Protein Family Models

This entry represents a novel form of signal peptide that occurs as an N-terminal domain with a recognizable motif, reminiscent of the YSIRK signal peptide. (from Pfam)

Date:

2024-08-14

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

Date:

2024-08-14

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

This model describes a region of about 63 amino acids that is composed of three repeats of a more broadly distributed family of shorter repeats modeled by Pfam model PF01473. While the shorter repeats are often associated with choline binding (and therefore with cell wall binding), the longer repeat described here represents a subgroup of repeat sequences associated with glucan binding, as found in a number glycosylhydrolases. Shah, et al. describe a repeat consensus, WYYFDANGKAVTGAQTINGQTLYFDQDGKQVKG, that corresponds to half of the repeat as modeled here and one and a half copies of the repeat as modeled by PF01473.

Date:

2023-11-14

This model describes a novel form of signal peptide that occurs as an N-terminal domain with a recognizable motif, reminiscent of the YSIRK and PEP-CTERM forms of signal peptide. This domain tends to occur on long, low-complexity (usually Serine-rich and heavily glycosylated) proteins of the Firmicutes, and (as with YSIRK) the majority of these proteins have the LPXTG cell wall-anchoring motif at the C-terminus.

Date:

2020-03-02