TERL_BPP1
ID TERL_BPP1 Reviewed; 494 AA.
AC P27753;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 73.
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;
DE AltName: Full=Terminase large subunit;
GN Name=pacB;
OS Escherichia phage P1 (Bacteriophage P1).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Punavirus.
OX NCBI_TaxID=2886926;
OH NCBI_TaxID=543; Enterobacteriaceae.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1538406; DOI=10.1016/0022-2836(92)90256-j;
RA Skorupski K., Pierce J.C., Sauer B., Sternberg N.;
RT "Bacteriophage P1 genes involved in the recognition and cleavage of the
RT phage packaging site (pac).";
RL J. Mol. Biol. 223:977-989(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15489417; DOI=10.1128/jb.186.21.7032-7068.2004;
RA Lobocka M.B., Rose D.J., Plunkett G. III, Rusin M., Samojedny A.,
RA Lehnherr H., Yarmolinsky M.B., Blattner F.R.;
RT "Genome of bacteriophage P1.";
RL J. Bacteriol. 186:7032-7068(2004).
RN [3]
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:0000305|PubMed:15489417}.
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:0000305|PubMed:15489417}.
CC -!- SIMILARITY: Belongs to the punalikevirus large terminase family.
CC {ECO:0000305}.
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DR EMBL; M74046; AAA21724.1; -; Genomic_DNA.
DR EMBL; AF234172; AAQ14080.1; -; Genomic_DNA.
DR PIR; S21779; S21779.
DR RefSeq; YP_006576.1; NC_005856.1.
DR SMR; P27753; -.
DR GeneID; 2777432; -.
DR KEGG; vg:2777432; -.
DR Proteomes; UP000008091; Genome.
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; Reference proteome; Viral genome packaging;
KW Viral release from host cell.
FT CHAIN 1..494
FT /note="Probable terminase, large subunit"
FT /id="PRO_0000165277"
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
