Detail Information for IndEnz0002004188
IED ID IndEnz0002004188
Enzyme Type ID protease004188
Protein Name Antitoxin HicB
Gene Name hicB ydcQ b1438 JW1433
Organism Escherichia coli (strain K12)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12)
Enzyme Sequence MRYPVTLTPAPEGGYMVSFVDIPEALTQGETVAEAMEAAKDALLTAFDFYFEDNELIPLPSPLNSHDHFIEVPLSVASKVLLLNAFLQSEITQQELARRIGKPKQEITRLFNLHHATKIDAVQLAAKALGKELSLVMV
Enzyme Length 138
Uniprot Accession Number P67697
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding DNA_BIND 93..112; /note=H-T-H motif; /evidence=ECO:0000255|PROSITE-ProRule:PRU00257
EC Number
Enzyme Function FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system. Functions as an mRNA interferase antitoxin; overexpression prevents HicA-mediated cessation of cell growth and inhibition of cell proliferation. {ECO:0000269|PubMed:19060138}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Beta strand (6); Chain (1); DNA binding (1); Domain (1); Erroneous initiation (1); Helix (5)
Keywords 3D-structure;DNA-binding;Reference proteome;Repressor;Stress response;Toxin-antitoxin system;Transcription;Transcription regulation
Interact With
Induction INDUCTION: Induced by amino acid starvation, carbon starvation and when translation is blocked. Induction no longer occurs in the absence of Lon protease suggesting, by homology to other toxin-antitoxin systems, that Lon may degrade the HicB antitoxin. A member of the hicA-hicB operon. {ECO:0000269|PubMed:19060138}.
Subcellular Location
Modified Residue
Post Translational Modification PTM: May be degraded by Lon protease. {ECO:0000250}.
Signal Peptide
Structure 3D X-ray crystallography (2)
Cross Reference PDB 6HPB; 6HPC;
Mapped Pubmed ID 15556475; 24561554; 31495532;
Motif
Gene Encoded By
Mass 15,247
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda