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Figure 3 | BMC Microbiology

Figure 3

From: EndoS from Streptococcus pyogenes is hydrolyzed by the cysteine proteinase SpeB and requires glutamic acid 235 and tryptophans for IgG glycan-hydrolyzing activity

Figure 3

Possible domain organization and sequence alignments of EndoS. Panel A, schematic representation of the 995 amino acids EndoS. Ss indicates signal peptide, the chitinase family 18 active site motif in the amino-terminal domain is indicated, the SpeB cleavage site is indicated with an arrow, and the putative leucine-rich repeat region (LRR) is shown. Panel B, ClustalW alignment of EndoS and leucine-rich proteins from P. gingivalis (NP_905954), C. tetani (NP_781184), and L. monocytogenes (NP_463795). Amino acid number one corresponds to amino acid 446 in the whole protein. Panel C, RADAR repeat analysis showing three 37 amino acids leucine rich repeats and two additional repeats. Numbering is based on the 995 amino acids sequence of full-length EndoS.

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BMC Microbiology

ISSN: 1471-2180

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