Amino-acid racemase able to utilize a broad range of substrates. Reversibly racemizes ten of the 19 natural chiral amino acids known, including both non-beta-branched aliphatic amino acids (Ala, Leu, Met, Ser, Cys, Gln and Asn) and positively charged amino acids (His, Lys and Arg). Among these substrates, is the most efficient with lysine and arginine. Is also able to catalyze the racemization of several amino acids that are not typically incorporated into proteins such as ornithine and norleucine. Is not active on negatively charged (Glu and Asp) or aromatic (Tyr, Trp and Phe) amino acids and displays minimal activity towards beta-branched aliphatic (Ile, Val and Thr) substrates (PubMed:24419381). Enables bacteria to produce and release extracellular non-canonical D-amino acids (NCDAAs) that regulate diverse cellular processes which may function as part of a cooperative strategy in vibrio communities to protect non-producing members from competing bacteria (PubMed:29446806, PubMed:29028003). D-amino acid production by BsrV provides a cue for V.cholerae to decrease peptidoglycan synthesis and to alter its cell wall via incorporation of NCDAAs into the muropeptides, in adaption to stationary phase conditions (PubMed:19762646, PubMed:29028003). an L-alpha-amino acid = a D-alpha-amino acid L-lysine = D-lysine L-arginine = D-arginine L-alanine = D-alanine L-serine = D-serine L-methionine = D-methionine L-leucine = D-leucine L-cysteine = D-cysteine L-glutamine = D-glutamine L-asparagine = D-asparagine L-histidine = D-histidine L-ornithine = D-ornithine L-2-aminohexanoate = D-2-aminohexanoate L-homoserine = D-homoserine kcat is 1.68 sec(-1) with L-alanine as substrate. kcat is 4.68 sec(-1) with L-serine as substrate. kcat is 2.94 sec(-1) with L-methionine as substrate. kcat is 2.30 sec(-1) with L-leucine as substrate. kcat is 2.59 sec(-1) with L-glutamine as substrate. kcat is 0.05 sec(-1) with L-asparagine as substrate. kcat is 4.76 sec(-1) with L-lysine as substrate. kcat is 5.09 sec(-1) with L-arginine as substrate. Homodimer. Cells lacking this gene have normal growth and morphology but produce minimal D-Met, D-Leu, D-Val, and D-Ile. They contain twice the amount of peptidoglycan (PG) of wild-type cells in stationary phase, whereas PG levels do not differ in exponential phase. Addition of physiological amounts of D-Met and D-Leu to cultures with a deletion in bsrV reduce the amount of PG to wild-type levels, which confirms that the absence of D-amino acids accounts for the increased PG in the bsrV mutant. Moreover, the structure of wild-type and bsrV mutant PG isolated from stationary phase cells differed significantly. The glycan chains in stationary phase PG from the bsrV mutant are about 80% the length of the wild type, pentapeptides are reduced by about 50%, and there is an increase in trimer muropeptides. Despite being less abundant, the PG in wild-type cells appears to be stronger than in bsrV mutant cells. Wild-type cells survive 20 times more than bsrV mutant cells when subjected to an osmotic challenge (PubMed:19762646). D-Arg is not detected in the supernatant of cells lacking this gene. Production of other D-amino acids (for example, D-Leu) is also impaired in the deletion mutant (PubMed:29028003). The substrate range of BsrV, which includes activity towards non-natural substrates (e.g. ornithine, norleucine, homoserine, N-acetyl lysine methyl ester, diaminobutyrate and aminobutyrate), is broader than any other known amino-acid racemase and suggests that it has great potential for biotechnological and industrial applications. Currently, production of DAA is an expensive process that is typically reliant upon inefficient chemical catalysts. Belongs to the alanine racemase family. Bsr subfamily. Extended N-terminus.