ID   TERL_BPLP2              Reviewed;         540 AA.
AC   D3WAC1;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=Terminase large subunit {ECO:0000303|PubMed:24027307};
DE   AltName: Full=DNA-packaging protein;
DE   AltName: Full=Gene product 2 {ECO:0000305};
DE            Short=gp2 {ECO:0000305};
DE   Includes:
DE     RecName: Full=Endonuclease;
DE              EC=3.1.-.-;
DE   Includes:
DE     RecName: Full=ATPase;
DE              EC=3.6.4.-;
OS   Lactococcus phage p2 (Lactococcus lactis bacteriophage p2).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Skunavirus.
OX   NCBI_TaxID=254252;
OH   NCBI_TaxID=1358; Lactococcus lactis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tremblay D.M., Deveau H., Moineau S.;
RT   "Complete genomic sequence of Lactococcus lactis phage p2.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
RX   PubMed=24027307; DOI=10.1128/jvi.02033-13;
RA   Bebeacua C., Tremblay D., Farenc C., Chapot-Chartier M.P., Sadovskaya I.,
RA   van Heel M., Veesler D., Moineau S., Cambillau C.;
RT   "Structure, adsorption to host, and infection mechanism of virulent
RT   lactococcal phage p2.";
RL   J. Virol. 87:12302-12312(2013).
CC   -!- FUNCTION: Probable terminase large subunit (PubMed:24027307). The
CC       terminase large subunit acts as an ATP driven molecular motor necessary
CC       for viral DNA translocation into empty capsids and as an endonuclease
CC       that cuts the viral genome to initiate and to end a packaging reaction
CC       (By similarity). The terminase lies at a unique vertex of the procapsid
CC       and is composed of two subunits, a small terminase subunit involved in
CC       viral DNA recognition (packaging sequence), and a large terminase
CC       subunit possessing endonucleolytic and ATPase activities (By
CC       similarity). Both terminase subunits heterooligomerize and are docked
CC       on the portal protein to form the packaging machine (By similarity).
CC       The terminase large subunit exhibits endonuclease activity and cleaves
CC       the viral genome concatemer (By similarity).
CC       {ECO:0000250|UniProtKB:Q9MCT1, ECO:0000269|PubMed:24027307}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:P54308};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P54308};
CC       Note=Binds 2 divalent metal cations per subunit.
CC       {ECO:0000250|UniProtKB:P54308};
CC   -!- SUBUNIT: Interacts with the terminase small subunit; the active complex
CC       is probably heterooligomeric. {ECO:0000250|UniProtKB:Q9MCT1}.
CC   -!- SIMILARITY: Belongs to the skunavirus terminase large subunit family.
CC       {ECO:0000305}.
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DR   EMBL; GQ979703; ADC80078.1; -; Genomic_DNA.
DR   SMR; D3WAC1; -.
DR   Proteomes; UP000002348; Genome.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005021; Terminase_largesu_Lambdalike.
DR   PANTHER; PTHR41287; PTHR41287; 1.
DR   Pfam; PF03354; Terminase_1; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Magnesium; Manganese; Metal-binding; Nuclease;
KW   Reference proteome; Viral genome packaging; Viral release from host cell.
FT   CHAIN           1..540
FT                   /note="Terminase large subunit"
FT                   /id="PRO_0000438221"
FT   BINDING         352
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic; for nuclease activity"
FT                   /evidence="ECO:0000250|UniProtKB:P54308"
FT   BINDING         352
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic; for nuclease activity"
FT                   /evidence="ECO:0000250|UniProtKB:P54308"
FT   BINDING         424
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic; for nuclease activity"
FT                   /evidence="ECO:0000250|UniProtKB:P54308"
FT   BINDING         523
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic; for nuclease activity"
FT                   /evidence="ECO:0000250|UniProtKB:P54308"
SQ   SEQUENCE   540 AA;  62935 MW;  2FA2BA647615349A CRC64;
     MYYLNKMLEY NKENGIIINK YIRKTIQKQI RIHNKYIYRY DRVTQAIEWI EDNFYLTTGN
     LMKIELLPTQ RWWYELMLGY DMIDEKGVQV NLINEIFLNL GRGSGKSSLM ATRVLNWMIL
     GGQYGGESLV IAYDNTQARH VFDQVRNQTE ASDTLRVYNE NKIFKSTKQG LEFTSFKTTF
     KKQTNDTLRA QGGNSSLNIF DEVHTYGEDI TESVNKGSRQ KQDNWQSIYI TSGGLKRDGL
     YDKLVERFKS EEEFYNDRSF GLLYMLENHE QVKDKKNWTM ALPLIGSVPK WSGVIEEYEL
     AQGDPALQNK FLAFNMGLPM QDTAYYFTPQ DTKLTDFNLS VFNKNRTYVG IDLSLIGDLT
     AVSFVCELEG KTYSHTLTFS VRSQYEQLDT EQQELWTEFV DRGELILLDT EYINVNDLIP
     HINDFRTKTG CRLRKIGYDP ARYEILKGLI ERYFFDKDGD NQRAIRQGFS MNDYIKLLKS
     KLAENKLIHN QKVMQWALNN TAVKIGQSGD YMYTKKLEKD KIDPTVALTM ALEMAVSDEV