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fliA fliA flgK flgK flgI flgI flgE flgE flgH flgH flgB flgB htrA htrA nagA nagA flgM flgM ptr ptr rpoS rpoS csrA csrA STM2446 STM2446 fliF fliF fliD fliD fliC fliC flgL flgL dnaK dnaK polB polB
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)
flgKHook-filament junction protein 1; Flagellar biosynthesis protein; flagellar hook-associated protein 1 (HAP1). (SW:FLGK_SALTY); Belongs to the flagella basal body rod proteins family. (553 aa)
flgIPutative flagella basal body protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (365 aa)
flgEHook protein; Flagellar biosynthesis; flagellar hook protein flge. (SW:FLGE_SALTY); Belongs to the flagella basal body rod proteins family. (403 aa)
flgHFlagellar biosynthesis protein; Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation. (232 aa)
flgBFlagellar biosynthesis protein; Structural component of flagellum, the bacterial motility apparatus. Part of the rod structure of flagellar basal body. (138 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)
nagASimilar to E. coli N-acetylglucosamine-6-phosphate deacetylase (AAC73771.1); Blastp hit to AAC73771.1 (382 aa), 92% identity in aa 1 - 380. (384 aa)
flgManti-FliA factor; Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of FliA by directly binding to FliA; Belongs to the FlgM family. (97 aa)
ptrProtease III; Endopeptidase that degrades small peptides of less than 7 kDa, such as glucagon and insulin. (962 aa)
rpoSSigma S (sigma 38) 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 is the master transcriptional regulator of the stationary phase and the general stress response. (330 aa)
csrACarbon storage regulator; A key translational regulator that binds mRNA to regulate translation initiation and/or mRNA stability. Mediates global changes in gene expression, shifting from rapid growth to stress survival by linking envelope stress, the stringent response and the catabolite repression systems. Usually binds in the 5'-UTR; binding at or near the Shine-Dalgarno sequence prevents ribosome-binding, repressing translation, binding elsewhere in the 5'-UTR can activate translation and/or stabilize the mRNA. Its function is antagonized by small RNA(s). (61 aa)
STM2446Putative iron-dependent peroxidase; Similar to E. coli orf, hypothetical protein (AAC75484.1); Blastp hit to AAC75484.1 (308 aa), 94% identity in aa 10 - 308. (299 aa)
fliFBasal-body MS (membrane and supramembrane)-ring and collar protein; The M ring may be actively involved in energy transduction. (560 aa)
fliDFilament capping protein; Required for the morphogenesis and for the elongation of the flagellar filament by facilitating polymerization of the flagellin monomers at the tip of growing filament. Forms a capping structure, which prevents flagellin subunits (transported through the central channel of the flagellum) from leaking out without polymerization at the distal end; Belongs to the FliD family. (467 aa)
fliCFlagellar biosynthesis; Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella. (495 aa)
flgLHook-filament junction protein; Flagellar biosynthesis protein; flagellar hook-associated protein 3 (HAP3) (hook-filament junctionprotein). (SW:FLGL_SALTY). (317 aa)
dnaKChaperone Hsp70; Acts as a chaperone. (638 aa)
polBDNA polymerase II; 3'->5' exonuclease; similar to E. coli DNA polymerase II (AAC73171.1); Blastp hit to AAC73171.1 (783 aa), 89% identity in aa 1 - 783. (783 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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