STRINGSTRING
relE relE relB relB mazF mazF mazE mazE mqsA mqsA mqsR mqsR higB higB yhaV yhaV yoeB yoeB
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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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query proteins and first shell of interactors
white nodes:
second shell of interactors
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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
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Your Input:
relEQin prophage; Toxic component of a type II toxin-antitoxin (TA) system. A sequence-specific, ribosome-dependent mRNA endoribonuclease that inhibits translation during amino acid starvation (the stringent response). In vitro acts by cleaving mRNA with high codon specificity in the ribosomal A site between positions 2 and 3. The stop codon UAG is cleaved at a fast rate while UAA and UGA are cleaved with intermediate and slow rates. In vitro mRNA cleavage can also occur in the ribosomal E site after peptide release from peptidyl- tRNA in the P site as well as on free 30S subunits. In vivo [...] (95 aa)
relBAntitoxin of the RelE-RelB toxin-antitoxin syste; Antitoxin component of a type II toxin-antitoxin (TA) system. Counteracts the effect of cognate toxin RelE via direct protein-protein interaction, preventing RelE from entering the ribosome A site and thus inhibiting its endoribonuclease activity. An autorepressor of relBE operon transcription. 2 RelB dimers bind to 2 operator sequences; DNA- binding and repression is stronger when complexed with toxin/corepressor RelE by conditional cooperativity. Increased transcription rate of relBE and activation of relE is consistent with a lower l [...] (79 aa)
mazFmRNA interferase toxin, antitoxin is MazE; Toxic component of a type II toxin-antitoxin (TA) system. A sequence-specific endoribonuclease it inhibits protein synthesis by cleaving mRNA and inducing bacterial stasis. It is stable, single- strand specific with mRNA cleavage independent of the ribosome, although translation enhances cleavage for some mRNAs. Cleavage occurs at the 5'-end of ACA sequences, yielding a 2',3'-cyclic phosphate and a free 5'-OH, although cleavage can also occur on the 3'-end of the first A. Digests 16S rRNA in vivo 43 nts upstream of the C- terminus; this remove [...] (111 aa)
mazEAntitoxin of the ChpA-ChpR toxin-antitoxin system; Antitoxin component of a type II toxin-antitoxin (TA) system. Labile antitoxin that binds to the MazF endoribonuclease toxin and neutralizes its endoribonuclease activity. Is considered to be an 'addiction' molecule as the cell dies in its absence. Toxicity results when the levels of MazE decrease in the cell, leading to mRNA degradation. This effect can be rescued by expression of MazE, but after 6 hours in rich medium the overexpression of MazF leads to programmed cell death. Cell growth and viability are not affected when MazF and M [...] (82 aa)
mqsAAntitoxin for MqsR toxin; Antitoxin component of a type II toxin-antitoxin (TA) system. Labile antitoxin that binds to the MqsR mRNA interferase toxin and neutralizes its endoribonuclease activity. Overexpression prevents MqsR-mediated cessation of cell growth and inhibition of cell proliferation. Initially reported to act as a cotranscription factor with MqsA. Following further experiments, the MqsR-MqsA complex does not bind DNA and all reported data are actually due to a small fraction of free MqsA alone binding DNA. Addition of MqsR to a preformed MqsA-promoter DNA complex causes d [...] (131 aa)
mqsRGCU-specific mRNA interferase toxin of the MqsR-MqsA toxin-antitoxin system; Toxic component of a type II toxin-antitoxin (TA) system. Plays a significant role in the control of biofilm formation and induction of persister cells in the presence of antibiotics. An mRNA interferase which has been reported to be translation-independent. It has also been reported to be translation-dependent. Cleavage has been reported to occur on either side of G in the sequence GCU. Also reported to cleave after C in GC(A/U) sequences. There are only 14 genes in E.coli W3110 (and probably also MG1655) tha [...] (98 aa)
higBmRNA interferase toxin of the HigB-HigA toxin-antitoxin system; Toxic component of a type II toxin-antitoxin (TA) system. A probable translation-dependent mRNA interferase. Overexpression causes cessation of cell growth and inhibits cell proliferation via inhibition of translation; this blockage is overcome by subsequent expression of antitoxin HigA. Overexpression causes cleavage of a number of mRNAs in a translation-dependent fashion, suggesting this is an mRNA interferase. mRNA interferases play a role in bacterial persistence to antibiotics; overexpression of this protein induces p [...] (104 aa)
yhaVToxin of the SohB(PrlF)-YhaV toxin-antitoxin system; Toxic component of a type II toxin-antitoxin (TA) system. Has RNase activity in vitro. Overexpression leads to growth arrest after 30 minutes; these effects are overcome by concomitant expression of antitoxin SohA (PrlF). Massive overexpression is toxic. Unlike most other characterized TA systems degrades rRNA, and co-folding of the both TA proteins is necessary in vitro for inhibition of the RNase activity. It is not known if it has any sequence-specificity. Acts as a transcription factor. The YhaV/PrlF complex binds the prlF-yhaV o [...] (154 aa)
yoeBToxin of the YoeB-YefM toxin-antitoxin system; Toxic component of a type II toxin-antitoxin (TA) system. Its mode of function is controversial; it has been proposed to be an mRNA interferase but also an inhibitor of translation initiation. When overproduced in wild-type cells, inhibits bacterial growth and translation by cleavage of mRNA molecules while it has a weak effect on colony forming ability. Overproduction of Lon protease specifically activates YoeB-dependent mRNA cleavage, leading to lethality. YefM binds to the promoter region of the yefM-yeoB operon to repress transcription [...] (84 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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