Detail Information for IndEnz0002013225
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