This family includes a range of acyltransferase enzymes. This domain is found in a wide range of acyltransferase enzymes, including, mainly, bacterial proteins which catalyse the transfer of acyl groups, other than amino-acyl, from one compound to another, such as Glucans biosynthesis protein C (OPGC) or protein OatA from Listeria monocytogenes serovar 1/2a and Staphylococcus aureus, an integral membrane protein which is responsible for O-acetylation at the C6-hydroxyl group of N-acetylmuramyl residues, forming the corresponding N,6-O-diacetylmuramic acid of the peptidoglycan, a modification that determines lysozyme resistance [1,2]. This domain is also present in eukaryotic proteins, namely O-acyltransferase like protein (OACYL) from mouse and RHY1 (Regulator of hypoxia-inducible factor 1) [3] and NRF6 (Nose resistant to fluoxetine protein 6) from Caenorhabditis elegans [4]. [1]. 21844299. OatA, a peptidoglycan O-acetyltransferase involved in Listeria monocytogenes immune escape, is critical for virulence. Aubry C, Goulard C, Nahori MA, Cayet N, Decalf J, Sachse M, Boneca IG, Cossart P, Dussurget O;. J Infect Dis. 2011;204:731-740. [2]. 32350117. Structural basis for the O-acetyltransferase function of the extracytoplasmic domain of OatA from Staphylococcus aureus. Jones CS, Sychantha D, Howell PL, Clarke AJ;. J Biol Chem. 2020;295:8204-8213. [3]. 16980385. The Caenorhabditis elegans rhy-1 gene inhibits HIF-1 hypoxia-inducible factor activity in a negative feedback loop that does not include vhl-1. Shen C, Shao Z, Powell-Coffman JA;. Genetics. 2006;174:1205-1214. [4]. 16118202. Fluoxetine-resistance genes in Caenorhabditi. TRUNCATED at 1650 bytes (from Pfam)
GO Terms:- Molecular Function:
- acyltransferase activity, transferring groups other than amino-acyl groups (GO:0016747)
- Date:
- 2024-10-16