IED ID | IndEnz0002012486 |
Enzyme Type ID | protease012486 |
Protein Name |
tRNA threonylcarbamoyladenosine biosynthesis protein TsaB t 6 A37 threonylcarbamoyladenosine biosynthesis protein TsaB |
Gene Name | tsaB yeaZ b1807 JW1796 |
Organism | Escherichia coli (strain K12) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
Enzyme Sequence | MRILAIDTATEACSVALWNDGTVNAHFELCPREHTQRILPMVQDILTTSGTSLTDINALAYGRGPGSFTGVRIGIGIAQGLALGAELPMIGVSTLMTMAQGAWRKNGATRVLAAIDARMGEVYWAEYQRDENGIWHGEETEAVLKPEIVHERMQQLSGEWVTVGTGWQAWPDLGKESGLVLRDGEVLLPAAEDMLPIACQMFAEGKTVAVEHAEPVYLRNNVAWKKLPGKE |
Enzyme Length | 231 |
Uniprot Accession Number | P76256 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | |
Enzyme Function | FUNCTION: Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD. In fact, can act as a protease that specifically degrades TsaD in vitro; therefore TsaB may post-translationally regulate cellular pools of TsaD via proteolytic degradation. Does not show sialoglycoprotease activity against glycophorin A. {ECO:0000269|PubMed:19376873, ECO:0000269|PubMed:22378793}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Beta strand (11); Chain (1); Helix (10); Turn (3) |
Keywords | 3D-structure;Cytoplasm;Reference proteome;tRNA processing |
Interact With | P05852 |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19376873}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (5) |
Cross Reference PDB | 1OKJ; 4WQ4; 4WQ5; 4YDU; 6Z81; |
Mapped Pubmed ID | 15690043; 16606699; 24561554; 24914962; 25578970; 33524148; |
Motif | |
Gene Encoded By | |
Mass | 25,181 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |