135  structures 82  species 3  interactions 7386  sequences 258  architectures

Family: CW_binding_1 (PF01473)

Summary

Putative cell wall binding repeat Add an annotation

These repeats are characterised by conserved aromatic residues and glycines are found in multiple tandem copies in a number of proteins. The CW repeat is 20 amino acid residues long. The exact domain boundaries may not be correct. It has been suggested that these repeats in P15057 might be responsible for the specific recognition of choline-containing cell walls [1]. Similar but longer repeats are found in the glucosyltransferases and glucan-binding proteins of oral streptococci and shown to be involved in glucan binding [2] as well as in the related dextransucrases of Leuconostoc mesenteroides. Repeats also occur in toxins of Clostridium difficile and other clostridia, though the ligands are not always known.


Literature references

  1. Garcia E, Garcia JL, Garcia P, Arraras A, Sanchez-Puelles JM, Lopez R; , Proc Natl Acad Sci U S A 1988;85:914-918.: Molecular evolution of lytic enzymes of Streptococcus pneumoniae and its bacteriophages. PUBMED:3422470

  2. Hermoso JA, Monterroso B, Albert A, Galan B, Ahrazem O, Garcia P, Martinez-Ripoll M, Garcia JL, Menendez M; , Structure (Camb) 2003;11:1239-1249.: Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1. PUBMED:14527392

  3. Sanchez-Beato AR, Ronda C, Garcia JL; , J Bacteriol 1995;177:1098-1103.: Tracking the evolution of the bacterial choline-binding domain: molecular characterization of the Clostridium acetobutylicum NCIB 8052 cspA gene. PUBMED:7860591

  4. Wren BW; , Mol Microbiol 1991;5:797-803.: A family of clostridial and streptococcal ligand-binding proteins with conserved C-terminal repeat sequences. PUBMED:1830357

  5. Banas JA, Russell RR, Ferretti JJ; , Infect Immun 1990;58:667-673.: Sequence analysis of the gene for the glucan-binding protein of Streptococcus mutans Ingbritt. PUBMED:2307516

  6. Ferretti JJ, Gilpin ML, Russell RR; , J Bacteriol 1987;169:4271-4278.: Nucleotide sequence of a glucosyltransferase gene from Streptococcus sobrinus MFe28. PUBMED:3040686

  7. Janecek S, Svensson B, Russell RR; , FEMS Microbiol Lett 2000;192:53-57.: Location of repeat elements in glucansucrases of Leuconostoc and Streptococcus species. PUBMED:11040428


InterPro entry IPR002479

This repeat is found in multiple tandem copies in several proteins. The repeat is 20 amino acid residues long. It has been suggested that these repeats in might be responsible for the specific recognition of choline-containing cell walls PUBMED:3422470. Similar repeats are found in the glucosyltransferases and glucan-binding protein of oral streptococci, dextransucrases of Leuconostoc mesenteroides as well as toxins of Clostridium difficile PUBMED:15576779.

External database links

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...

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Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.

You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.

Pfam alignments:
Full length sequences

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.

Pfam alignments:

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.

Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Bateman A
Previous IDs: none
Type: Repeat
Author: Bateman A, Mistry J, Russell R
Number in seed: 213
Number in full: 7386
Average length of the domain: 18.70 aa
Average identity of full alignment: 40 %
Average coverage of the sequence by the domain: 3.08 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 20.5 9.8
Trusted cut-off 20.5 9.8
Noise cut-off 20.4 9.7
Model length: 19
Family (HMM) version: 13
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 3 interactions for this family. More...

Glyco_hydro_25 Lactamase_B CW_binding_1

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the CW_binding_1 domain has been found.

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