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Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate‐forming enzymes
Author(s) -
Turgay K.,
Krause M.,
Marahiel M. A.
Publication year - 1992
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1992.tb01498.x
Subject(s) - biology , amino acid , homology (biology) , gene , genetics , nucleic acid sequence , protein primary structure , peptide sequence , biochemistry , open reading frame , sequence alignment , conserved sequence , operon , escherichia coli
Summary The entire nucleotide sequence of the Bacillus brevis grsB gene encoding the gramicidin S synthetase 2, which activates and condenses the four amino acids proline, valine, ornithine and leucine has been determined. The gene contains an open reading frame of 13359bp which encodes a protein of 4453 amino acids with a predicted M r of 510287. The gene is located within the gramicidin S biosynthetic operon, also containing the genes grsT and grsA , whose nucleotide sequences have been determined previously. Within the GrsB amino acid sequence four conserved and repeated domains of about 600 amino acids (45–50% identity) have been identified. The four domains are separated by non‐homologous sequences of about 500 amino acids. The domains also share a high degree of similarity (20–70%) with eight peptide synthetases of bacterial and fungal origin as well as with conserved sequences of nine other adenylate‐forming enzymes of diverse origin. On the basis of sequence homology and functional similarities, we infer that those enzymes share a common evolutionary origin and present a phylogenetic tree for this superfamily of domain‐bearing enzymes.