| IED ID |
IndEnz0002007480 |
| Enzyme Type ID |
protease007480 |
| Protein Name |
Antitoxin RelB
|
| Gene Name |
relB b1564 JW1556 |
| Organism |
Escherichia coli (strain K12) |
| Taxonomic Lineage |
cellular organisms
Bacteria
Proteobacteria
Gammaproteobacteria
Enterobacterales
Enterobacteriaceae
Escherichia
Escherichia coli
Escherichia coli (strain K12)
|
| Enzyme Sequence |
MGSINLRIDDELKARSYAALEKMGVTPSEALRLMLEYIADNERLPFKQTLLSDEDAELVEIVKERLRNPKPVRVTLDEL |
| Enzyme Length |
79 |
| Uniprot Accession Number |
P0C079 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
|
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
|
| Enzyme Function |
FUNCTION: 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 (PubMed:18501926, PubMed:22981948). Increased transcription rate of relBE and activation of relE is consistent with a lower level of RelB in starved cells due to degradation of RelB by protease Lon. {ECO:0000269|PubMed:11274135, ECO:0000269|PubMed:11717402, ECO:0000269|PubMed:12123459, ECO:0000269|PubMed:18501926, ECO:0000269|PubMed:18532983, ECO:0000269|PubMed:19707553, ECO:0000269|PubMed:19747491, ECO:0000269|PubMed:22210768, ECO:0000269|PubMed:22981948, ECO:0000269|PubMed:9767574}.; FUNCTION: Seems to be a principal mediator of cell death in liquid media. {ECO:0000269|PubMed:19707553}. |
| Temperature Dependency |
|
| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Beta strand (2); Chain (1); Helix (4); Mutagenesis (9) |
| Keywords |
3D-structure;DNA-binding;Reference proteome;Repressor;Stress response;Toxin-antitoxin system;Transcription;Transcription regulation |
| Interact With |
P0C077 |
| Induction |
INDUCTION: By amino acid starvation, by glucose starvation and by chloramphenicol; induction is independent of ppGpp. Autorepressed by RelB, RelE acts as a corepressor (PubMed:9767574, PubMed:19747491, PubMed:18501926, PubMed:22981948). Member of the relBEF operon (PubMed:2990907). Operon induced by ectopic expression of toxins HicA, HipA, MazF, MqsR and RelE, but not by YafQ (PubMed:23432955). {ECO:0000269|PubMed:11717402, ECO:0000269|PubMed:18501926, ECO:0000269|PubMed:18532983, ECO:0000269|PubMed:19747491, ECO:0000269|PubMed:22981948, ECO:0000269|PubMed:23432955, ECO:0000269|PubMed:2990907, ECO:0000269|PubMed:9767574}. |
| Subcellular Location |
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| Modified Residue |
|
| Post Translational Modification |
PTM: Probably degraded by Lon protease during amino acid starvation (PubMed:11717402). Degraded in vitro by Lon (PubMed:19747491). {ECO:0000269|PubMed:11717402, ECO:0000269|PubMed:19747491}. |
| Signal Peptide |
|
| Structure 3D |
NMR spectroscopy (2); X-ray crystallography (1) |
| Cross Reference PDB |
2K29;
2KC8;
4FXE;
|
| Mapped Pubmed ID |
16606699;
|
| Motif |
|
| Gene Encoded By |
|
| Mass |
9,071 |
| Kinetics |
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| Metal Binding |
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| Rhea ID |
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| Cross Reference Brenda |
|