Homologous Superfamily

Lytic transglycosylase, superhelical linker domain superfamily (IPR037061)

Short name: Lytic_TGlycoase_superhlx_L_sf


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. There are both soluble (Slt enzymes) and membrane-bound (Mlt enzymes) lytic transglycosylases that differ in size, sequence, activity, specificity and location. The multi-domain structure of the 70 Kd soluble lytic transglycosylase Slt70 is known [PMID: 10452894]. Slt70 has 3 distinct domains, each rich in alpha helices: an N-terminal superhelical U-shaped domain, a superhelical linker domain (L-domain, IPR012289), and a C-terminal catalytic domain (IPR023346). Both the U- and L-domain share a similar superhelical structure. These two domains are connected, and together form a closed ring with a large central hole; the catalytic domain is packed on top of, and interacts with, this ring. The catalytic domain has a lysosome-like fold.

This entry represents the superhelical linker domain (also called the L domain) superfamily, which contains two small and four large alpha helices, the latter forming a four-alpha-helical bundle with a double-layer, superhelical topology that is similar to that found in the U-shaped domain.

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds

Cellular Component

GO:0042597 periplasmic space

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.