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PROSITE documentation PDOC51170

Cell wall-binding repeat profile





Description

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 2.4.1.5). 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 3.5.1.28). 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 3.2.1.96). 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.

Note:

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.

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Technical section

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

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


References

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
DOI10.1016/j.femsre.2004.05.002

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
DOI10.1128/JB.186.24.8301-8308.2004

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
DOI10.1038/nsb724

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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