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. 2008 Mar 27;8:51. doi: 10.1186/1471-2180-8-51

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Copyright © 2008 Casart et al; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Alignment of the ParA and ParB proteins. Comparison of the ParA (left) and ParB (right) aminoacid sequences of M. bovis BCG (MbBCG), M. smegmatis (Msm), M. tuberculosis (Mtb), M. leprae (Mlep) and S. coelicolor (Sc). The alignment was carried out using CLUSTAL W (1.83) http://www.ebi.ac.uk/clustalw/. Conserved amino acids are indicated with asterisk below the alignment; "-" represents gaps, ":" indicate conserved substitutions and "." semi-conserved substitutions. The A (VL/FTIANQKGGVGKT), A' (GLKTLVIDLDP) and B (FDYVFV/ID) boxes typical of the Walker-ATPases and the C motif (LGLLTINALVAAPEVM/L) of ParA proteins are highlighted on grey. The Helix-turn-Helix motif (HDELAARIGRSRPLITNMIR) involved in DNA-protein interactions of ParB is also highlighted on grey [3]. As noted, mycobacterial ParA have a longer N-terminal domain (between 67 to 91 aa) than other bacterial-ParA proteins.