PROSITE documentation PDOC00713
Prokaryotic transglycosylases signature


Bacterial lytic transglycosylases degrade murein via cleavage of the β-1,4-glycosidic bond between N-acetylmuramic acid and N-acetylglucosamine, with the concomitant formation of a 1,6-anhydrobond in the muramic acid residue. Escherichia coli has at least three different lytic transglycosylases: two soluble isozymes of 65 Kd and 35 Kd and a membrane-bound enzyme of 38 Kd. The sequence of the 65 Kd enzyme (gene slt) has been determined [1]. A domain of about 90 residues located near the C-terminal section of slt was recently shown [2] to be present in a number of other prokaryotic and phage proteins:

  • Membrane-bound lytic murein transglycosylase C (gene mltC).
  • Membrane-bound lytic murein transglycosylase D (gene mltD).
  • Membrane-bound lytic murein transglycosylase E (gene mltE).
  • Phage T7 internal protein D which may be involved in the lysis of the bacterial cell wall during the release of phage progeny.
  • Phage PRD1 gene 7 protein.
  • Alteromonas strain M-1 possible tributyltin chloride resistance protein.
  • Escherichia coli hypothetical protein yfhD.

The domain shared by these proteins could be involved in catalytic activity. The most conserved part of this domain is its N-terminal extremity which we used as a signature pattern. It contains two conserved serines and a glutamate which has been shown [3] to be involved in the catalytic mechanism.

Expert(s) to contact by email:

Dijkstra A.J.

Last update:

November 1997 / Pattern and text revised.


Technical section

PROSITE method (with tools and information) covered by this documentation:

TRANSGLYCOSYLASE, PS00922; Prokaryotic transglycosylases signature  (PATTERN)


1AuthorsEngel H. Kazemier B. Keck W.
TitleMurein-metabolizing enzymes from Escherichia coli: sequence analysis and controlled overexpression of the slt gene, which encodes the soluble lytic transglycosylase.
SourceJ. Bacteriol. 173:6773-6782(1991).
PubMed ID1938883

2AuthorsKoonin E.V. Rudd K.E.
TitleA conserved domain in putative bacterial and bacteriophage transglycosylases.
SourceTrends Biochem. Sci. 19:106-107(1994).
PubMed ID8203016

3AuthorsThunnissen A.-M.W. Dijkstra A.J. Kalk K.H. Rozeboom H.J. Engel H. Keck W. Dijkstra B.W.
TitleDoughnut-shaped structure of a bacterial muramidase revealed by X-ray crystallography.
SourceNature 367:750-753(1994).
PubMed ID8107871

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