Transglycosylase SLT domain 1 (IPR008258)

Short name: Transglycosylase_SLT_dom_1

Overlapping homologous superfamilies

Domain relationships



This domain is found mainly in proteins from phages and type II, type III and type IV secretion systems [PMID: 8203016, PMID: 8692991, PMID: 14625683, PMID: 14625683].

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.

Contributing signatures

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