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. 2009 Jul 10;191(18):5603–5612. doi: 10.1128/JB.00627-09

FIG. 2.

FIG. 2.

The TM domain of SrtA is required for the assembly of SpaA pili and the formation of high-molecular-weight pilin-sortase complexes. (A) Presentation of wild-type SrtA predicted to have the N-terminal signal peptide sequence (hatched) and the C-terminal TM domain (black), followed by a positively charged tail. A putative catalytic pocket is composed of His160 and Cys222. The positions where truncations were made are underlined. (B and C) Cells of the wild-type (WT) strain and its isogenic derivative carrying deletions of srtA or the derivative expressing SrtA mutants grown in HIB were fractionated into culture medium (M), cell wall (W), and protoplast (P) fractions. Protein samples were separated on 4 to 12% Tris-glycine gradient gels and detected by immunoblotting them with the specific antisera α-SpaA (B) and α-SrtA (C). The positions of molecular mass markers (kDa), high-molecular-weight polymers (HMW), and sortase monomers (P) are indicated.