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fliA fliA htpG htpG flgC flgC adhE adhE motB motB fliG fliG fliM fliM fliN fliN gyrA gyrA pta pta grpE grpE tpiA tpiA rpoB rpoB 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.
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:
fliASigma F (sigma 28) factor of RNA polymerase; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes. May regulate the expression of genes involved in virulence. (239 aa)
htpGChaperone Hsp90, heat shock protein C 62.5; Molecular chaperone. Has ATPase activity. (632 aa)
flgCFlagellar biosynthesis protein; Cell-proximal portion of basal-body rod; flagellar basal-body rod protein FLGC (putative proximal rod protein). (SW:FLGC_SALTY); Belongs to the flagella basal body rod proteins family. (134 aa)
adhESimilar to E. coli CoA-linked acetaldehyde dehydrogenase and iron-dependent alcohol dehydrogenase; pyruvate-formate-lyase deactivase (AAC74323.1); Blastp hit to AAC74323.1 (891 aa), 97% identity in aa 1 - 891; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family. (892 aa)
motBEnables flagellar motor rotation; MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity). (309 aa)
fliGFlagellar biosynthesis protein; FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity). (331 aa)
fliMFlagellar biosynthesis protein; FliM is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity). (334 aa)
fliNFlagellar biosynthesis protein; FliN is one of three proteins (FliG, FliN, FliM) that form the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity). Belongs to the FliN/MopA/SpaO family. (137 aa)
gyrADNA gyrase, subunit A; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state, and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. Replenishes negative supercoiling downstream of highly transcribed genes to help control overall chromosomal supercoiling density. E.coli makes 15% more negative supercoils in pBR322 plasmid DNA than S.typhimurium; the S.typhimurium GyrB s [...] (878 aa)
ptaPhosphotransacetylase; Involved in acetate metabolism. Catalyzes the reversible interconversion of acetyl-CoA and acetyl phosphate. The direction of the overall reaction changes depending on growth conditions. Required for acetate recapture but not for acetate excretion when this organism is grown on ethanolamine; In the N-terminal section; belongs to the CobB/CobQ family. (714 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)
tpiATriosephosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family. (255 aa)
rpoBRNA polymerase, beta subunit; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. (1342 aa)
mopBChaperone Hsp10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. (97 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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