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. 2014 Mar 12;4:283–289. doi: 10.1016/j.fob.2014.02.012

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© 2014 The Authors

This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/3.0/).

PMC Copyright notice

Fig. 1 — Domain organization of S. pyogenes AspA and sequence alignment of the C_2–3 domains of AspA, SpaP and SspB. (A) The primary sequence of AspA begins with a signal peptide (SP), followed in sequence by a small N-terminal domain (N), an alanine rich repeat region (A), a variable domain (V), a proline rich repeat region (P), a C-terminal region (C), and finally a cell wall anchor segment (CW) containing an LPxTG-motif for sortase mediated cell wall attachment. (B) Sequence alignment of the AspA (Uniprot id. Q48S75), SpaP (P23404) and SspB (P16952) C_2–3 domains. Secondary structure elements from the structure of AspA-C_2–3 are marked above the alignment.