TERL_BPT7
ID TERL_BPT7 Reviewed; 586 AA.
AC P03694;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 86.
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};
DE Includes:
DE RecName: Full=Endonuclease {ECO:0000255|HAMAP-Rule:MF_04147};
DE EC=3.1.21.- {ECO:0000255|HAMAP-Rule:MF_04147};
GN OrderedLocusNames=19;
OS Escherichia phage T7 (Bacteriophage T7).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Autographiviridae; Studiervirinae; Teseptimavirus.
OX NCBI_TaxID=10760;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6864790; DOI=10.1016/s0022-2836(83)80282-4;
RA Dunn J.J., Studier F.W.;
RT "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of
RT T7 genetic elements.";
RL J. Mol. Biol. 166:477-535(1983).
RN [2]
RP DOMAIN.
RX PubMed=16377618; DOI=10.1074/jbc.m511817200;
RA Ponchon L., Boulanger P., Labesse G., Letellier L.;
RT "The endonuclease domain of bacteriophage terminases belongs to the
RT resolvase/integrase/ribonuclease H superfamily: a bioinformatics analysis
RT validated by a functional study on bacteriophage T5.";
RL J. Biol. Chem. 281:5829-5836(2006).
RN [3] {ECO:0007744|PDB:4BIJ, ECO:0007744|PDB:4BIL}
RP STRUCTURE BY ELECTRON MICROSCOPY (16.0 ANGSTROMS) OF 1-476, FUNCTION,
RP INTERACTION WITH THE PORTAL PROTEIN, SUBUNIT, AND INTERACTION WITH THE
RP TERMINASE SMALL SUBUNIT.
RX PubMed=23632014; DOI=10.1074/jbc.m112.448951;
RA Dauden M.I., Martin-Benito J., Sanchez-Ferrero J.C., Pulido-Cid M.,
RA Valpuesta J.M., Carrascosa J.L.;
RT "Large terminase conformational change induced by connector binding in
RT bacteriophage T7.";
RL J. Biol. Chem. 288:16998-17007(2013).
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 (By
CC similarity). The terminase lies at a unique vertex of the procapsid and
CC is composed of two subunits, a small terminase subunit involved in
CC viral DNA recognition (packaging sequence), and a large terminase
CC subunit possessing endonucleolytic and ATPase activities (By
CC similarity). Both terminase subunits heterooligomerize and are docked
CC on the portal protein to form the packaging machine (PubMed:23632014).
CC The terminase large subunit exhibits endonuclease activity and cleaves
CC the viral genome concatemer (By similarity). Once the DNA is packaged,
CC the terminase detaches from the portal and gets replaced by the tail to
CC finish maturation of the virion (PubMed:23632014). {ECO:0000255|HAMAP-
CC Rule:MF_04147, ECO:0000269|PubMed:23632014}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P17312,
CC ECO:0000255|HAMAP-Rule:MF_04147};
CC -!- SUBUNIT: Homopentamer (PubMed:23632014). Interacts with the terminase
CC small subunit; the active complex is probably heterooligomeric
CC (PubMed:23632014). Interacts with the portal protein (PubMed:23632014).
CC {ECO:0000255|HAMAP-Rule:MF_04147, ECO:0000269|PubMed:23632014}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; V01146; CAA24440.1; -; Genomic_DNA.
DR PIR; S42338; JVBPB7.
DR RefSeq; NP_042010.1; NC_001604.1.
DR PDB; 4BIJ; EM; 16.00 A; A/B/C/D/E=1-476.
DR PDB; 4BIL; EM; 29.00 A; A/B/C/D/E=1-476.
DR PDBsum; 4BIJ; -.
DR PDBsum; 4BIL; -.
DR SMR; P03694; -.
DR IntAct; P03694; 1.
DR MINT; P03694; -.
DR GeneID; 1261062; -.
DR KEGG; vg:1261062; -.
DR Proteomes; UP000000840; Genome.
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 3D-structure; ATP-binding; Endonuclease; Hydrolase; Magnesium;
KW Metal-binding; Nuclease; Nucleotide-binding; Reference proteome;
KW Viral genome packaging; Viral release from host cell.
FT CHAIN 1..586
FT /note="Terminase, large subunit"
FT /id="PRO_0000106541"
FT REGION 1..229
FT /note="ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04147,
FT ECO:0000305|PubMed:23632014"
FT REGION 344..429
FT /note="Nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04147,
FT ECO:0000305|PubMed:23632014"
FT REGION 571..586
FT /note="Involved in prohead binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04147"
FT MOTIF 58..65
FT /note="Walker A motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04147"
FT MOTIF 156..161
FT /note="Walker B motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04147"
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 ECO:0000305|PubMed:16377618"
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 ECO:0000305|PubMed:16377618"
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 ECO:0000305|PubMed:16377618"
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 ECO:0000305|PubMed:16377618"
SQ SEQUENCE 586 AA; 66261 MW; 0030B8EE701CB0A9 CRC64;
MSTQSNRNAL VVAQLKGDFV AFLFVLWKAL NLPVPTKCQI DMAKVLANGD NKKFILQAFR
GIGKSFITCA FVVWSLWRDP QLKILIVSAS KERADANSIF IKNIIDLLPF LSELKPRPGQ
RDSVISFDVG PANPDHSPSV KSVGITGQLT GSRADIIIAD DVEIPSNSAT MGAREKLWTL
VQEFAALLKP LPSSRVIYLG TPQTEMTLYK ELEDNRGYTT IIWPALYPRT REENLYYSQR
LAPMLRAEYD ENPEALAGTP TDPVRFDRDD LRERELEYGK AGFTLQFMLN PNLSDAEKYP
LRLRDAIVAA LDLEKAPMHY QWLPNRQNII EDLPNVGLKG DDLHTYHDCS NNSGQYQQKI
LVIDPSGRGK DETGYAVLYT LNGYIYLMEA GGFRDGYSDK TLELLAKKAK QWGVQTVVYE
SNFGDGMFGK VFSPILLKHH NCAMEEIRAR GMKEMRICDT LEPVMQTHRL VIRDEVIRAD
YQSARDVDGK HDVKYSLFYQ MTRITREKGA LAHDDRLDAL ALGIEYLRES MQLDSVKVEG
EVLADFLEEH MMRPTVAATH IIEMSVGGVD VYSEDDEGYG TSFIEW
