TERL_BPT3
ID TERL_BPT3 Reviewed; 586 AA.
AC P10310;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Terminase, large subunit {ECO:0000255|HAMAP-Rule:MF_04147};
DE AltName: Full=DNA-packaging protein {ECO:0000255|HAMAP-Rule:MF_04147};
DE AltName: Full=Gene product 19;
DE Short=gp19;
DE Includes:
DE RecName: Full=ATPase {ECO:0000255|HAMAP-Rule:MF_04147};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_04147, ECO:0000269|PubMed:2956757, ECO:0000269|PubMed:8289246};
DE Includes:
DE RecName: Full=Endonuclease {ECO:0000255|HAMAP-Rule:MF_04147};
DE EC=3.1.21.- {ECO:0000255|HAMAP-Rule:MF_04147, ECO:0000269|PubMed:8289246};
GN Name=19;
OS Enterobacteria phage T3 (Bacteriophage T3).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Autographiviridae; Studiervirinae; Teetrevirus;
OC Escherichia virus T3.
OX NCBI_TaxID=10759;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3010556; DOI=10.1016/0042-6822(86)90055-3;
RA Yamada M., Fujisawa H., Kato H., Hamada K., Minagawa T.;
RT "Cloning and sequencing of the genetic right end of bacteriophage T3 DNA.";
RL Virology 151:350-361(1986).
RN [2]
RP ERRATUM OF PUBMED:3010556.
RA Yamada M., Fujisawa H., Kato H., Hamada K., Minagawa T.;
RL Virology 154:246-246(1986).
RN [3]
RP FUNCTION, AND COFACTOR.
RX PubMed=3754362; DOI=10.1016/0042-6822(86)90109-1;
RA Hamada K., Fujisawa H., Minagawa T.;
RT "A defined in vitro system for packaging of bacteriophage T3 DNA.";
RL Virology 151:119-123(1986).
RN [4]
RP FUNCTION, AND COFACTOR.
RX PubMed=3617498; DOI=10.1016/0042-6822(87)90462-4;
RA Shibata H., Fujisawa H., Minagawa T.;
RT "Early events in DNA packaging in a defined in vitro system of
RT bacteriophage T3.";
RL Virology 159:250-258(1987).
RN [5]
RP CATALYTIC ACTIVITY.
RX PubMed=2956757; DOI=10.1016/0042-6822(87)90461-2;
RA Hamada K., Fujisawa H., Minagawa T.;
RT "Characterization of ATPase activity of a defined in vitro system for
RT packaging of bacteriophage T3 DNA.";
RL Virology 159:244-249(1987).
RN [6]
RP MUTAGENESIS OF GLY-61; GLY-424; LYS-430 AND HIS-553.
RX PubMed=1989388; DOI=10.1016/0042-6822(91)90084-o;
RA Kimura M., Fujisawa H.;
RT "Dissection of functional domains of the packaging protein of bacteriophage
RT T3 by site-directed mutagenesis.";
RL Virology 180:709-715(1991).
RN [7]
RP FUNCTION, MUTAGENESIS OF HIS-344; HIS-347; GLY-369 AND GLY-424, CATALYTIC
RP ACTIVITY, AND COFACTOR.
RX PubMed=8289246; DOI=10.1016/s0022-2836(05)80031-2;
RA Morita M., Tasaka M., Fujisawa H.;
RT "Analysis of functional domains of the packaging proteins of bacteriophage
RT T3 by site-directed mutagenesis.";
RL J. Mol. Biol. 235:248-259(1994).
RN [8]
RP DOMAIN.
RX PubMed=7844832; DOI=10.1006/jmbi.1994.0052;
RA Morita M., Tasaka M., Fujisawa H.;
RT "Structural and functional domains of the large subunit of the
RT bacteriophage T3 DNA packaging enzyme: importance of the C-terminal region
RT in prohead binding.";
RL J. Mol. Biol. 245:635-644(1995).
RN [9]
RP DOMAIN.
RX PubMed=7645255; DOI=10.1006/viro.1995.1433;
RA Morita M., Tasaka M., Fujisawa H.;
RT "Analysis of the fine structure of the prohead binding domain of the
RT packaging protein of bacteriophage T3 using a hexapeptide, an analog of a
RT prohead binding site.";
RL Virology 211:516-524(1995).
RN [10]
RP MOTIF.
RX PubMed=15051382; DOI=10.1016/j.virol.2003.11.006;
RA Mitchell M.S., Rao V.B.;
RT "Novel and deviant Walker A ATP-binding motifs in bacteriophage large
RT terminase-DNA packaging proteins.";
RL Virology 321:217-221(2004).
