Fig. 1From: Immunoreactivity of the AAA+ chaperone ClpB from Leptospira interrogans with sera from Leptospira-infected animalsProposed domain organization of ClpB from L. interrogans. a The diagram shows structural domains of the protein: N-terminal domain (ND) with the double Clp_N motif, nucleotide binding domain 1 (NBD1), middle coiled-coil domain (MD) and nucleotide binding domain 2 (NBD2). Conserved ATPase motifs such as the Walker A (A), Walker B (B), sensor 1, sensor 2 (GAR) and the Arg fingers (R), coordinating ATP binding and hydrolysis are also indicated. Conserved residues of these motifs are marked in bold. b Sequence alignment of ClpB from E. coli (BEc) and L. interrogans (BLi). Domain boundaries are indicated below the amino acid sequence. The conserved motifs are shown in red. Identical and similar amino acid resides are shaded in black and gray, ... respectivelyBack to article page