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Biotin protein ligase (BPL) is widespread in the three domains of the life. The paradigm BPL is the  Escherichia coli  BirA protein, which also functions as a repressor for the biotin biosynthesis pathway. Here we report that  Lactococcus lactis  possesses two different orthologues of  birA  ( birA 1 _LL  and  birA 2 _LL ). Unlike the scenario in  E. coli, L. lactis  appears to be auxotrophic for biotin in that it lacks a full biotin biosynthesis pathway. In contrast, it retains two biotin transporter-encoding genes ( bioY 1 _LL  and  bioY 2 _LL ), suggesting the use of a scavenging strategy to obtain biotin from the environment. The  in vivo  function of the two  L. lactis birA  genes was judged by their abilities to complement the conditional lethal  E. coli birA  mutant. Thin-layer chromatography and mass spectroscopy assays demonstrated that these two recombinant BirA proteins catalyze the biotinylation reaction of the acceptor biotin carboxyl carrier protein (BCCP), through the expected biotinoyl-AMP intermediate. Gel shift assays were used to characterize  bioY 1 _LL  and BirA1 _LL . We also determined the ability to uptake  3 H-biotin by  L. lactis.  Taken together, our results deciphered a unique biotin scavenging pathway with redundant genes present in the probiotic bacterium  L. lactis .

Deciphering a unique biotin scavenging pathway with redundant genes in the probiotic bacterium Lactococcus lactis