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 .
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
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.
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This superfamily all contain a right handed beta helix similar to that first found in pectate lyase .
The clan 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-tail
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Curation and family details
|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 build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||5|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
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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 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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