Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Combined Automated Annotation using Multiple IEA Methods.
Analysis of T4 phage proteins. I. Conversion of precursor proteins into lower molecular weight peptides during normal capsid formation.
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Precursor P23 (gp23) is proteolytically converted into the mature major capsid protein (A-protein / gp23*), accounting for ~60% of total capsid protein during normal T4 head morphogenesis.
"conversion of P23 into A-protein and alteration of the protein coded by gene 22 (P22) appeared to be vital steps in formation of normal capsids."
UniProtKB entry P04535 (CAPSD_BPT4)
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gp23 self-associates into hexamers to build the icosahedral capsid shell and is folded by the host GroEL-phage gp31 chaperonin complex.
"The major capsid protein self-associates to form 160 hexamers, building most of the T=13 laevo capsid."
Deep research literature synthesis for bacteriophage T4 gene gp23 (23)
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930 copies of mature gp23* assemble into 155 hexamers forming the Tend=13 laevo, Tmid=20 prolate icosahedral capsid of bacteriophage T4.
"In the mature virion it is present as the **proteolytically processed** form **gp23***, which assembles into **hexameric capsomers** to build the **hexagonal lattice** of the **prolate icosahedral** head."