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2 (Terminase, large subunit)
FEATURES
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FAMILY
DESCRIPTION
Also known as TERL_BPLP7, 2. The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome to initiate and to end a packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer once the capsid is full (headful packaging). Once the capsid is packaged with the DNA, the terminase complex is substituted by the tail. Interacts with the terminase small subunit gp3; the active complex is probably heterooligomeric. Interacts with the portal protein; this interaction allows the packaging of viral DNA.
Also known as TERL_BPLP7, 2. The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome to initiate and to end a packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small termina ... More
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Terminase, large subunit

Molecular Synopsis