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mopB mopB aceA aceA grpE grpE aer aer msrP msrP bfr bfr STM3820 STM3820 trxA trxA cyaY cyaY hslV hslV dnaK dnaK dnaJ dnaJ htrA htrA clpP clpP htpG htpG sucA sucA pepT pepT fumA fumA narJ narJ htpX htpX mopA mopA soxR soxR
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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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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
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textmining
co-expression
protein homology
Your Input:
mopBChaperone Hsp10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (97 aa)
aceAIsocitrate lyase; Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates. (434 aa)
grpEMolecular chaparone; 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-depe [...] (196 aa)
aerAerotaxis sensor receptor; Senses cellular redox state or proton motive force; similar to E. coli aerotaxis sensor receptor, flavoprotein (AAC76107.1); Blastp hit to AAC76107.1 (506 aa), 83% identity in aa 1 - 506. (506 aa)
msrPPutative nitrate reductase; Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation, including the primary periplasmic chaperone SurA and the lipoprotein Pal. The cata [...] (334 aa)
bfrBacterioferrin; Iron-storage protein, whose ferroxidase center binds Fe(2+) ions, oxidizes them by dioxygen to Fe(3+), and participates in the subsequent Fe(3+) oxide mineral core formation within the central cavity of the protein complex. (158 aa)
STM3820Similar to E. coli putative cytochrome C peroxidase (AAC76543.1); Blastp hit to AAC76543.1 (465 aa), 82% identity in aa 2 - 463. (466 aa)
trxAThioredoxin 1; Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions; Belongs to the thioredoxin family. (109 aa)
cyaYPutative frataxin family transport protein; Involved in iron-sulfur (Fe-S) cluster assembly. May act as a regulator of Fe-S biogenesis. (106 aa)
hslVPeptidase component of the HslUV protease; 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)
dnaKChaperone Hsp70; Acts as a chaperone. (638 aa)
dnaJHeat shock 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, [...] (379 aa)
htrAPeriplasmic serine protease Do, heat shock protein; DegP acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. It degrades transiently denatured and unfolded proteins which accumulate in the periplasm following heat shock or other stress conditions. DegP is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable of being cleaved, thereby preventing non-specific proteolysis of folded proteins. Its proteolyt [...] (475 aa)
clpPProteolytic subunit of clpA-clpP ATP-dependent 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)
htpGChaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity. (632 aa)
sucASimilar to E. coli 2-oxoglutarate dehydrogenase (decarboxylase component) (AAC73820.1); Blastp hit to AAC73820.1 (933 aa), 94% identity in aa 1 - 933. (933 aa)
pepTPutative peptidase T; Cleaves the N-terminal amino acid of tripeptides. Hydrolyzes tripeptides containing N-terminal methionine, leucine, or phenylalanine. Displays little or no activity against dipeptides, N- blocked or C-blocked tripeptides, and tetrapeptides. Belongs to the peptidase M20B family. (409 aa)
fumAFumarase A; Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activity in vitro, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the isomerization of enol- to keto-oxaloacetate. (548 aa)
narJNitrate reductase 1, delta subunit; Chaperone required for molybdenum cofactor assembly in nitrate reductase 1; similar to E. coli nitrate reductase 1, delta subunit, assembly function (AAC74310.1); Blastp hit to AAC74310.1 (236 aa), 88% identity in aa 1 - 236. (236 aa)
htpXHeat shock protein; Integral membrane protein; similar to E. coli heat shock protein, integral membrane protein (AAC74899.1); Blastp hit to AAC74899.1 (293 aa), 96% identity in aa 1 - 293; Belongs to the peptidase M48B family. (293 aa)
mopAChaperone Hsp60 with peptide-dependent ATPase activity; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (548 aa)
soxRRedox-sensing transcriptional activator SoxR; Activates the transcription of the soxS gene which itself controls the superoxide response regulon. SoxR contains a 2Fe-2S iron- sulfur cluster that may act as a redox sensor system that recognizes superoxide. The variable redox state of the Fe-S cluster is employed in vivo to modulate the transcriptional activity of SoxR in response to specific types of oxidative stress (By similarity). (152 aa)
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
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