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- *******************************************
- * Prokaryotic transglycosylases signature *
- *******************************************
-
- Bacterial lytic transglycosylases degrade murein via cleavage of the beta-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:
-
- - 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 yafG.
- - 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.
-
- -Consensus pattern: [LIVM]-x(3)-E-S-x(3)-[AP]-x(3)-S-x(5)-G-[LIVM]-[LIVMFYW]-
- x-[LIVMFYW]-x(4)-[AG]
- [E is the active site residue]
- -Sequences known to belong to this class detected by the pattern: ALL.
- -Other sequence(s) detected in SWISS-PROT: NONE.
-
- -Expert(s) to contact by email: Koonin E.V.
- koonin@ncbi.nlm.nih.gov
-
- -Last update: June 1994 / Text revised.
-
- [ 1] Engel H., Kazemier B., Keck W.
- J. Bacteriol. 173:6773-6782(1991).
- [ 2] Koonin E.V., Rudd K.E.
- Trends Biochem. Sci. 19:106-107(1994).
- [ 3] Thunnissen A.-M.W., Dijkstra A.J., Kalk K.H., Rozeboom H.J., Engel H.,
- Keck W., Dijkstra B.W.
- Nature 367:750-753(1994).
-