Protein Family Models

Soluble lytic murein transglycosylase (SLT) consists of three domains, an N-terminal U domain, an L domain (linker domain) and a C-terminal domain (C). The L domain may be involved in the interaction of the enzyme with peptidoglycan [1]. [1]. 10452894. High resolution crystal structures of the Escherichia coli lytic transglycosylase Slt70 and its complex with a peptidoglycan fragment. van Asselt EJ, Thunnissen AM, Dijkstra BW;. J Mol Biol. 1999;291:877-898. (from Pfam)

Date:

2024-10-16

This family is distantly related to Pfam:PF00062. Members are found in phages, type II, type III and type IV secretion systems (reviewed in [4]). [1]. 8203016. A conserved domain in putative bacterial and bacteriophage transglycosylases. Koonin EV, Rudd KE;. Trends Biochem Sci 1994;19:106-107. [2]. 8692991. A family of lysozyme-like virulence factors in bacterial pathogens of plants and animals. Mushegian AR, Fullner KJ, Koonin EV, Nester EW;. Proc Natl Acad Sci U S A 1996;93:7321-7326. [3]. 7548026. Structure of the 70-kDa soluble lytic transglycosylase complexed with bulgecin A. Implications for the enzymatic mechanism. Thunnissen AM, Rozeboom HJ, Kalk KH, Dijkstra BW;. Biochemistry 1995;34:12729-12737. [4]. 14625683. Lytic transglycosylases in macromolecular transport systems of Gram-negative bacteria. Koraimann G;. Cell Mol Life Sci 2003;60:2371-2388. (from Pfam)

Date:

2024-10-16

Catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan

Gene:

sltY

Date:

2021-08-25

soluble lytic murein transglycosylase is a murein-degrading enzyme that catalyzes cleavage of glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan

Date:

2018-07-12