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Notice of Retraction
After careful and considered review of the content of this paper by a duly constituted expert committee, this paper has been found to be in violation of IEEE's Publication Principles.
We hereby retract the content of this paper. Reasonable effort should be made to remove all past references to this paper.
The presenting author of this paper has the option to appeal this decision by contacting TPII@ieee.org.
Lipase activity is popular in staphylococci. We described here that a 781-bp consensus lipase gene sequence of Staphylococcus caprae TCCC 11546, which encoded a deduced polypeptide of 260 amino acid residues, was cloned using the degenerate primers. The amino acid sequence alignment and the phylogenetic tree revealed that this 260-amino acid partial lipase of S. caprae was highly homologous from 55.0% to 98.8% among other 11 conserved lipase stretches from other 11 Staphylococcus species. Moreover, two amino acid residues, Ser39 and Asp230, were identified in the putative lipase catalytic triad, the consensus `P-loop' motif (-[AG]-x4-G-K-[ST]-) was also found in this partial lipase stretch.