| Type: | Domain | Name: | Transglycosylase SLT domain 2 |
| Description: | This domain is found mainly in proteins from bacteria, such as membrane-bound lytic murein transglycosylase B (mltB, also known as Slt35) from E. coli. MltB is a murein-degrading enzyme that catalyses the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan []. This domain is related to the SLT domain 1 ().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 []. Slt70 has 3 distinct domains, each rich in alpha helices: an N-terminal superhelical U-shaped domain (U-domain; ), a superhelical linker domain (L-domain, ), and a C-terminal catalytic domain (). 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. | Short Name: | SLT_2 |