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 at a unique and precise
CC dsDNA sequence to initiate and to end a packaging reaction
CC (PubMed:3617498, PubMed:3754362). The terminase lies at a unique vertex
CC of the procapsid and is composed of two subunits, a small terminase
CC subunit involved in viral DNA recognition (packaging sequence), and a
CC large terminase subunit possessing endonucleolytic and ATPase
CC activities (PubMed:8289246). Both terminase subunits heterooligomerize
CC and are docked on the portal protein to form the packaging machine (By
CC similarity). The terminase large subunit exhibits endonuclease activity
CC and cleaves the viral genome concatemer. Once the DNA is packaged, the
CC terminase detaches from the connector and gets replaced by the tail to
CC finish maturation of the virion (By similarity). {ECO:0000255|HAMAP-
CC Rule:MF_04147, ECO:0000269|PubMed:3617498, ECO:0000269|PubMed:3754362,
CC ECO:0000305|PubMed:8289246}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04147,
CC ECO:0000269|PubMed:3617498, ECO:0000269|PubMed:3754362,
CC ECO:0000305|PubMed:8289246};
CC -!- SUBUNIT: Homopentamer. Interacts with the terminase small subunit; the
CC active complex is probably heterooligomeric. Interacts with the portal
CC protein. {ECO:0000255|HAMAP-Rule:MF_04147}.
CC -!- DOMAIN: The ATPase region is in the N-terminus, whereas the nuclease
CC region is in the central part. The C-terminus is involved in prohead
CC binding (PubMed:7844832). {ECO:0000269|PubMed:7844832}.
CC -!- DOMAIN: The ATPase region is in the N-terminus, whereas the nuclease
CC region is in the central part. The C-terminus is involved in prohead
CC binding. {ECO:0000255|HAMAP-Rule:MF_04147}.
CC -!- SIMILARITY: Belongs to the Teseptimavirus large terminase family.
CC {ECO:0000255|HAMAP-Rule:MF_04147}.
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DR EMBL; M14784; AAA92528.1; -; Genomic_DNA.
DR PIR; F23476; JVBPB3.
DR SMR; P10310; -.
DR PRIDE; P10310; -.
DR GO; GO:0098009; C:viral terminase, large subunit; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019073; P:viral DNA genome packaging; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_04147; TERL_T7; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR044271; Terminase_large_su_gp19.
PE 1: Evidence at protein level;
KW ATP-binding; Endonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease;
KW Nucleotide-binding; Viral genome packaging; Viral release from host cell.
FT CHAIN 1..586
FT /note="Terminase, large subunit"
FT /id="PRO_0000106540"
FT REGION 1..229
FT /note="ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04147,
FT ECO:0000269|PubMed:8289246"
FT REGION 344..429
FT /note="Nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04147"
FT REGION 571..586
FT /note="Involved in prohead binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04147,
FT ECO:0000269|PubMed:7844832"
FT MOTIF 58..65
FT /note="Walker A motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04147,
FT ECO:0000269|PubMed:15051382"
FT MOTIF 156..161
FT /note="Walker B motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04147,
FT ECO:0000269|PubMed:15051382"
FT BINDING 364
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04147"
FT BINDING 364
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04147"
FT BINDING 420
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04147"
FT BINDING 518
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04147"
FT MUTAGEN 61
FT /note="G->D: Defective in DNA packaging."
FT /evidence="ECO:0000269|PubMed:1989388"
FT MUTAGEN 344
FT /note="H->D: Defective in DNA packaging. No effect on DNA
FT cleavage."
FT /evidence="ECO:0000269|PubMed:8289246"
FT MUTAGEN 347
FT /note="H->R: Possibly defective in packaging initiation."
FT /evidence="ECO:0000269|PubMed:8289246"
FT MUTAGEN 369
FT /note="G->D: Defective in DNA cleavage."
FT /evidence="ECO:0000269|PubMed:8289246"
FT MUTAGEN 424
FT /note="G->E: Defective in DNA cleavage."
FT /evidence="ECO:0000269|PubMed:1989388,
FT ECO:0000269|PubMed:8289246"
FT MUTAGEN 430
FT /note="K->T: No effect on DNA packaging."
FT /evidence="ECO:0000269|PubMed:1989388"
FT MUTAGEN 553
FT /note="H->L: No effect on DNA packaging."
FT /evidence="ECO:0000269|PubMed:1989388"
SQ SEQUENCE 586 AA; 66673 MW; F9FD00D59DDF2D26 CRC64;
MSTQSNRNAL VVAQLKGDFV AFLFVLWKAL NLPVPTKCQI DMAKVLANGD NKKFILQAFR
GIGKSFITCA FVVWTLWRDP QLKILIVSAS KERADLNSIF IKNIIDLLPF LDELKPSPGQ
RDSVISFDVG PAKPDHSPSV KSVGITGQLT GSRADIIIAD DVEIPSNSAT QGAREKLWTL
VQEFRALLKP LPTSRVIYLG TPQTEMTLYK ELEDNRGYTT IIWPALYPRS REEDLYYGER
LAPMLREEFN DGFEMLQGQP TDPVRFDMED LRERELEYGK AGFTLQFMLN PNLSDAEKYP
LRLRDAIVCG LDFEKAPMHY QWLPNRQNRN EELPNVGLKG DDIHSYHSCS QNTGQYQQRI
LVIDPSGRGK DETGYAVLFT LNGYIYLMEA GGFPDGYSDK TLESLAKKAN EWKVQTVVFE
SNFGDGMFGK VFSPVLLKHH AAALEEIRAR GMKELRICDT LEPVLSTHRL VIRDEVIRED
YQTARDADGK HDVRYSLFYQ LTRMAREKGA VAHDDRLDAF RLGVEFLRST MELDAVKVEA
EVLEAFLEEH MEHPIHSAGH VVTAMVDGME LYWEDDDVNG DRFINW
