Protein Family Models

This domain can be found in the C-terminal region of phosphatidylglycerol lysyltransferase mprF, which catalyses the transfer of a lysyl group from L-lysyl-tRNA(Lys) to to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG) [1,3]. This domain can also be found in lysylphosphatidylglycerol biosynthesis bifunctional protein LysX, which is the two-domain lysyl-transferase (mprF)-lysyl-tRNA synthetase (lysU) protein is responsible for LPG production [2]. [1]. 14769468. MprF-mediated biosynthesis of lysylphosphatidylglycerol, an important determinant in staphylococcal defensin resistance. Staubitz P, Neumann H, Schneider T, Wiedemann I, Peschel A;. FEMS Microbiol Lett. 2004;231:67-71. [2]. 19649276. The two-domain LysX protein of Mycobacterium tuberculosis is required for production of lysinylated phosphatidylglycerol and resistance to cationic antimicrobial peptides. Maloney E, Stankowska D, Zhang J, Fol M, Cheng QJ, Lun S, Bishai WR, Rajagopalan M, Chatterjee D, Madiraju MV;. PLoS Pathog. 2009;5:e1000534. [3]. 30563904. Gain-of-Function Mutations in the Phospholipid Flippase MprF Confer Specific Daptomycin Resistance. Ernst CM, Slavetinsky CJ, Kuhn S, Hauser JN, Nega M, Mishra NN, Gekeler C, Bayer AS, Peschel A;. mBio. 2018; [Epub ahead of print] (from Pfam)

Date:

2024-10-16

LPG_synthase_TM is the N-terminal region of this family of bacterial phosphatidylglycerol lysyltransferases. The function of the family is to add lysyl groups to membrane lipids, and this region is the transmembrane domain of 7xTMs. In order to counteract attack by membrane-damaging external cationic antimicrobial molecules - from host immune systems, bacteriocins, defensins, etc - bacteria modify their anionic membrane phosphatidylglycerol with positively-charged L-lysine; this results in repulsion of the foreign cationic peptides [1,2,3]. [1]. 11342591. Staphylococcus aureus resistance to human defensins and evasion of neutrophil killing via the novel virulence factor MprF is based on modification of membrane lipids with l-lysine. Peschel A, Jack RW, Otto M, Collins LV, Staubitz P, Nicholson G, Kalbacher H, Nieuwenhuizen WF, Jung G, Tarkowski A, van Kessel KP, van Strijp JA;. J Exp Med 2001;193:1067-1076. [2]. 12496209. MprF-mediated lysinylation of phospholipids in Staphylococcus aureus leads to protection against oxygen-independent neutrophil killing. Kristian SA, Durr M, Van Strijp JA, Neumeister B, Peschel A;. Infect Immun. 2003;71:546-549. [3]. 14769468. MprF-mediated biosynthesis of lysylphosphatidylglycerol, an important determinant in staphylococcal defensin resistance. Staubitz P, Neumann H, Schneider T, Wiedemann I, Peschel A;. FEMS Microbiol Lett. 2004;231:67-71. (from Pfam)

Date:

2024-10-16

The C-terminal region of MprF tranfers lysine from a charged tRNA onto phosphatidylglycerol to make lysylphosphatidylglycerol (EC 2.3.2.3). The N-terminal region of MprF acts as a flippase. MprF helps confer resistance to antimicrobial cationic peptides.

Gene:

mprF

Date:

2020-10-26

Members of this family show sequence homology to the flippase region of lysylphosphatidylglycerol synthetase/flippase proteins. Characterized members include AglD (archaeal glycosylation protein) of Haloferax volcanii, which also has a glycosyltransferase domain and which is involved in biosynthesis of a pentasaccharide moiety for N-linked glycosylation of the S-layer-forming major cell surface glycoprotein.

Date:

2019-09-10