P03694 · TERL_BPT7

Function

function

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 at a unique and precise dsDNA sequence to initiate and to end a packaging reaction (By similarity).
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 (By similarity).
Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine (PubMed:23632014).
The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer (By similarity).
Once the DNA is packaged, the terminase detaches from the portal and gets replaced by the tail to finish maturation of the virion (PubMed:23632014).

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Features

Showing features for binding site.

158650100150200250300350400450500550
TypeIDPosition(s)Description
Binding site364Mg2+ 1 (UniProtKB | ChEBI); catalytic; for nuclease activity
Binding site364Mg2+ 2 (UniProtKB | ChEBI); catalytic; for nuclease activity
Binding site420Mg2+ 2 (UniProtKB | ChEBI); catalytic; for nuclease activity
Binding site518Mg2+ 1 (UniProtKB | ChEBI); catalytic; for nuclease activity

GO annotations

AspectTerm
Cellular Componentviral terminase, large subunit
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular Functionendonuclease activity
Molecular Functionmetal ion binding
Biological Processchromosome organization
Biological Processviral DNA genome packaging

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Terminase, large subunit
  • Alternative names
    • DNA-packaging protein
    • Gene product 19 (Gp19)

Including 2 domains:

  • Recommended name
    ATPase
  • EC number
  • Recommended name
    Endonuclease
  • EC number

Gene names

    • Ordered locus names
      19

Organism names

Accessions

  • Primary accession
    P03694

Proteomes

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001065411-586Terminase, large subunit

Interaction

Subunit

Homopentamer (PubMed:23632014).
Interacts with the terminase small subunit; the active complex is probably heterooligomeric (PubMed:23632014).
Interacts with the portal protein (PubMed:23632014).

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, motif.

TypeIDPosition(s)Description
Region1-229ATPase activity
Motif58-65Walker A motif
Motif156-161Walker B motif
Region344-429Nuclease activity
Region571-586Involved in prohead binding

Domain

The ATPase region is in the N-terminus, whereas the nuclease region is in the central part. The C-terminus is involved in prohead binding.

Sequence similarities

Belongs to the Teseptimavirus large terminase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    586
  • Mass (Da)
    66,261
  • Last updated
    1986-07-21 v1
  • Checksum
    0030B8EE701CB0A9
MSTQSNRNALVVAQLKGDFVAFLFVLWKALNLPVPTKCQIDMAKVLANGDNKKFILQAFRGIGKSFITCAFVVWSLWRDPQLKILIVSASKERADANSIFIKNIIDLLPFLSELKPRPGQRDSVISFDVGPANPDHSPSVKSVGITGQLTGSRADIIIADDVEIPSNSATMGAREKLWTLVQEFAALLKPLPSSRVIYLGTPQTEMTLYKELEDNRGYTTIIWPALYPRTREENLYYSQRLAPMLRAEYDENPEALAGTPTDPVRFDRDDLRERELEYGKAGFTLQFMLNPNLSDAEKYPLRLRDAIVAALDLEKAPMHYQWLPNRQNIIEDLPNVGLKGDDLHTYHDCSNNSGQYQQKILVIDPSGRGKDETGYAVLYTLNGYIYLMEAGGFRDGYSDKTLELLAKKAKQWGVQTVVYESNFGDGMFGKVFSPILLKHHNCAMEEIRARGMKEMRICDTLEPVMQTHRLVIRDEVIRADYQSARDVDGKHDVKYSLFYQMTRITREKGALAHDDRLDALALGIEYLRESMQLDSVKVEGEVLADFLEEHMMRPTVAATHIIEMSVGGVDVYSEDDEGYGTSFIEW

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
V01146
EMBL· GenBank· DDBJ
CAA24440.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp