TY - JOUR

T1 - Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate‐forming enzymes

AU - Turgay, K.

AU - Krause, Michael

AU - Marahiel, M. A.

N1 - Copyright: Copyright 2016 Elsevier B.V., All rights reserved.

PY - 1992/2

Y1 - 1992/2

N2 - 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 Mr 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.

AB - 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 Mr 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.

UR - http://www.scopus.com/inward/record.url?scp=0026588298&partnerID=8YFLogxK

U2 - 10.1111/j.1365-2958.1992.tb01498.x

DO - 10.1111/j.1365-2958.1992.tb01498.x

M3 - Article

C2 - 1560782

AN - SCOPUS:0026588298

VL - 6

SP - 529

EP - 546

JO - Molecular microbiology

JF - Molecular microbiology

SN - 0950-382X

IS - 4

ER -