Protein Summary

TsaE from Escherichia coli

Full name: tRNA N6-threonylcarbamoyladenosine(37) synthesis protein
Synonym: YjeE
GI: 16131990
Orf:
COG: COG0802
UniProt: P0AF67
Structures: | |
Complex: TsaBDE
Enzyme type: ATPase
Position of modification - modification: t:37 - t6A

Comments:

This protein belongs to P-loop ATPases. It binds ATP and displays a weak ATPase activity (produce ADP). This protein tends to oligomerize in vitro. Despite TsaC (YrdC), TsaD (YgjD) and TsaB (YeaZ) are present in all bacteria, TsaE (YjeE) is absent in several unicellular and symbiotic bacteria, suggesting that some bacteria can carry out t6A synthesis in absence of YjeE. However, TsaD, TsaC, TsaE and TsaB are both necessary and sufficient for t6A biosynthesis in vitro.

Protein sequence:

MMNRVIPLPDEQATLDLGERVAKACDGATVIYLYGDLGAGKTTFSRGFLQ
ALGHQGNVKSPTYTLVEPYTLDNLMVYHFDLYRLADPEELEFMGIRDYFA
NDAICLVEWPQQGTGVLPDPDVEIHIDYQAQGREARVSAVSSAGELLLAR
LAG

Publications

Title Authors Journal Details PubMed Id DOI
Biosynthesis of threonylcarbamoyl adenosine (t6A), a universal tRNA nucleoside. Deutsch C, El Yacoubi B, de Crecy-Lagard V, Iwata-Reuyl D J Biol Chem [details] 22378793 -
Effects on transcription of mutations in ygjD, yeaZ, and yjeE genes, which are involved in a universal tRNA modification in Escherichia coli. Hashimoto C, Sakaguchi K, Taniguchi Y, Honda H, Oshima T, Ogasawara N, Kato J J Bacteriol [details] 21873492 -
Known bioactive small molecules probe the function of a widely conserved but enigmatic bacterial ATPase, YjeE. Mangat CS, Brown ED Chem Biol [details] 19101473 -
Conserved P-loop GTPases of unknown function in bacteria: an emerging and vital ensemble in bacterial physiology. Brown ED Biochem Cell Biol [details] 16333325 -
Mechanism of N6-threonylcarbamoyladenonsine (t(6)A) biosynthesis: isolation and characterization of the intermediate threonylcarbamoyl-AMP. Lauhon CT... Biochemistry [details] 23072323 -

Last modification of this entry: 2014-06-04 20:55:10.719657
Edited by a user: magda
Edited content: Changed complex.