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The first temperature-dependent proteins (expressed at 37°C, but not 26°C) to be identified inYersinia pestis were antigens 3 (fraction 1), 4 (pH 6 antigen), and 5 (hereafter termed KatY). Antigens 3 and 4 are now established virulence factors, whereas little is known about KatY, except that it is encoded chromosomally, produced in abundance, possesses modest catalase activity, and is shared byYersinia pseudotuberculosis , but notYersinia enterocolitica . We report here an improved chromatographic method (DEAE-cellulose, calcium hydroxylapatite, and Sephadex G-150) that yields enzymatically active KatY (2,423 U/mg of protein). Corresponding mouse monoclonal antibody 1B70.1 detected plasminogen activator-mediated hydrolysis of KatY, and a polyclonal rabbit antiserum raised against outer membranes ofY. pestis was enriched for anti-KatY. A sequenced ∼16-kbY. pestis DNA insert of a positive pLG338 clone indicated thatkatY encodes an 81.4-kDa protein (pI 6.98) containing a leader sequence of 2.6 kDa; the deduced molecular mass and pI of processed KatY were 78.8 kDa and 6.43, respectively. A minor truncated variant (predicted molecular mass of 53.6 kDa) was also expressed. KatY is similar (39 to 59% identity) to vegetative bacterial catalase-peroxidases (KatG inEscherichia coli ) and is closely related to plasmid-encoded KatP of enterohemorrhagicE. coli O157:H7 (75% identity).katY encoded a putative Ca2+ -binding site, and its promoter contained three homologues to the consensus recognition sequence of the pCD-encoded transcriptional activator LcrF.rbsA was located upstream ofkatY , andcybB ,cybC ,dmsABC , andaraD were mapped downstream. These genes are not linked tokatG orkatP inE. coli .

Molecular Characterization of KatY (Antigen 5), a Thermoregulated Chromosomally Encoded Catalase-Peroxidase ofYersinia pestis