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.
Automatic Gene Ontology annotation based on Rhea mapping.
Self-association properties of the bacteriophage lambda terminase holoenzyme: implications for the DNA packaging motor.
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Purified lambda terminase forms a heterotrimer of one gpA subunit and two gpNu1 subunits that assembles into a tetramer of heterotrimers and catalyzes IHF-dependent cos cleavage and viral DNA packaging.
"We find that purified, recombinant lambda terminase forms a homogeneous, heterotrimeric structure, consisting of one gpA molecule associated with two gpNu1 molecules (114.2 kDa)."
Bacteriophage lambda gpNu1 and Escherichia coli IHF proteins cooperatively bind and bend viral DNA: implications for the assembly of a genome-packaging motor.
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gpNu1 binds multiple recognition elements within cos and introduces a strong bend in cos-containing DNA cooperatively with E. coli IHF.
"Further, circular permutation experiments demonstrate that the viral and host proteins each introduce a strong bend in cos-containing DNA, but not nonspecific DNA substrates."
Prediction of an ATP reactive center in the small subunit, gpNu1, of the phage lambda terminase enzyme.
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Purified gpNu1 contains sequence motifs conserved in ATPases and hydrolyzes ATP with a low turnover number.
"The small subunit of the bacteriophage lambda terminase enzyme, the product of the phage's Nu1 gene, is shown to contain amino acid segments homologous to those present in a large number of ATPases. In keeping with these predictions, the purified protein has been found to hydrolyze ATP with a relatively low turnover number."
Kinetic and mutational dissection of the two ATPase activities of terminase, the DNA packaging enzyme of bacteriophage Chi.
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Note that the PubMed title prints "Chi" due to an indexing/typesetting error for the Greek letter lambda; the abstract and study characterize bacteriophage lambda terminase (gpNu1 and gpA) and demonstrate a low-affinity, DNA-stimulated ATPase site in gpNu1.
"In summary, the results indicate the presence of a low-affinity, DNA-stimulated ATPase center in gpNul, and a high-affinity site in gpA."
UniProtKB record for Nu1 (P03707)
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gpNu1 is the small subunit of the phage lambda terminase complex responsible for recognizing cosB packaging initiation elements.
"The small subunit is responsible for the binding to multiple recognition elements within the packaging initiation site cos (PubMed:15755448, PubMed:16618107, PubMed:2989542)."