ID   TERL_BPLSK              Reviewed;         540 AA.
AC   O21870;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Terminase large subunit {ECO:0000250|UniProtKB:D3WAC1};
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 SK1 (Lactococcus lactis bacteriophage SK1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Skunavirus.
OX   NCBI_TaxID=31532;
OH   NCBI_TaxID=1358; Lactococcus lactis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9383189; DOI=10.1046/j.1365-2958.1997.5491926.x;
RA   Chandry P.S., Moore S.C., Boyce J.D., Davidson B.E., Hillier A.J.;
RT   "Analysis of the DNA sequence, gene expression, origin of replication and
RT   modular structure of the Lactococcus lactis lytic bacteriophage sk1.";
RL   Mol. Microbiol. 26:49-64(1997).
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 (By similarity). The terminase lies at a unique
CC       vertex of the procapsid and is composed of two subunits, a small
CC       terminase subunit involved in viral DNA recognition (packaging
CC       sequence), and a large terminase subunit possessing endonucleolytic and
CC       ATPase activities (By similarity). Both terminase subunits
CC       heterooligomerize and are docked on the portal protein to form the
CC       packaging machine (By similarity). The terminase large subunit exhibits
CC       endonuclease activity and cleaves the viral genome concatemer (By
CC       similarity). {ECO:0000250|UniProtKB:Q9MCT1}.
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; AF011378; AAB70041.1; -; Genomic_DNA.
DR   RefSeq; NP_044948.1; NC_001835.1.
DR   SMR; O21870; -.
DR   GeneID; 1261297; -.
DR   KEGG; vg:1261297; -.
DR   Proteomes; UP000000839; 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_0000438251"
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;  62934 MW;  3AB5ABBEC2D89CFB CRC64;
     MYYLNKMLEY NKENGIIINK YIRKTIQKQI RIHNKYIYRY DRVTQAIEWI EDNFYLTTGN
     LMKIELLPTQ RWWYELMLGY DMIDEKGVQV NLINEIFLNL GRGSGKSSLM ATRVLNWMIL
     GGQYGGESLV IAYDNTQARH VFDQVRNQTE ASDTLRVYNE NKIFKSTKQG LEFASFKTTF
     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
     KLVENKLIHN QKVMQWALNN TAVKIGQSGD YMYTKKLEKD KIDPTVALTM ALEMAVSDEV