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InterPro: IPR018337 Cell wall/choline-binding repeat

Protein matchesHelp
UniProtKB
Matches:
1661 proteins
AccessionHelp IPR018337 Cell_wall/Cho-bd_repeat
TypeHelp Repeat
SignaturesHelp
InterPro RelationshipsHelp
Children IPR002479 Putative cell wall binding repeat
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

The cell wall-binding repeat (CW) is an about 20 amino acid residue module, essentially found in two bacterial Gram-positive protein families; the 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, the repeats adopt a solenoid fold consisting exclusively of beta-hairpins that stack to form a left-handed superhelix with a boomerang-like shape. The choline groups bind between beta-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 beta-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 include:
  • 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-beta-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 catalyses 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 cell wall binding repeats are also known as the choline-binding repeats (ChBr) or the choline-binding domain (ChBD).

Structural linksHelp
SCOP: b.109.1.1

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR018337 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P06653 Autolysin

P15057 Lysozyme

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR013781 Glycoside hydrolase, subgroup, catalytic core
IPR018337 Cell wall/choline-binding repeat
IPR002053 Glycoside hydrolase, family 25
IPR002502 N-acetylmuramoyl-L-alanine amidase, family 2
IPR002479 Putative cell wall binding repeat
IPR008270 Glycoside hydrolase, family 25, active site
IPR017853 Glycoside hydrolase, catalytic core
IPR018077 Glycoside hydrolase, family 25 subgroup
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Garcia-Bustos JF, Tomasz A.
Teichoic acid-containing muropeptides from Streptococcus pneumoniae as substrates for the pneumococcal autolysin.
J. Bacteriol. 169 447-53 1987 [PubMed: 2879828]
http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=2879828&action=stream&blobtype=pdf
2. Lopez R, Garcia E.
Recent trends on the molecular biology of pneumococcal capsules, lytic enzymes, and bacteriophage.
FEMS Microbiol. Rev. 28 553-80 2004 [PubMed: 15539074]
http://dx.doi.org/10.1016/j.femsre.2004.05.002
3. Shah DS, Joucla G, Remaud-Simeon M, Russell RR.
Conserved repeat motifs and glucan binding by glucansucrases of oral streptococci and Leuconostoc mesenteroides.
J. Bacteriol. 186 8301-8 2004 [PubMed: 15576779]
http://dx.doi.org/10.1128/JB.186.24.8301-8308.2004
4. Fernandez-Tornero C, Lopez R, Garcia E, Gimenez-Gallego G, Romero A.
A novel solenoid fold in the cell wall anchoring domain of the pneumococcal virulence factor LytA.
Nat. Struct. Biol. 8 1020-4 2001 [PubMed: 11694890]
http://dx.doi.org/10.1038/nsb724
5. Hermoso JA, Monterroso B, Albert A, Galan B, Ahrazem O, Garcia P, Martinez-Ripoll M, Garcia JL, Menendez M.
Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1.
Structure 11 1239-49 2003 [PubMed: 14527392]
http://dx.doi.org/10.1016/j.str.2003.09.005

Additional ReadingHelp
Hermoso JA, Lagartera L, Gonzalez A, Stelter M, Garcia P, Martinez-Ripoll M, Garcia JL, Menendez M.
Insights into pneumococcal pathogenesis from the crystal structure of the modular teichoic acid phosphorylcholine esterase Pce.
Nat. Struct. Mol. Biol. 12 2005 533-8 [PubMed: 15895092]
http://dx.doi.org/10.1038/nsmb940
Fernandez-Tornero C, Garcia E, Lopez R, Gimenez-Gallego G, Romero A.
Two new crystal forms of the choline-binding domain of the major pneumococcal autolysin: insights into the dynamics of the active homodimer.
J. Mol. Biol. 321 2002 163-73 [PubMed: 12139941]
http://dx.doi.org/10.1016/S0022-2836(02)00596-X
Perez-Dorado I, Campillo NE, Monterroso B, Hesek D, Lee M, Paez JA, Garcia P, Martinez-Ripoll M, Garcia JL, Mobashery S, Menendez M, Hermoso JA.
Elucidation of the molecular recognition of bacterial cell wall by modular pneumococcal phage endolysin CPL-1.
J. Biol. Chem. 282 2007 24990-9 [PubMed: 17581815]
http://dx.doi.org/10.1074/jbc.M704317200
Fernandez-Tornero C, Garcia E, de Pascual-Teresa B, Lopez R, Gimenez-Gallego G, Romero A.
Ofloxacin-like antibiotics inhibit pneumococcal cell wall-degrading virulence factors.
J. Biol. Chem. 280 2005 19948-57 [PubMed: 15769740]
http://dx.doi.org/10.1074/jbc.M501236200
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InterPro 23.1