YjjX: from structure "Tu" function.
It has been shown by structural analysis that YjjX, a hypothetical protein in E. coli, is an ITPase/XTPase and suggest that it may play dual roles in prokaryotic translational regulation and oxidative cell stress response.
Rao
Zihe
Z
National Laboratory of Biomacromolecules, Institute of Biophysics (IBP), Chinese Academy of Sciences, Beijing 100101, China.
D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics; D001665:Binding Sites; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics; D005786:Gene Expression Regulation; D007293:Inosine Triphosphate / Q000737:chemistry; D017017:Methanococcus / Q000201:enzymology / Q000235:genetics; D010444:Peptide Elongation Factor Tu / Q000378:metabolism*; D011485:Protein Binding; D017510:Protein Folding; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D012265:Ribonucleotides / Q000737:chemistry; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; C081169:Maf protein, Bacillus subtilis; D012265:Ribonucleotides; D007293:Inosine Triphosphate; C065326:xanthosine 5'-triphosphate; D010444:Peptide Elongation Factor Tu