Recombinant Campylobacter jejuni subsp. doylei Undecaprenyl-diphosphatase (uppP) is a bacterially derived enzyme produced through recombinant DNA technology. This protein, encoded by the uppP gene (locus JJD26997_0215 in strain ATCC BAA-1458/RM4099/269.97), catalyzes the hydrolysis of undecaprenyl diphosphate (UPP) to undecaprenyl phosphate (UP), a critical step in bacterial cell wall biosynthesis . Its role in lipid carrier regeneration makes it a target for studying antibiotic resistance mechanisms, particularly bacitracin resistance .
Amino Acid Sequence: Partial sequence (residues 1–267) with predicted domains for phosphatase activity .
Expression Systems: Produced in E. coli, baculovirus, or mammalian cells .
uppP confers bacitracin resistance by recycling UP, a lipid carrier essential for peptidoglycan synthesis. Disruption of uppP activity sensitizes bacteria to bacitracin, highlighting its role as a drug target .
Host Interaction: uppP contributes to C. jejuni survival in host environments, including poultry reservoirs .
Recombinant Use: The protein is utilized in ELISA and immunoblot assays to study immune responses during Campylobacter infections .
Genetic Diversity: The uppP gene is conserved across C. jejuni strains but undergoes rapid evolution via recombination, as observed in C. jejuni subsp. doylei .
Horizontal Gene Transfer: Recombination rates in Campylobacter spp. are twice the mutation rate, facilitating interspecies gene flow (e.g., with C. coli) .
Reconstitution: Lyophilized protein should be dissolved in sterile water to 0.1–1.0 mg/mL, with glycerol (5–50%) added for long-term stability .
Limitations: Avoid repeated freeze-thaw cycles; working aliquots stored at 4°C retain activity for ≤1 week .
Current research gaps include direct functional assays for uppP in C. jejuni subsp. doylei and structural studies to guide inhibitor design. The protein’s role in zoonotic transmission and antibiotic resistance warrants further exploration .
KEGG: cjd:JJD26997_0215