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. 2007 May 4;73(13):4142–4151. doi: 10.1128/AEM.02729-06

FIG. 5.

FIG. 5.

(A) CLUSTAL X alignment of the deduced amino acid sequences for metalloproteases expressed by E. sakazakii strains 29544 and BAA 894 compared to that for S. proteamaculans. Numbers at the beginning and end of each line refer to the amino acid residue for each sequence. Arrowheads in bold font above the sequence for strain 29544 indicate the amino acid residues found by our analysis of the purified protease. (B) Comparison of the conservative motifs of E. sakazakii metalloprotease with other microbial metalloproteases. Numbers at the beginning and end of each sequence within each motif refer to the amino acid residue for each of the metalloprotease sequences. Amino acid residues common among the Zn-binding, catalytic, and Met turn motifs are indicated by shading. *, completely conserved residue; :, strongly conserved residue;., weakly conserved residue (as defined by Clustal X). Other microbial metalloprotease sequences came from the following GenBank references: S. proteamaculans, gi no. 118067788l; P. cartovorum, gi no. 1172650; P. atroseptica, gi no. 50122133; B. parapertussis 12822, gi no. 33597460; X. axonopodis pv. citri strain 306, gi no. 21240878; Anabaena sp. strain PCC 7120, gi no. 17228478; Anabaena variabilis ATCC 29413, gi no. 75909157; Arthrobacter sp. strain FB24, gi no. 116671175; S. coelicolor A3(2), gi no. 21220989; B. anthracis strain Ames, gi no. 30260755; S. aureus subsp. aureus MRSA252, gi no. 49242963.