| IED ID |
IndEnz0002004071 |
| Enzyme Type ID |
protease004071 |
| Protein Name |
Antitoxin HipB
|
| Gene Name |
hipB b1508 JW1501 |
| Organism |
Escherichia coli (strain K12) |
| Taxonomic Lineage |
cellular organisms
Bacteria
Proteobacteria
Gammaproteobacteria
Enterobacterales
Enterobacteriaceae
Escherichia
Escherichia coli
Escherichia coli (strain K12)
|
| Enzyme Sequence |
MMSFQKIYSPTQLANAMKLVRQQNGWTQSELAKKIGIKQATISNFENNPDNTTLTTFFKILQSLELSMTLCDAKNASPESTEQQNLEW |
| Enzyme Length |
88 |
| Uniprot Accession Number |
P23873 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
ACTIVITY REGULATION: Degraded by Lon protease; degradation is inhibited in a HipA-HipB complex and when bound to the operator consensus sequence dsDNA. {ECO:0000269|PubMed:22720069}. |
| Binding Site |
|
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
DNA_BIND 21..47; /note="H-T-H motif"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00257, ECO:0000269|PubMed:19150849" |
| EC Number |
|
| Enzyme Function |
FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system. Neutralizes the toxic effect of cognate toxin HipA (PubMed:20616060). Also neutralizes the toxic effect of non-cognate toxin YjjJ (PubMed:28430938). Binds to operator sites with the consensus sequence 5-'TATCCN(8)GGATA-3' to repress the hipBA operon promoter (PubMed:8021189, PubMed:19150849); binding of HipB(2) to DNA induces a 70 degree bend (PubMed:19150849). This forces HipA dimerization, which blocks HipA's active site and thus its toxic action (PubMed:26222023). May play a role in biofilm formation (PubMed:23329678). {ECO:0000269|PubMed:19150849, ECO:0000269|PubMed:20616060, ECO:0000269|PubMed:23329678, ECO:0000269|PubMed:26222023, ECO:0000269|PubMed:28430938, ECO:0000269|PubMed:8021189}. |
| Temperature Dependency |
|
| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Beta strand (1); Chain (1); DNA binding (1); Domain (1); Helix (5); Mutagenesis (2) |
| Keywords |
3D-structure;DNA-binding;Direct protein sequencing;Reference proteome;Repressor;Toxin-antitoxin system;Transcription;Transcription regulation |
| Interact With |
P23874 |
| Induction |
|
| Subcellular Location |
|
| Modified Residue |
|
| Post Translational Modification |
PTM: Degraded by Lon protease in vivo; half-life is 17 minutes in wild-type cells and over 200 minutes in a lon deletion strain. In vitro degradation by Lon is Mg(2+)-ATP-dependent (PubMed:22720069). {ECO:0000269|PubMed:22720069}. |
| Signal Peptide |
|
| Structure 3D |
X-ray crystallography (12) |
| Cross Reference PDB |
2WIU;
3DNV;
3HZI;
4YG1;
4YG4;
4YG7;
4Z58;
4Z59;
4Z5C;
4Z5D;
4Z5H;
5K98;
|
| Mapped Pubmed ID |
16606699;
|
| Motif |
|
| Gene Encoded By |
|
| Mass |
10,016 |
| Kinetics |
|
| Metal Binding |
|
| Rhea ID |
|
| Cross Reference Brenda |
|