9  structures 874  species 0  interactions 5250  sequences 83  architectures

Family: SLT (PF01464)

Summary

Transglycosylase SLT domain Add an annotation

This family is distantly related to PF00062. Members are found in phages, type II, type III and type IV secretion systems (reviewed in [4]).


Literature references

  1. Koonin EV, Rudd KE; , Trends Biochem Sci 1994;19:106-107.: A conserved domain in putative bacterial and bacteriophage transglycosylases. PUBMED:8203016

  2. 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

  3. 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

  4. Koraimann G; , Cell Mol Life Sci 2003;60:2371-2388.: Lytic transglycosylases in macromolecular transport systems of Gram-negative bacteria. PUBMED:14625683


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; ), 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.

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 .

Clan

This family is a member of clan Lysozyme (CL0037), which contains the following 10 members:

DUF847 Glucosaminidase Glyco_hydro_19 Glyco_hydro_46 Lys Phage_lysozyme REGB_T4 SLT TraH_2 Transglycosylas

External database links

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Alignments

There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...

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Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.

You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.

Pfam alignments:
Full length sequences

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.

Pfam alignments:

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed or full alignments.

Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Prodom_3175 (release 99.1)
Previous IDs: none
Type: Family
Author: Bateman A
Number in seed: 39
Number in full: 5250
Average length of the domain: 116.70 aa
Average identity of full alignment: 22 %
Average coverage of the sequence by the domain: 29.32 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.3 21.3
Trusted cut-off 21.3 21.3
Noise cut-off 21.2 21.2
Model length: 121
Family (HMM) version: 13
Download: download the raw HMM for this family

Species distribution

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Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the MSD 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.

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