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dnaK dnaK lpxA lpxA acrR acrR htpG htpG clpA clpA fliC fliC dedA dedA hscA hscA grpE grpE fljB fljB hflB hflB yicF yicF ibpB ibpB ibpA ibpA 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.
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:
dnaKChaperone Hsp70; Acts as a chaperone. (638 aa)
lpxAUDP-N-acetylglucosamine acetyltransferase; Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. (262 aa)
acrRSimilar to E. coli acrAB operon repressor (AAC73566.1); Blastp hit to AAC73566.1 (215 aa), 87% identity in aa 1 - 214. (217 aa)
htpGChaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity. (632 aa)
clpASimilar to E. coli ATP-binding component of serine protease (AAC73969.1); Blastp hit to AAC73969.1 (758 aa), 97% identity in aa 1 - 758; Belongs to the ClpA/ClpB family. (758 aa)
fliCFlagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (495 aa)
dedAPutative DedA family; Similar to E. coli orf, hypothetical protein (AAC75377.1); Blastp hit to AAC75377.1 (219 aa), 96% identity in aa 1 - 219. (219 aa)
hscAChaperone protein; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB. Involved in the maturation of IscU. (616 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)
fljBFilament structural protein; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (506 aa)
hflBATP-dependent zinc-metallo protease; Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins; In the central section; belongs to the AAA ATPase family. (644 aa)
yicFPutative DNA ligase; Catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. Belongs to the NAD-dependent DNA ligase family. LigB subfamily. (561 aa)
ibpBSmall heat 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)
ibpASmall heat 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)
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)
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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