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XB-ART-22957
Biochem J 1993 Jan 01;289 ( Pt 1):179-84.
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Hyaluronate synthase: cloning and sequencing of the gene from Streptococcus sp.

Lansing M , Lellig S , Mausolf A , Martini I , Crescenzi F , O'Regan M , Prehm P .


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The complete nucleotide sequence of hyaluronate synthase from Streptococcus sp. and its flanking regions is presented. The gene locus was designated has. Southern-blotting results suggested that the gene was conserved in hyaluronate-producing streptococci. A putative translation-initiation codon was identified and the open reading frame consists of 1566 bp, specifying a protein of 56 kDa. Sequences resembling the promoter and ribosome-binding site of Gram-positive organisms are found upstream of the synthase. The predicted amino-acid sequence reveals the presence of a 35-residue signal peptide. The sequence has some similarity to bacterial peptide-binding proteins.

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References [+] :
Abouhamad, Peptide transport and chemotaxis in Escherichia coli and Salmonella typhimurium: characterization of the dipeptide permease (Dpp) and the dipeptide-binding protein. 1991, Pubmed