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. 2014 Aug 31;14:219. doi: 10.1186/s12866-014-0219-1

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© Donahue et al.; licensee BioMed Central Ltd. 2014

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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SrtB _ΔN26 substrate specificity. Purified recombinant SrtB_ΔN26 protein was incubated with a range of peptide sequences to investigate its substrate specificity. The motifs SPKTG, PPKTG, SPSTG and SPQTG were all recognized and cleaved following incubation with SrtB_ΔN26. The scrambled peptide sequences GSKTP, GPKTG, GSSTP, and GSQTP serve as controls for the cleavage specificity of SrtB_ΔN26. The sequences LPETG and NPQTN, corresponding to the motifs recognized by S. aureus sortase A and B, respectively, do not appear to be substrates for SrtB_ΔN26. SrtB_ΔN26 also failed to cleave the proposed sorting signal NVQTG from recently characterized collagen binding protein, CbpA. Bars indicate the mean, and error bars represent the standard error (**corresponds to p < 0.01).