Summary: Transglycosylase SLT domain
Transglycosylase SLT domain Provide feedback
Mushegian AR, Fullner KJ, Koonin EV, Nester EW; , Proc Natl Acad Sci U S A 1996;93:7321-7326.: A family of lysozyme-like virulence factors in bacterial pathogens of plants and animals. PUBMED:8692991 EPMC:8692991
Thunnissen AM, Rozeboom HJ, Kalk KH, Dijkstra BW; , Biochemistry 1995;34:12729-12737.: Structure of the 70-kDa soluble lytic transglycosylase complexed with bulgecin A. Implications for the enzymatic mechanism. PUBMED:7548026 EPMC:7548026
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR008258
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 [PUBMED:10452894]. Slt70 has 3 distinct domains, each rich in alpha helices: an N-terminal superhelical U-shaped domain (U-domain; INTERPRO), a superhelical linker domain (L-domain, INTERPRO), and a C-terminal catalytic domain (INTERPRO). 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 catalytic domain, which is structurally conserved in some membrane-bound lytic glycosylases and in bacteriophage transglycosylases, even though their sequences can differ considerably proteins [PUBMED:8203016]. The most conserved part of this domain is its N-terminal extremity that contains two conserved serines and a glutamate, which have been shown [PUBMED:8107871] to be involved in the catalytic mechanism. This family is distantly related to INTERPRO.
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Barley chitinase, bacterial chitosanase, and lysozymes from phage and animals all hydrolyse related polysaccharides. The proteins little amino-acid similarity, but have a structurally invariant core consisting of two helices and a three-stranded beta-sheet which form the substrate-binding and catalytic cleft .
The clan contains the following 12 members:Glucosaminidase Glyco_hydro_108 Glyco_hydro_19 Glyco_hydro_46 Lys Lysozyme_like Phage_lysozyme REGB_T4 SLT SLT_2 TraH_2 Transglycosylas
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Prodom_3175 (release 99.1)|
|Number in seed:||39|
|Number in full:||14235|
|Average length of the domain:||115.80 aa|
|Average identity of full alignment:||22 %|
|Average coverage of the sequence by the domain:||28.70 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||15|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the SLT domain has been found. There are 20 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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