IED ID | IndEnz0002013225 |
Enzyme Type ID | protease013225 |
Protein Name |
Toxin YoeB EC 3.1.-.- Putative endoribonuclease YoeB Putative mRNA interferase Yoeb |
Gene Name | yoeB b4539 JW5331 |
Organism | Escherichia coli (strain K12) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
Enzyme Sequence | MKLIWSEESWDDYLYWQETDKRIVKKINELIKDTRRTPFEGKGKPEPLKHNLSGFWSRRITEEHRLVYAVTDDSLLIAACRYHY |
Enzyme Length | 84 |
Uniprot Accession Number | P69348 |
Absorption | |
Active Site | ACT_SITE 46; /note=Proton acceptor; /evidence=ECO:0000305|PubMed:16109374; ACT_SITE 83; /note=Proton donor; /evidence=ECO:0000305|PubMed:16109374 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.1.-.- |
Enzyme Function | FUNCTION: 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, YeoB acts as a corepressor.; FUNCTION: Shown in vitro to be an mRNA interferase that requires translation for substrate cleavage; if the mRNA is mutated so as to not be translatable it is no longer cleaved. Cleavage only occurs within translated regions. Has RNase activity and preferentially cleaves at the 3'-end of purine ribonucleotides. {ECO:0000269|PubMed:16109374}.; FUNCTION: Also shown in vitro to be a translation initiation blocker. Binds to the 70S ribosome and 50S ribosomal subunit; binding is inhibited by hygromycin A and tetracycline, both of which bind to the 30S subunit in the A site. Thus YoeB is located at the interface between 50S and 30S ribosomes and interacts with the A site where it cleaves mRNA, blocking translation initiation. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Beta strand (4); Chain (1); Helix (3); Mutagenesis (3) |
Keywords | 3D-structure;Endonuclease;Hydrolase;Nuclease;RNA-binding;Reference proteome;Repressor;Toxin-antitoxin system;Transcription;Transcription regulation |
Interact With | |
Induction | INDUCTION: Repressed by YefM, more strongly repressed by the YefM(2)YoeB heterotrimer. Induced in persister cells. Ectopic expression of Salmonella or Shigella toxin VapC induces the yefM-yoeB operon and also induces Yoeb toxin activity in a Lon protease-dependent manner. {ECO:0000269|PubMed:16768798, ECO:0000269|PubMed:17170003, ECO:0000269|PubMed:19400780}. |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (5) |
Cross Reference PDB | 2A6Q; 2A6R; 2A6S; 4V8X; 6NY6; |
Mapped Pubmed ID | 23945936; 24028219; 24561554; 31501867; |
Motif | |
Gene Encoded By | |
Mass | 10,216 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |