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UniProt functional annotation for P20345 | ||
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| UniProt codes: P20345, B3VMP8. |
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| Organism: | |
Bacillus phage phi29 (Bacteriophage phi-29). |
| Taxonomy: | |
Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; Caudovirales; Podoviridae; Picovirinae; Salasvirus. |
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| Function: | |
Structural component of the 12 appendages that hang from the lower collar. Adhesion protein that binds to the host cell surface during virus attachment and mediates teichoic acids degradation. {ECO:0000269|PubMed:7241648}. |
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| Cofactor: | |
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19450535}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:19450535}; |
| Subunit: | |
Homotrimer. Each appendage is a homotrimer of gp12*. {ECO:0000269|PubMed:19450535}. |
| Subcellular location: | |
Virion {ECO:0000269|PubMed:11562162, ECO:0000269|PubMed:19450535}. Note=Present in 36 copies in the virion. {ECO:0000305|PubMed:19450535}. |
| Domain: | |
The N-terminus has three domains that function to attach the appendages to the phage, digest the cell wall teichoic acids, and bind irreversibly to the host. The C-terminus is an autochaperone that aids trimerization. {ECO:0000269|PubMed:19450535}. |
| Ptm: | |
Autocleaved to produce the 74 kDa gp12* assembly attached to the phage particles. Autocleavage of the C-terminus is a posttrimerization event that is followed by an ATP-dependent release. {ECO:0000269|PubMed:19450535}. |
Annotations taken from UniProtKB at the EBI.