UniProt functional annotation for P26746



	UniProt functional annotation for P26746

UniProt code: P26746.

Organism: Salmonella phage P22 (Bacteriophage P22).

Taxonomy: Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; Caudovirales; Podoviridae; Lederbergvirus.

Function: Tail protein located at the vertex occupied by the portal ring. 12 copies of gp4 form a structural ring at the bottom of the portal ring. Together with gp10 and gp26, gp4 is required for stabilization of the condensed DNA within the capsid; perhaps by plugging the hole through which the DNA enters. Probably functions as a head completion protein. Plays a role in ejection of the bacteriophage DNA into the host cell at the initiation of infection. Functions as an exolysin that catalyzes the cleavage of the glycosidic bonds between N- acetylmuramic acid and N-acetylglucosamine residues in peptidoglycans. {ECO:0000269|PubMed:14763988, ECO:0000269|PubMed:16970964, ECO:0000269|PubMed:21499245}.

Subunit: Monomer; homododecamer upon binding to the portal ring (PubMed:16970964). Interacts (via C-terminus) with the portal protein; this interaction participates in the head completion (PubMed:28134243, PubMed:16970964). {ECO:0000269|PubMed:28134243}.

Subcellular location: Virion {ECO:0000305}.

Domain: The N-terminus changes its conformation when transitioning from the preassembly state to the postassembly state. {ECO:0000250|UniProtKB:Q716G8}.

Annotations taken from UniProtKB at the EBI.


Organism:		Salmonella phage P22 (Bacteriophage P22).
Taxonomy:		Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; Caudovirales; Podoviridae; Lederbergvirus.



Function:		Tail protein located at the vertex occupied by the portal ring. 12 copies of gp4 form a structural ring at the bottom of the portal ring. Together with gp10 and gp26, gp4 is required for stabilization of the condensed DNA within the capsid; perhaps by plugging the hole through which the DNA enters. Probably functions as a head completion protein. Plays a role in ejection of the bacteriophage DNA into the host cell at the initiation of infection. Functions as an exolysin that catalyzes the cleavage of the glycosidic bonds between N- acetylmuramic acid and N-acetylglucosamine residues in peptidoglycans. {ECO:0000269\|PubMed:14763988, ECO:0000269\|PubMed:16970964, ECO:0000269\|PubMed:21499245}.


Subunit:		Monomer; homododecamer upon binding to the portal ring (PubMed:16970964). Interacts (via C-terminus) with the portal protein; this interaction participates in the head completion (PubMed:28134243, PubMed:16970964). {ECO:0000269\|PubMed:28134243}.
Subcellular location:		Virion {ECO:0000305}.
Domain:		The N-terminus changes its conformation when transitioning from the preassembly state to the postassembly state. {ECO:0000250\|UniProtKB:Q716G8}.