PROSITE documentation PDOC51170
Cell wall-binding repeat profile


The cell wall-binding repeat (CW) is a ~20 amino acid residue module essentially found in two bacterial Gram-positive protein families: choline binding proteins and glucosyltransferases (EC In choline-binding proteins cell wall binding repeats bind to choline moieties of both teichoic and lipoteichoic acids, two components peculiar to the cell surface of Gram-positive bacteria [1,2]. In glucosyltransferases the region spanning the CW repeats is a glucan binding domain [3].

Several crystal structures of CW have been solved [4,5]. In the choline binding protein LytA (see <PDB:1HCX>), the repeats adopt a solenoid fold consisting exclusively of β-hairpins that stack to form a left-handed superhelix with a boomerang-like shape. The choline groups bind between β-hairpin 'steps' of the superhelix [4]. In Cpl-1 CW repeats assemble in two sub-domains: an N-terminal superhelical moiety similar to the LytA one and a C-terminal β-sheet involved in interactions with the lysozyme domain. Choline is bound between repeats 1 and 2, and, 2 and 3 of the superhelical sub-domain [5].

Some proteins known to contain cell-wall binding repeats:

  • Pneumococcal N-acetylmuramoyl-L-alanine amidase (autolysin, lytA) (EC It is a surface-exposed enzyme that rules the self-destruction of pneumococcal cells through degradation of their peptidoglycan backbone. It mediates the release of toxic substances that damage the host tissues.
  • Pneumococcal endo-β-N-acetylglucosaminidase (lytB) (EC It plays an important role in cell wall degradation and cell separation
  • Pneumococcal teichoic acid phosphorylcholine esterase (pce or cbpE), a cell wall hydrolase important for cellular adhesion and colonisation.
  • Lactobacillales glucosyltransferase. It catalyzes the transfer of glucosyl units from the cleavage of sucrose to a growing chain of glucan.
  • Clostridium difficile toxin A (tcdA) and toxin B (tcdb). They are the causative agents of the antibiotic-associated pseudomembranous colitis. They are intracellular acting toxins that reach their targets after receptor-mediated endocytosis.
  • Clostridium acetobutylicum cspA protein.
  • Siphoviridae bacteriophages N-acetylmuramoyl-L-alanine amidase. It lyses the bacterial host cell wall.
  • Podoviridae lysozyme protein (cpl-1). It is capable of digesting the pneumococcal cell wall.

The profile we developed covers the 20 amino acids of the CW repeat.


The cell wall binding repeats are also known as the choline-binding repeats (ChBr) or the choline-binding domain (ChBD).

Last update:

December 2005 / First entry.


Technical section

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

CW, PS51170; Cell wall-binding repeat profile  (MATRIX)


1AuthorsGarcia-Bustos J.F. Tomasz A.
TitleTeichoic acid-containing muropeptides from Streptococcus pneumoniae as substrates for the pneumococcal autolysin.
SourceJ. Bacteriol. 169:447-453(1987).
PubMed ID2879828

2AuthorsLopez R. Garcia E.
TitleRecent trends on the molecular biology of pneumococcal capsules, lytic enzymes, and bacteriophage.
SourceFEMS. Microbiol. Rev. 28:553-580(2004).
PubMed ID15539074

3AuthorsShah D.S. Joucla G. Remaud-Simeon M. Russell R.R.
TitleConserved repeat motifs and glucan binding by glucansucrases of oral streptococci and Leuconostoc mesenteroides.
SourceJ. Bacteriol. 186:8301-8308(2004).
PubMed ID15576779

4AuthorsFernandez-Tornero C. Lopez R. Garcia E. Gimenez-Gallego G. Romero A.
TitleA novel solenoid fold in the cell wall anchoring domain of the pneumococcal virulence factor LytA.
SourceNat. Struct. Biol. 8:1020-1024(2001).
PubMed ID11694890

5AuthorsHermoso J.A. Monterroso B. Albert A. Galan B. Ahrazem O. Garcia P. Martinez-Ripoll M. Garcia J.L. Menendez M.
TitleStructural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1.
SourceStructure 11:1239-1249(2003).
PubMed ID14527392

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