Summary: Transglycosylase SLT domain
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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.
Transglycosylase SLT domain Provide feedback
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
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Koonin EV, Rudd KE; , Trends Biochem Sci 1994;19:106-107.: A conserved domain in putative bacterial and bacteriophage transglycosylases. PUBMED:8203016 EPMC:8203016
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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
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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
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Koraimann G; , Cell Mol Life Sci 2003;60:2371-2388.: Lytic transglycosylases in macromolecular transport systems of Gram-negative bacteria. PUBMED:14625683 EPMC:14625683
External database links
| HOMSTRAD: | SLT |
| PANDIT: | PF01464 |
| PROSITE: | PDOC00713 |
| Pseudofam: | PF01464 |
| SCOP: | 1sly |
| SYSTERS: | SLT |
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.
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan Lysozyme (CL0037), which 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 TransglycosylasAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
View options
We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (39) |
Full (14235) |
Representative proteomes | NCBI (11652) |
Meta (3304) |
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| RP15 (900) |
RP35 (1993) |
RP55 (2657) |
RP75 (3295) |
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| PP/heatmap | 1 | |||||||
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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not generated,
— not available.
Format an alignment
Download options
We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (39) |
Full (14235) |
Representative proteomes | NCBI (11652) |
Meta (3304) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (900) |
RP35 (1993) |
RP55 (2657) |
RP75 (3295) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
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 HMMER3.
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's seed alignment. 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 alignment.
Note: You can also download the data file for the tree.
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
| Seed source: | Prodom_3175 (release 99.1) |
| Previous IDs: | none |
| Type: | Family |
| Author: | Bateman A |
| 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 information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 121 | ||||||||||||
| Family (HMM) version: | 15 | ||||||||||||
| 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 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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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence