PROSITE documentation PDOC51782
LysM domain profile


A highly conserved carbohydrate binding module, LysM (lysin-like motif), is found in proteins from viruses, bacteria, fungi, plants and mammals. It is present in bacterial extracellular proteins including hydrolases, adhesins and virulence factors such as Protein A from Staphylococcus aureus. It is also found in proteins produced by fungal pathogens acting as modulators of host immunity, and is present in a large number of proteins from insects, mammals and plants involved in defence against pathogens and symbiotic signalling. LysM modules recognize polysaccharides containing N-acetylglucosamine (GlcNAc) residues including peptidoglycan, an essential component of the bacterial cell wall. Prokaryotic LysM modules bind peptidoglycan, the main component of the bacterial cell wall, made of alternating N-acetylglycosamine (GlcNac) and N-acetylmuramic acid (MurNac) residues, substituted by short peptide stems. In eukaryotes, LysM domains have been shown to bind mainly to chitin, a β 1,4-linked GlcNac polymer that is the main constituent of fungal cell walls, as well as to peptidoglycan [1,2].

LysM modules consist of 43-50 amino acids that adopt a highly conserved βααβ-fold, with the two helices packing onto the same side of a two stranded anti-parallel β-sheet (see <PDB:1E0G>). The sequence conservation is particularly high in the first 16 residues [1,2].

Some proteins known to contain a LysM domain are listed below:

  • Caenorhabditis elegans LysM Domain (Peptidoglycan binding) protein.
  • Kluyveromyces lactis killer toxin subunits α/β.
  • Arabidopsis thaliana LysM domain receptor-like kinases.
  • Listeria probable endopeptidase p60.
  • Haemophilus influenzae probable N-acetylmuramoyl-L-alanine amidase AmiB.
  • Enterococcus faecalis autolysin.
  • Staphylococci immunoglobulin G-binding protein A, helps the bacteria to avoid the immune response.
  • Mycobacterium tuberculosis uncharacterized protein Rv1288.
  • Escherichia coli murein hydrolase activator NlpD, activator of the cell wall hydrolase AmiC.
  • Escherichia coli probable L,D-transpeptidase YnhG.
  • Escherichia coli membrane-bound lytic murein transglycosylase D (mltD), a murein-degrading enzyme.
  • Enterohaemorrhagic and enteropathogenic Escherichia coli intimin, an outer membrane protein required for intimate attachment to mammalian cells.
  • Bacillus subtilis N-acetylmuramoyl-L-alanine amidase XlyA.
  • Bacillus phage phi29 lysozyme, helps to release the mature phage particles from the cell wall by breaking down the peptidoglycan.

The profile we developed covers the entire LysM domain.

Last update:

November 2015 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

LYSM, PS51782; LysM domain profile  (MATRIX)


1AuthorsBateman A. Bycroft M.
TitleThe structure of a LysM domain from E. coli membrane-bound lytic murein transglycosylase D (MltD).
SourceJ. Mol. Biol. 299:1113-1119(2000).
PubMed ID10843862

2AuthorsMesnage S. Dellarole M. Baxter N.J. Rouget J.-B. Dimitrov J.D. Wang N. Fujimoto Y. Hounslow A.M. Lacroix-Desmazes S. Fukase K. Foster S.J. Williamson M.P.
TitleMolecular basis for bacterial peptidoglycan recognition by LysM domains.
SourceNat. Commun. 5:4269-4269(2014).
PubMed ID24978025

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)