TERL_BPP21
ID TERL_BPP21 Reviewed; 642 AA.
AC P36693; Q38453;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Terminase, large subunit {ECO:0000255|HAMAP-Rule:MF_04144};
DE AltName: Full=DNA-packaging protein {ECO:0000255|HAMAP-Rule:MF_04144};
DE AltName: Full=DNA-packaging protein gp2;
DE AltName: Full=Gene product 2;
DE Short=gp2;
DE AltName: Full=Large terminase protein {ECO:0000255|HAMAP-Rule:MF_04144};
DE Includes:
DE RecName: Full=Endonuclease {ECO:0000255|HAMAP-Rule:MF_04144};
DE EC=3.1.21.4 {ECO:0000255|HAMAP-Rule:MF_04144};
DE Includes:
DE RecName: Full=Helicase {ECO:0000255|HAMAP-Rule:MF_04144};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_04144};
DE Includes:
DE RecName: Full=ATPase {ECO:0000255|HAMAP-Rule:MF_04144};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_04144};
GN Name=2;
OS Enterobacteria phage P21 (Bacteriophage 21) (Bacteriophage P21).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Lambdavirus.
OX NCBI_TaxID=10711;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith M.P.;
RL Thesis (1991), University of Iowa, United States.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8468297; DOI=10.1128/jb.175.8.2393-2399.1993;
RA Smith M.P., Feiss M.;
RT "Sites and gene products involved in lambdoid phage DNA packaging.";
RL J. Bacteriol. 175:2393-2399(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-309.
RX PubMed=3159906; DOI=10.1016/0022-2836(85)90217-7;
RA Miller G., Feiss M.;
RT "Sequence of the left end of phage 21 DNA.";
RL J. Mol. Biol. 183:246-249(1985).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 564-642.
RX PubMed=2969839; DOI=10.1093/genetics/119.3.477;
RA Wu W.-F., Christiansen S., Feiss M.;
RT "Domains for protein-protein interactions at the N and C termini of the
RT large subunit of bacteriophage lambda terminase.";
RL Genetics 119:477-484(1988).
RN [5]
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: 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 from the concetamer to
CC initiate and to end the packaging reaction. The terminase lies at a
CC unique vertex of the procapsid and is composed of two subunits, a small
CC terminase subunit involved in viral DNA recognition (binding to
CC packaging sequence cos), and a large terminase subunit possessing
CC endonucleolytic, ATPase and helicase activities (DNA maturation and
CC packaging). The terminase binds cooperatively with the host factor
CC IHFA/IHFB to the cos site at the junction of adjacent viral genomes.
CC The endonuclease activity cleaves the viral DNA generating 5'overhangs
CC of 12 bp in length. The helicase activity separates the cohesive ends
CC generating the single-stranded 'sticky' ends of the mature genome.
CC IHFA/IHFB is also necessary for the strand separation activity of the
CC terminase. The terminase remains bound to the left end of the genome to
CC be packaged, forming a stable DNA-terminase complex. In a reaction
CC facilitated by the viral assembly catalyst gpFI, the DNA-terminase
CC complex binds to the portal of the procapsid thereby activating the
CC translocase activity of the terminase. The terminase packages the viral
CC DNA into the procapsid until the next cos site on the concatemer
CC reaches the complex. The downstream cos site is then cut generating the
CC mature right end of the genome, the heterotrimer undocks from the DNA-
CC filled head and remains bound to the left end of concatemer's next
CC genome. {ECO:0000255|HAMAP-Rule:MF_04144}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endonucleolytic cleavage of DNA to give specific double-
CC stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04144};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04144};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04144};
CC Note=Probably binds 2 Mg(2+) ions per subunit (By similarity).
CC Necessary for the ATPase activity (By similarity).
CC {ECO:0000250|UniProtKB:P17312};
CC -!- SUBUNIT: Heterotrimer of two small and one large terminase subunits.
CC The catalytically competent terminase is composed of a tetramer of
CC heterotrimers. The tetramer forms a ring structure large enough to
CC encircle duplex DNA. Host IHFA/IHFB induces bending of viral DNA to
CC facilitate the assembly of the terminase tetramer of heterotrimers.
CC Interacts (via N-terminus) with the terminase small subunit (via C-
CC terminus). Interacts (via C-terminus) with the portal protein; this
CC interaction allows the packaging of viral DNA. {ECO:0000255|HAMAP-
CC Rule:MF_04144}.
CC -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04144}.
CC Note=The terminase lies at a unique vertex of the procapsid during
CC viral DNA packaging. {ECO:0000255|HAMAP-Rule:MF_04144}.
CC -!- DOMAIN: The N-terminus is involved in the formation of the heterotrimer
CC with the small subunit. The N-terminus part contains the translocase
CC activity involved in DNA packaging. At the N-terminus, there is a high
CC affinity ATPase center that is probably needed for the packaging
CC activity. The Walker A motif of the ATPase center is responsible for
CC interacting with the ATP phosphate and the Q motif governs force
CC generation and the interaction with DNA. The C-terminus contains the
CC site specific endonuclease (cos-cleavage) and strand separation
CC (helicase) activities required for genome maturation. A second ATPase
CC catalytic site regulates the genome maturation. The C-terminus very end
CC is involved in binding to the procapsid. Contains a basic leucine
CC zipper (bZIP) that may be involved in the formation of the terminase.
CC {ECO:0000255|HAMAP-Rule:MF_04144}.
CC -!- SIMILARITY: Belongs to the lambdavirus large terminase family.
CC {ECO:0000255|HAMAP-Rule:MF_04144}.
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DR EMBL; M81255; AAA32340.1; -; Genomic_DNA.
DR EMBL; X02501; CAA26343.1; -; Genomic_DNA.
DR EMBL; M23775; AAA32338.1; -; Genomic_DNA.
DR EMBL; X12638; CAA31174.1; -; Genomic_DNA.
DR PIR; B49849; B49849.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0098009; C:viral terminase, large subunit; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019073; P:viral DNA genome packaging; IEA:UniProtKB-UniRule.
DR HAMAP; MF_04144; TERL_LAMBDA; 1.
DR InterPro; IPR008866; Phage_lambda_GpA-like.
DR Pfam; PF05876; Terminase_GpA; 1.
PE 3: Inferred from homology;
KW ATP-binding; Endonuclease; Host cytoplasm; Hydrolase; Magnesium;
KW Metal-binding; Nuclease; Nucleotide-binding; Viral genome packaging;
KW Viral release from host cell.
FT CHAIN 1..642
FT /note="Terminase, large subunit"
FT /id="PRO_0000077674"
FT REGION 1..48
FT /note="Interaction with the terminase small subunit"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04144"
FT REGION 166..353
FT /note="DNA packaging/ATPase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04144"
FT REGION 401..587
FT /note="Endonuclease/helicase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04144"
FT REGION 574..585
FT /note="Basic"
FT /evidence="ECO:0000250|UniProtKB:P03708"
FT REGION 589..617
FT /note="Leucine zipper"
FT /evidence="ECO:0000250|UniProtKB:P03708"
FT REGION 611..642
FT /note="Prohead binding"
FT /evidence="ECO:0000250|UniProtKB:P03708"
FT MOTIF 42..51
FT /note="Q motif"
FT /evidence="ECO:0000250|UniProtKB:P03708"
FT MOTIF 76..83
FT /note="Walker A motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04144"
FT MOTIF 174..179
FT /note="Walker B motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04144"
FT ACT_SITE 179
FT /note="For ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04144"
FT BINDING 401
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04144"
FT BINDING 491..498
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04144"
FT SITE 46
FT /note="ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04144"
FT CONFLICT 129
FT /note="M -> L (in Ref. 3; CAA26343/AAA32338)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 642 AA; 72622 MW; 46FB8DAD19EA5917 CRC64;
MISDAQKAAN AAGAIATGLL SLIIPVPLTT VQWANKHYYL PKESSYTPGR WETLPFQVGI
MNCMGNDLIR TVNLIKSARV GYTKMLLGVE AYFIEHKSRN SLLFQPTDSA AEDFMKSHVE
PTIRDVPAML ELAPWFGRKH RDNTLTLKRF SSGVGFWCLG GAAAKNYREK SVDVVCYDEL
SSFEPDVEKE GSPTLLGDKR IEGSVWPKSI RGSTPKIKGS CQIEKAANES AHFMRFYVPC
PHCGEEQYLK FGDDASPFGL KWEKNKPESV FYLCEHHGCV IHQSELDQSN GRWICENTGM
WTRDGLMFFS ARGDEIPPPR SITFHIWTAY SPFTTWVQIV YDWLDALKDP NGLKTFVNTT
LGETWEEAVG EKLDHQVLMD KVVRYTAAVP ARVVYLTAGI DSQRNRFEMY VWGWAPGEEA
FLVDKIIIMG RPDEEETLLR VDAAINKKYR HADGTEMTIS RVCWDIGGID GEIVYQRSKK
HGVFRVLPVK GASVYGKPVI TMPKTRNQRG VYLCEVGTDT AKEILYARMK ADPTPVDEAT
SYAIRFPDDP EIFSQTEAQQ LVAEELVEKW EKGKMRLLWD NKKRRNEALD CLVYAYAALR
VSVQRWQLDL AVLAKSREEE TTRPTLKELA AKLSGGVNGY SR
