Summary: Catalytic domain of bacteriophage endosialidase
Catalytic domain of bacteriophage endosialidase Provide feedback
This domain family is found in bacteria and viruses, and is approximately 160 amino acids in length. There are two conserved sequence motifs: VSR and YGA. This domain is the C terminal domain of the bacteriophage protein endosialidase. The endosialidase protein forms homotrimeric molecules and this domain complexes into a tail-spike stalk. The stalk region folds in a triple beta-helix that is interrupted by a small triple beta-prism domain. The tail-spike is a multifunctional protein device used by the phage to fulfill the following functions: (i) to adsorb to the bacterial polySia capsule (ii) to de-polymerise the capsule to gain access to the outer bacterial membrane, and finally (iii) to mediate tight adhesion to the membrane, a prerequisite for the initiation of the infection cycle.
Stummeyer K, Dickmanns A, Muhlenhoff M, Gerardy-Schahn R, Ficner R;, Nat Struct Mol Biol. 2005;12:90-96.: Crystal structure of the polysialic acid-degrading endosialidase of bacteriophage K1F. PUBMED:15608653 EPMC:15608653
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This tab holds annotation information from the InterPro database.
InterPro entry IPR024430This entry represents the C-terminal domain of endosialidases which is approximately 160 amino acids in length. There are two conserved sequence motifs: VSR and YGA. The endosialidase protein forms homotrimeric molecules and this domain complexes into a tail-spike stalk. The stalk region folds in a triple beta-helix that is interrupted by a small triple beta-prism domain. The tail-spike is a multifunctional protein device used by the phage to fulfil the following functions: (i) to adsorb to the bacterial polySia capsule (ii) to de-polymerise the capsule to gain access to the outer bacterial membrane, and finally (iii) to mediate tight adhesion to the membrane, a prerequisite for the initiation of the infection cycle [PUBMED:15608653].
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Curation and family details
|Author:||Mistry J, Gavin OL|
|Number in seed:||5|
|Number in full:||36|
|Average length of the domain:||136.90 aa|
|Average identity of full alignment:||78 %|
|Average coverage of the sequence by the domain:||17.33 %|
|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:||3|
|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 End_tail_spike domain has been found. There are 24 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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