trxBThioredoxin reductase. (331 aa)
KPN_01190Putative glutathione peroxidase; Belongs to the glutathione peroxidase family. (160 aa)
yeaAMethionine sulfoxide reductase B; Belongs to the MsrB Met sulfoxide reductase family. (137 aa)
katECatalase; Serves to protect cells from the toxic effects of hydrogen peroxide. (752 aa)
KPN_01401Putative antitermination protein. (251 aa)
KPN_01596Heat shock protein; Belongs to the small heat shock protein (HSP20) family. (157 aa)
KPN_01805Putative cytochrome c biogenesis protein. (386 aa)
katGPutative catalase (hydroperoxidase I); Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity; Belongs to the peroxidase family. Peroxidase/catalase subfamily. (725 aa)
sodCSuperoxide dismutase precursor (Cu-Zn); Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Belongs to the Cu-Zn superoxide dismutase family. (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)
tdcCL-threonine/L-serine permease, anaerobically inducible (HAAAP family); Involved in the import of threonine and serine into the cell, with the concomitant import of a proton (symport system). Belongs to the amino acid/polyamine transporter 2 family. SdaC/TdcC subfamily. (443 aa)
yegDPutative heat shock protein. (456 aa)
yfcGPutative S-transferase. (209 aa)
trxCPutative thioredoxin-like protein. (141 aa)
clpBATP-dependent protease, Hsp 100; 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)
grpEHsp 24 nucleotide exchange factor; 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 roun [...] (196 aa)
hslRHsp15; DNA/RNA binding heat shock protein; Belongs to the HSP15 family. (133 aa)
hslOHsp33-like 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. (294 aa)
malTTranscriptional regulator MalT; Positively regulates the transcription of the maltose regulon whose gene products are responsible for uptake and catabolism of malto- oligosaccharides. Specifically binds to the promoter region of its target genes, recognizing a short DNA motif called the MalT box. (901 aa)
gorGlutathione reductase. (452 aa)
grxCGlutaredoxin 3; Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. (83 aa)
yibNPutative phosphatase. (143 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. (142 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. (152 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. (210 aa)
hslUATP-dependent protease ATP-binding 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. (444 aa)
hslVATP-dependent protease peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery. (176 aa)
trxAThioredoxin; Belongs to the thioredoxin family. (109 aa)
yccDHypothetical protein. (106 aa)
cbpAPutative chaperone DnaJ; DNA-binding protein that preferentially recognizes a curved DNA sequence. It is probably a functional analog of DnaJ; displays overlapping activities with DnaJ, but functions under different conditions, probably acting as a molecular chaperone in an adaptive response to environmental stresses other than heat shock. Lacks autonomous chaperone activity; binds native substrates and targets them for recognition by DnaK. Its activity is inhibited by the binding of CbpM. (305 aa)
KPN_04510Putative transmembrane protein. (218 aa)
groESCo-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (97 aa)
groEL-2Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (548 aa)
msrAMethionine sulfoxide reductase A; 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. (232 aa)
Your Current Organism:
Klebsiella pneumoniae MGH78578
NCBI taxonomy Id: 272620
Other names: K. pneumoniae subsp. pneumoniae MGH 78578, Klebsiella pneumoniae MCG 78578, Klebsiella pneumoniae str. MCG 78578, Klebsiella pneumoniae subsp. pneumoniae ATCC 700721, Klebsiella pneumoniae subsp. pneumoniae MGH 78578, Klebsiella pneumoniae subsp. pneumoniae str. MGH 78578, Klebsiella pneumoniae subsp. pneumoniae strain MGH 78578
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