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UniProt functional annotation for P12528 | ||
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| UniProt code: P12528. |
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| Organism: | |
Salmonella phage P22 (Bacteriophage P22). |
| Taxonomy: | |
Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; Caudovirales; Podoviridae; Lederbergvirus. |
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| Function: | |
Structural component of the short non-contractile tail. The tail comprises six spikes that mediate primary attachment to the host cell lipopolysaccharides (LPS) and display endorhamnosidase enzymatic activity, hydrolyzing the alpha-1,3-O-glycosidic linkage between rhamnose and galactose of the O-antigen polysaccharide. Digestion of the LPS brings the capsid near the cell outer membrane. {ECO:0000269|PubMed:12837775, ECO:0000269|PubMed:20817910}. |
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| Subunit: | |
Homotrimer. Interacts with the host O-antigen lipopolysaccharides; this interaction induces cleavage of host O- antigen. {ECO:0000269|PubMed:20817910, ECO:0000269|PubMed:8855221}. |
| Subcellular location: | |
Virion {ECO:0000305}. |
| Domain: | |
The interdigitation of the polypeptide chains at the C-termini is important to protrimer formation in the folding pathway and to thermostability of the mature protein. |
| Similarity: | |
Belongs to the P22likevirus tail fiber protein family. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.