Summary: Salmonella phage P22 tail-spike
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Salmonella phage P22 tail-spike Provide feedback
Members of this family of viral domains adopt a structure consisting of a single-stranded right-handed beta-helix, which in turn is made of parallel beta-strands and short turns. They are required for recognition of the 0-antigenic repeating units of the cell surface, and for subsequent infection of the bacterial cell [1].
Literature references
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Steinbacher S, Baxa U, Miller S, Weintraub A, Seckler R, Huber R; , Proc Natl Acad Sci U S A. 1996;93:10584-10588.: Crystal structure of phage P22 tailspike protein complexed with Salmonella sp. O-antigen receptors. PUBMED:8855221 EPMC:8855221
External database links
| PANDIT: | PF09251 |
| Pseudofam: | PF09251 |
| SCOP: | 1tyv |
| SYSTERS: | PhageP22-tail |
This tab holds annotation information from the InterPro database.
InterPro entry IPR015331
The tailspike protein of Salmonella bacteriophage P22 is a viral adhesion protein that mediates attachment of the viral protein to host cell-surface lipopolysaccharide. The tailspike protein displays both receptor binding and destroying properties, inactivating the receptor by endoglycosidase activity. P22 tailspike is a homotrimer composed of 666 amino acid polypeptide chains. P22 tailspike consists of three main structural elements: the head-binding domain at the N terminus (INTERPRO), the beta-helix in the centre of the protein, and the beta-prism and caudal fin at the C terminus [PUBMED:14627734]. The P22 tailspike protein contains similar structural elements to pectin lyase [PUBMED:10600383]. The binding of the disaccharide product occurs within a positively charged cleft formed by loops extending from the surface of the beta-helix structure. Amino acid residues responsible for recognition of the disaccharide, as well as potential catalytic residues, have been identified [PUBMED:12063249].
This entry represents the C-terminal domain of the tailspike protein.
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 Pec_lyase-like (CL0268), which contains the following 22 members:
Adeno_E1B_55K Autotrns_rpt Beta_helix Chlam_PMP Chondroitinas_B Disaggr_assoc DUF1565 DUF3737 Fil_haemagg Fil_haemagg_2 Glyco_hydro_28 Glyco_hydro_49 Glyco_hydro_80 Glyco_hydro_92 Haemagg_act NosD Pec_lyase_C Pectate_lyase Pectate_lyase_3 Pectinesterase Pertactin PhageP22-tailAlignments
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 (6) |
Full (48) |
Representative proteomes | NCBI (51) |
Meta (0) |
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| RP15 (0) |
RP35 (0) |
RP55 (0) |
RP75 (0) |
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| PP/heatmap | 1 | |||||||
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
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 (6) |
Full (48) |
Representative proteomes | NCBI (51) |
Meta (0) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (0) |
RP35 (0) |
RP55 (0) |
RP75 (0) |
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| Raw Stockholm | ||||||||
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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: | pdb_1tyv |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Sammut SJ |
| Number in seed: | 6 |
| Number in full: | 48 |
| Average length of the domain: | 509.60 aa |
| Average identity of full alignment: | 79 % |
| Average coverage of the sequence by the domain: | 82.26 % |
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: | 549 | ||||||||||||
| Family (HMM) version: | 5 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Sunburst controls
ShowThis visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...
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Interactions
There is 1 interaction for this family. More...
PhageP22-tailStructures
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 PhageP22-tail domain has been found. There are 23 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