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. 2006 Jan;188(2):487–498. doi: 10.1128/JB.188.2.487-498.2006

FIG.1.

FIG.1.

Amino acid sequence alignment of the Rap and Phr proteins of B. anthracis. (A) The Rap proteins of B. anthracis were aligned against the RapA protein of B. subtilis. The six TPR domains in RapA are underlined. The gray box in the BA3760 sequence indicates a duplication in the nucleotide sequence of the 34F2 strain used in this study that is not present in the database at accession number NC_003997. The dash replacing residue 226 in the sequence of BA4060 indicates the position of the frame shift that inactivates this gene product. The alignment was obtained by the ClustalW program. (B) Amino acid sequences of the Phr proteins of B. anthracis and the PhrA protein of B. subtilis. Gray boxes in the BsPhrA and BXA0205phr sequences indicate the sequence of the active pentapeptide inhibitor. The gray box in the BA3791 sequence indicates the region presumably containing the pentapeptide inhibitor. The amino-terminal positively charged domain (N), the hydrophobic domain (H), and the putative signal peptidase cleavage domain (C) of PhrA are indicated. The dashes indicate the putative signal peptidase cleavage site identified by the SignalP program (30). Inline graphic, identical residue; :, conserved residue.