Abstract:
:The primary structure of a bacteriocin produced by Enterococcus hirae DCH5 was determined by combined amino acid and DNA sequencing. Nucleotide analysis of a 2838-bp DNA fragment of E. hirae DCH5 revealed five putative ORFs. The first orf (hirJM79) encodes a 74-amino-acid peptide containing an N-terminal signal peptide of 30 amino acids, followed by the amino acid sequence of the mature bacteriocin, hiracin JM79 (HirJM79), of 44 amino acids. The second orf (hiriJM79) encodes the putative immunity protein of HirJM79. Contiguous ORFs encode a putative mobilization protein (orfC), a relaxase/mobilization nuclease domain (orfD), and a hypothetical protein (orfE). The production and functional expression of HirJM79 by heterologous hosts suggest that hirJM79 is the minimum requirement for production of biologically active HirJM79, that HirJM79 is most likely externalized by the general secretory pathway or sec-dependent pathway, and that HiriJM79 is the immunity protein for HirJM79.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Sánchez J,Diep DB,Herranz C,Nes IF,Cintas LM,Hernández PEdoi
10.1111/j.1574-6968.2007.00673.xsubject
Has Abstractpub_date
2007-05-01 00:00:00pages
227-36issue
2eissn
0378-1097issn
1574-6968pii
FML673journal_volume
270pub_type
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journal_title:FEMS microbiology letters
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journal_title:FEMS microbiology letters
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