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A chromosomally located beta-lactamase gene, cloned and expressed in Escherichia coli from a reference strain of the enterobacterial species Kluyvera cryocrescens, encoded a clavulanic acid-inhibited Ambler class A enzyme, KLUC-1, with a pI value of 7.4. KLUC-1 shared 86% amino acid identity with a subgroup of plasmid-mediated CTX-M-type extended-spectrum beta-lactamases (CTX-M-1, -3, -10, -11, and -12), the most closely related enzymes, and 77% amino acid identity with KLUA-1 from Kluyvera ascorbata. The substrate profile of KLUC-1 corresponded to that of CTX-M-type enzymes.
Decousser et al. (Sat,) studied this question.