Identification of the L,D-transpeptidases responsible for attachment of the Braun lipoprotein to Escherichia coli peptidoglycan

J Bacteriol. 2007 May;189(10):3927-31. doi: 10.1128/JB.00084-07. Epub 2007 Mar 16.

Abstract

The L,D-transpeptidase Ldt(fm) catalyzes peptidoglycan cross-linking in beta-lactam-resistant mutant strains of Enterococcus faecium. Here, we show that in Escherichia coli Ldt(fm) homologues are responsible for the attachment of the Braun lipoprotein to murein, indicating that evolutionarily related domains have been tailored to use muropeptides or proteins as acyl acceptors in the L,D-transpeptidation reaction.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism
  • Lipoproteins / metabolism
  • Molecular Sequence Data
  • Peptides / chemistry
  • Peptides / metabolism
  • Peptidoglycan / metabolism
  • Peptidyl Transferases / genetics
  • Peptidyl Transferases / metabolism*

Substances

  • Escherichia coli Proteins
  • Lipoproteins
  • Peptides
  • Peptidoglycan
  • Peptidyl Transferases