Protein Family Models

Pair of presumed choline-binding repeats often found adjacent to Pfam:PF01473. (from Pfam)

Date:

2024-08-14

this entry contains a pair of presumed choline-binding repeats that are often found adjacent to Pfam:PF01473. [1]. 27917891. Modular Architecture and Unique Teichoic Acid Recognition Features of Choline-Binding Protein L (CbpL) Contributing to Pneumococcal Pathogenesis. Gutierrez-Fernandez J, Saleh M, Alcorlo M, Gomez-Mejia A, Pantoja-Uceda D, Trevino MA, Voss F, Abdullah MR, Galan-Bartual S, Seinen J, Sanchez-Murcia PA, Gago F, Bruix M, Hammerschmidt S, Hermoso JA;. Sci Rep. 2016;6:38094. (from Pfam)

Date:

2024-10-16

This domain is found in a wide range of extracellular proteins. It is found tandemly repeated in up to 8 copies. It is found in the N-terminus of peptidases belonging to the M26 family which cleave human IgA. The domain is also found in proteins involved in metabolism of bacterial cell walls suggesting this domain may have an adhesive function. [1]. 18992255. Crystal structure of the resuscitation-promoting factor (DeltaDUF)RpfB from M. tuberculosis. Ruggiero A, Tizzano B, Pedone E, Pedone C, Wilmanns M, Berisio R;. J Mol Biol. 2009;385:153-162. [2]. 15598841. The G5 domain: a potential N-acetylglucosamine recognition domain involved in biofilm formation. Bateman A, Holden MT, Yeats C;. Bioinformatics. 2005;21:1301-1303. (from Pfam)

Date:

2024-10-16

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 Swiss: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. [1]. 3422470. Molecular evolution of lytic enzymes of Streptococcus pneumoniae and its bacteriophages. Garcia E, Garcia JL, Garcia P, Arraras A, Sanchez-Puelles JM, Lopez R;. Proc Natl Acad Sci U S A 1988;85:914-918. [2]. 14527392. Structural basis for selective recognition of pneumococcal cell wall by modular endolysin from phage Cp-1. 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. [3]. 7860591. Tracking the evolution of the bacterial choline-binding domain: molecular characterization of the Clostridium acetobutylicum NCIB 8052 cspA gene. Sanchez-Beato AR, Ronda C, Garcia JL;. J Bacteriol 1995;177:1098-1103. [4]. 1830357. A family of clostridial and streptococcal ligand-binding proteins with conserved C-terminal repeat sequences. Wren BW;. Mol Microbiol 1991;5:797-803. [5]. 2307516. Sequence analysis of the gene. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-10-16

Members of this family share C-terminal homology to the choline-binding form of the pneumococcal surface antigen PspC, but not to its allelic LPXTG-anchored forms because they lack the choline-binding repeat region. Members of this family should not be confused with PspC itself, whose identity and function reflect regions N-terminal to the choline-binding region. See Iannelli, et al. (PMID: 11891047) for information about the different allelic forms of PspC.

Date:

2020-10-26