Open AccessA putative new peptide synthase operon in Bacillus subtilis: partial characterization
Author(s) -
Angelo Togi,
Elisabetta Franchi,
Claudio Magistrelli,
Emanuela Colombo,
Paola Cosmina,
Guido Grandi
Publication year - 1995
Publication title -
microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.019
H-Index - 179
eISSN - 1465-2080
pISSN - 1350-0872
DOI - 10.1099/13500872-141-3-645
Subject(s) - bacillus subtilis , operon , bacillaceae , gal operon , microbiology and biotechnology , peptide , biology , atp synthase , biochemistry , chemistry , bacillales , bacteria , genetics , escherichia coli , enzyme , gene
A large operon-type structure has been located between the gltA and citB loci on the Bacillus subtilis chromosome. On the basis of the analysis of the 25 kb sequenced so far, it potentially encodes at least three large proteins which contain structural motifs associated with the subunits of all characterized peptide synthases. The amino acid recognition specificity of this new peptide synthase is discussed in the light of sequence homology with other synthases.