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. 2009 May 5;1:45–55. doi: 10.1093/gbe/evp005

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© The Author(s) 2009. Published by Oxford University Press on behalf of the Society for Molecular Biology and Evolution.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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FIG. 1.— — Frequencies of uptake sequence-encodable tripeptides in bacterial proteomes. H. influenzae proteome, blue; A. pleuropneumoniae proteome, red; N. meningitidis proteome, orange; Escherichia coli proteome, green. (A) Tripeptides that can be specified by each of the three uptake sequences: left group by H. influenzae USS; center group by A. pleuropneumoniae USS; and right group by N. meningitidis DUS. The enrichment in the H. influenzae proteome of peptides encodable by the H. influenzae USS was significant (P = 0.010), the enrichment in the A. pleuropneumoniae proteome of peptides encodable by the A. pleuropneumoniae USS was just above the significance threshold (P = 0.058), and the enrichment in the N. meningitidis proteome of peptides encodable by the N. meningitidis DUS was highly significant (P < 0.0001). Boxed areas of bars indicate the fraction of peptides specified by perfect-core uptake sequences. (B) Reversed-sequence tripeptide controls. None of the controls showed significant enrichment.