Summary: Phage capsid scaffolding protein (GPO) serine peptidase
Phage capsid scaffolding protein (GPO) serine peptidase Provide feedback
This family consists of several bacteriophage capsid scaffolding proteins (GPO) and some related bacterial sequences. GPO is thought to function in both the assembly of proheads and the cleavage of GPN . The family is found to function as a serine peptidase, with a conserved Asp, His and Ser catalytic triad, as in subtilisin, and as represented in S73. The family includes SwissProt:P25478 from Enterobacteria phage P2 which cleaves itself and then becomes the scaffold protein upon which the bacteriophage prohead is built - a mechanism quite common amongst phages .
Linderoth NA, Ziermann R, Haggard-Ljungquist E, Christie GE, Calendar R; , Nucleic Acids Res 1991;19:7207-7214.: Nucleotide sequence of the DNA packaging and capsid synthesis genes of bacteriophage P2. PUBMED:1837355 EPMC:1837355
Chang JR, Spilman MS, Rodenburg CM, Dokland T; , 2008; [Epub ahead of print]: Functional domains of the bacteriophage P2 scaffolding protein: Identification of residues involved in assembly and protease activity. PUBMED:19064277 EPMC:19064277
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR009228
The bacteriophage P2 capsid is formed by multiple copies of the capsid protein GpN. The scaffolding protein GpO, which is essential for the assembly of this capsid, consists of an N-terminal serine protease domain and a C-terminal scaffolding domain [PUBMED:1837355, PUBMED:19064277]. During capsid assembly, GpO interacts with GpN via the N-terminal domain, while the C-terminal domain plays an essential role as a scaffold. When capsid assembly is complete the C-terminal domain of GpO is cleaved autocatalytically. Cleavage of GpN to its mature form by the remaining N-terminal domain then completes the maturation process.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Biological process||viral capsid assembly (GO:0019069)|
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Curation and family details
|Seed source:||Pfam-B_1730 (release 9.0)|
|Number in seed:||5|
|Number in full:||734|
|Average length of the domain:||255.80 aa|
|Average identity of full alignment:||42 %|
|Average coverage of the sequence by the domain:||93.46 %|
|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:||6|
|Download:||download the raw HMM for this family|
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