ID   TERL_BPP7               Reviewed;         494 AA.
AC   Q5XLR0;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Probable terminase, large subunit {ECO:0000305};
DE            EC=3.1.-.- {ECO:0000305};
DE   AltName: Full=DNA-packaging protein B;
DE   AltName: Full=PACase B protein;
DE   AltName: Full=Terminase B protein;
GN   Name=pacB;
OS   Enterobacteria phage P7 (Bacteriophage P7).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Punavirus.
OX   NCBI_TaxID=10682;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Sauer B.V., McDermott J.;
RT   "Survey of the pac-c1 region in P1-related phages.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   REVIEW.
RX   PubMed=18687036; DOI=10.1146/annurev.genet.42.110807.091545;
RA   Rao V.B., Feiss M.;
RT   "The bacteriophage DNA packaging motor.";
RL   Annu. Rev. Genet. 42:647-681(2008).
CC   -!- FUNCTION: Component of the molecular motor that translocates genomic
CC       DNA in empty capsid during DNA packaging. Heterooligomerize with small
CC       terminase protein to be docked on capsid portal protein. Forms a ring-
CC       like structure through which genomic DNA is translocated into the
CC       capsid. May have or induce an endonuclease activity to cleave the
CC       genome concatemer after encapsidation. {ECO:0000250|UniProtKB:P27753}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P17312};
CC       Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P17312};
CC   -!- SUBUNIT: Interacts with pacA protein. {ECO:0000250|UniProtKB:P27753}.
CC   -!- SIMILARITY: Belongs to the punalikevirus large terminase family.
CC       {ECO:0000305}.
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DR   EMBL; AY751747; AAV28854.1; -; Genomic_DNA.
DR   SMR; Q5XLR0; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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.
PE   3: Inferred from homology;
KW   ATP-binding; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW   Nucleotide-binding; Viral genome packaging; Viral release from host cell.
FT   CHAIN           1..494
FT                   /note="Probable terminase, large subunit"
FT                   /id="PRO_0000165278"
FT   MOTIF           56..63
FT                   /note="Walker A motif"
FT   MOTIF           158..163
FT                   /note="Walker B motif"
FT   ACT_SITE        163
FT                   /note="For ATPase activity"
FT                   /evidence="ECO:0000255"
FT   BINDING         26..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         293
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic; for nuclease activity"
FT                   /evidence="ECO:0000250|UniProtKB:P17312"
FT   BINDING         293
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic; for nuclease activity"
FT                   /evidence="ECO:0000250|UniProtKB:P17312"
FT   BINDING         356
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic; for nuclease activity"
FT                   /evidence="ECO:0000250|UniProtKB:P17312"
FT   BINDING         446
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic; for nuclease activity"
FT                   /evidence="ECO:0000250|UniProtKB:P17312"
SQ   SEQUENCE   494 AA;  55605 MW;  3935D394DDBF7AF3 CRC64;
     MARSCVTDPR WRELVALYRY DWIAAADVLF GKTPTWQQDE IIESTQQDGS WTSVTSGHGT
     GKSDMTSIIA ILFIMFFPGA RVILVANKRQ QVLDGIFKYI KSNWATAVSR FPWLSKYFIL
     TETSFFEVTG KGVWTILIKS CRPGNEEALA GEHADHLLYI IDEASGVSDK AFSVITGALT
     GKDNRILLLS QPTRPSGYFY DSHHRLAIRP GNPDGLFTAI ILNSEESPLV DAKFIRAKLA
     EYGGRDNPMY MIKVRGEFPK SQDGFLLGRD EVERATRRKV KIAKGWGWVA CVDVAGGTGR
     DKSVINIMMV SGQRNKRRVI NYRMLEYTDV TETQLAAKIF AECNPERFPN ITIAIDGDGL
     GKSTADLMYE RYGITVQRIR WGKKMHSRED KSLYFDMRAF ANIQAAEAVK SGRMRLDKGA
     ATIEEASKIP VGINSAGQWK VMSKEDMKKK LNLHSPDHWD TYCFAMLANY VPQDEVLSVE
     DEAQVDEALA WLNE