Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt.
Gene Ontology annotation based on UniProtKB/Swiss-Protize keywords
Combined Automated Annotation using Multiple IEA Methods.
Membrane interaction of the portal protein gp20 of bacteriophage T4.
-
Nascent gp20 is escorted by host chaperones DnaK, trigger factor, and GroEL to dock on the E. coli inner membrane at YidC, where it initiates prohead assembly.
"With a cross-linking approach, we show here that gp20 and gp20s are escorted by the chaperones DnaK, trigger factor, and GroEL and dock on the membrane at the membrane protein YidC."
Cryo-EM structure of the bacteriophage T4 portal protein assembly at near-atomic resolution.
-
The 3.6 A cryo-EM structure of the dodecameric gp20 portal complex reveals the clip, stem, wing, and crown domains and demonstrates its roles in head initiation, gp17 motor docking, and DNA packaging.
"The gp20 structure also verifies that the portal assembly is required for initiating head assembly, for attachment of the packaging motor, and for participation in DNA packaging."
UniProtKB entry P13334 (PORT_BPT4)
Deep research literature synthesis for bacteriophage T4 gene 20 (gp20)
-
gp20 forms a 12-subunit ring at the unique fivefold vertex of the prolate capsid and coordinates head initiation, DNA packaging, and genome ejection.
"The target protein is **gene product 20 (gp20)** of **Enterobacteria phage T4**, which is experimentally characterized as the **portal protein** forming the unique portal vertex of the T4 capsid (head)."