ID   TERL_BPLP7              Reviewed;         475 AA.
AC   P16938;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Terminase, large subunit {ECO:0000255|HAMAP-Rule:MF_04148};
DE   AltName: Full=DNA-packaging protein gp2 {ECO:0000255|HAMAP-Rule:MF_04148};
DE   Includes:
DE     RecName: Full=Endonuclease {ECO:0000255|HAMAP-Rule:MF_04148};
DE              EC=3.1.21.- {ECO:0000255|HAMAP-Rule:MF_04148};
DE   Includes:
DE     RecName: Full=ATPase {ECO:0000255|HAMAP-Rule:MF_04148};
DE              EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_04148};
DE   Flags: Fragment;
GN   Name=2;
OS   Enterobacteria phage LP7 (Bacteriophage LP7).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Podoviridae; Lederbergvirus.
OX   NCBI_TaxID=10750;
OH   NCBI_TaxID=590; Salmonella.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2341038; DOI=10.1016/0378-1119(90)90058-y;
RA   Petri J.B., Schmieger H.;
RT   "Isolation of fragments with pac function for phage P22 from phage LP7 DNA
RT   and comparison of packaging gene 3 sequences.";
RL   Gene 88:47-55(1990).
CC   -!- FUNCTION: The terminase large subunit acts as an ATP driven molecular
CC       motor necessary for viral DNA translocation into empty capsids and as
CC       an endonuclease that cuts the viral genome to initiate and to end a
CC       packaging reaction. The terminase lies at a unique vertex of the
CC       procapsid and is composed of two subunits, a small terminase subunit
CC       involved in viral DNA recognition (packaging sequence), and a large
CC       terminase subunit possessing endonucleolytic and ATPase activities.
CC       Both terminase subunits heterooligomerize and are docked on the portal
CC       protein to form the packaging machine. The terminase large subunit
CC       exhibits endonuclease activity and cleaves the viral genome concatemer
CC       once the capsid is full (headful packaging). Once the capsid is
CC       packaged with the DNA, the terminase complex is substituted by the
CC       tail. {ECO:0000255|HAMAP-Rule:MF_04148}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_04148};
CC       Note=Nuclease activity probably requires 2 Mg(2+) ions per subunit.
CC       {ECO:0000255|HAMAP-Rule:MF_04148};
CC   -!- SUBUNIT: Interacts with the terminase small subunit; the active complex
CC       is composed of a monomer of the terminase large subunit and a nonamer
CC       ring of terminase small subunits. Interacts with the portal protein;
CC       this interaction allows the packaging of viral DNA. {ECO:0000255|HAMAP-
CC       Rule:MF_04148}.
CC   -!- DOMAIN: The ATPase region is in the N-terminus, whereas the nuclease
CC       region is in the C-terminus. {ECO:0000255|HAMAP-Rule:MF_04148}.
CC   -!- SIMILARITY: Belongs to the Lederbergvirus large terminase family.
CC       {ECO:0000255|HAMAP-Rule:MF_04148}.
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DR   EMBL; M32403; AAA88220.1; -; Genomic_DNA.
DR   SMR; P16938; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_04148; TERL_BPP22; 1.
DR   InterPro; IPR035421; Terminase_6C.
DR   InterPro; IPR044265; Terminase_large_su_BPP22.
DR   Pfam; PF17289; Terminase_6C; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Endonuclease; Hydrolase; Late protein; Magnesium;
KW   Metal-binding; Nuclease; Nucleotide-binding; Viral genome packaging;
KW   Viral release from host cell.
FT   CHAIN           1..>475
FT                   /note="Terminase, large subunit"
FT                   /id="PRO_0000077732"
FT   REGION          1..282
FT                   /note="ATPase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04148"
FT   REGION          1..58
FT                   /note="Interaction with the terminase small subunit"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04148"
FT   REGION          308..>475
FT                   /note="Nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04148"
FT   BINDING         317
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic; for nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04148"
FT   BINDING         455
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic; for nuclease activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04148"
FT   NON_TER         475
SQ   SEQUENCE   475 AA;  54673 MW;  6618F6D8A184F9CE CRC64;
     MELDAILDNL SDEEQIELLE LLEEEENYRN THLLYEFTPY SKQREFIDAG HDYQSDVLWL
     VTSLVSHLLA LLKSRFTLPG DTRERKVIRL MVNMAESGKV SVSMSQLSSG IGGETNETVT
     KTTQRILCGR IEENDEPGYG SPKEDSSWEK SSVLLILLII FSLSHHRLMV LKMHSICYFK
     HTRRHRHAAG DTITAYGLTK RLPYSIYAEG LTRTNKYGQF SILTFTPLMG MSDGVTKFLK
     NPSKSQKVVN MTIYDAEHYT DEQKEQIIAS YPEHEREARA RGIPTMGSGR IFQIPEETIK
     CQPFECPDHF YVIDAQDFGW NHPQAHIQLW WDKDADVFYL ARVWKKSENT AVQAWGAVKS
     WANKIPVAWP HDGHQHEKGG GEQLKTQYAD AGFSMLPDHA TFPDGGNSVE SGISELRDLM
     LEGRFKVFNT CEPFFEEFRL YHRDENGKIV KTNDDVLDAT RYGYMMRLRQ DDARY