Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate‐forming enzymes

verfasst von

K. Turgay, Michael Krause, M. A. Marahiel

Abstract

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.

Externe Organisation(en)

Philipps-Universität Marburg

Typ

Artikel

Journal

Molecular microbiology

Band

6

Seiten

529-546

Anzahl der Seiten

18

ISSN

0950-382X

Publikationsdatum

02.1992

Publikationsstatus

Veröffentlicht

Peer-reviewed

Ja

ASJC Scopus Sachgebiete

Mikrobiologie, Molekularbiologie

Elektronische Version(en)

https://doi.org/10.1111/j.1365-2958.1992.tb01498.x (Zugang: Unbekannt)