TERL_BP234
ID TERL_BP234 Reviewed; 485 AA.
AC A7XXB7;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Terminase, large subunit {ECO:0000255|HAMAP-Rule:MF_04146, ECO:0000303|PubMed:30737287};
DE AltName: Full=DNA-packaging protein {ECO:0000255|HAMAP-Rule:MF_04146};
DE AltName: Full=Gene product 85 {ECO:0000305};
DE Short=gp85 {ECO:0000303|PubMed:30737287};
DE Includes:
DE RecName: Full=ATPase {ECO:0000255|HAMAP-Rule:MF_04146};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_04146};
DE Includes:
DE RecName: Full=Endonuclease {ECO:0000255|HAMAP-Rule:MF_04146};
DE EC=3.1.21.- {ECO:0000250|UniProtKB:A0A1L4BKS3, ECO:0000255|HAMAP-Rule:MF_04146};
GN ORFNames=P23p85 {ECO:0000312|EMBL:ABU96918.1};
OS Thermus virus P23-45 (Thermus thermophilus phage P23-45).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Oshimavirus.
OX NCBI_TaxID=466051;
OH NCBI_TaxID=274; Thermus thermophilus.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=18355836; DOI=10.1016/j.jmb.2008.02.018;
RA Minakhin L., Goel M., Berdygulova Z., Ramanculov E., Florens L., Glazko G.,
RA Karamychev V.N., Slesarev A.I., Kozyavkin S.A., Khromov I., Ackermann H.W.,
RA Washburn M., Mushegian A., Severinov K.;
RT "Genome comparison and proteomic characterization of Thermus thermophilus
RT bacteriophages P23-45 and P74-26: siphoviruses with triplex-forming
RT sequences and the longest known tails.";
RL J. Mol. Biol. 378:468-480(2008).
RN [2]
RP FUNCTION.
RX PubMed=30737287; DOI=10.1073/pnas.1813204116;
RA Bayfield O.W., Klimuk E., Winkler D.C., Hesketh E.L., Chechik M., Cheng N.,
RA Dykeman E.C., Minakhin L., Ranson N.A., Severinov K., Steven A.C.,
RA Antson A.A.;
RT "Cryo-EM structure and in vitro DNA packaging of a thermophilic virus with
RT supersized T=7 capsids.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:3556-3561(2019).
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 to initiate and to end a
CC packaging reaction The terminase lies at a unique vertex of the
CC procapsid and is composed of two subunits, a small terminase subunit
CC involved in viral DNA recognition (packaging sequence), and a large
CC terminase subunit possessing endonucleolytic and ATPase activities.
CC Both terminase subunits heterooligomerize and are docked on the portal
CC protein to form the packaging machine. The terminase large subunit
CC exhibits endonuclease activity and cleaves the viral genome concatemer.
CC Once the capsid is packaged with the DNA, the terminase complex is
CC substituted by the tail. {ECO:0000255|HAMAP-Rule:MF_04146,
CC ECO:0000305|PubMed:30737287}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1L4BKS3};
CC Note=Nuclease activity requires 2 Mg(2+) ions per subunit (By
CC similarity). Also active in the presence of Mn(2+) or Co(2+) (By
CC similarity). {ECO:0000250|UniProtKB:A0A1L4BKS3};
CC -!- SUBUNIT: Interacts with the terminase small subunit; the active complex
CC is composed of a pentamer of terminase large subunits and a dodecamer
CC of terminase small subunits (By similarity). Interacts with the portal
CC protein (By similarity). {ECO:0000250|UniProtKB:A7XXR1,
CC ECO:0000255|HAMAP-Rule:MF_04146}.
CC -!- DOMAIN: The N-terminus contains an ATPase domain. The C-terminus
CC contains an endonuclease domain. {ECO:0000255|HAMAP-Rule:MF_04146}.
CC -!- SIMILARITY: Belongs to the Tequatrovirus large terminase family.
CC {ECO:0000255|HAMAP-Rule:MF_04146}.
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DR EMBL; EU100883; ABU96918.1; -; Genomic_DNA.
DR RefSeq; YP_001467938.1; NC_009803.1.
DR SMR; A7XXB7; -.
DR GeneID; 5600506; -.
DR KEGG; vg:5600506; -.
DR Proteomes; UP000001132; 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_04146; TERL_T4; 1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035421; Terminase_6C.
DR InterPro; IPR044267; Terminase_large_su_gp17-like.
DR Pfam; PF17289; Terminase_6C; 1.
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..485
FT /note="Terminase, large subunit"
FT /id="PRO_0000447194"
FT REGION 22..197
FT /note="ATPase activity"
FT /evidence="ECO:0000250|UniProtKB:P17312"
FT REGION 256..438
FT /note="Nuclease"
FT /evidence="ECO:0000250|UniProtKB:P17312"
FT MOTIF 125..131
FT /note="Walker A motif"
FT /evidence="ECO:0000250|UniProtKB:P17312"
FT MOTIF 145..150
FT /note="Walker B motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146"
FT ACT_SITE 150
FT /note="For ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146"
FT BINDING 17..22
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:A7XXR1"
FT BINDING 40..45
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:A7XXR1"
FT BINDING 79
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:A7XXR1"
FT BINDING 97
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P17312"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P17312"
FT BINDING 294
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 294
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 347
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 429
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 SITE 300
FT /note="Modulates nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146"
SQ SEQUENCE 485 AA; 55124 MW; 65C19106BC817A39 CRC64;
MKRLRPSDKF FELLGYKPHH VQLAIHRSTA KRRVACLGRQ SGKSEAASVE AVFELFARPG
SQGWIIAPTY DQAEIIFGRV VEKVERLAEV FPATEVQLQR RRLRLLVHHY DRPVNAPGAK
RVATSEFRGK SADRPDNLRG ATLDFVILDE AAMIPFSVWS EAIEPTLSVR DGWALIISTP
KGLNWFYEFF LMGWRGGLKE GIPNSGVNQT HPDFESFHAA SWDVWPERRE WYMERRLYIP
DLEFRQEYGA EFVSHSNSVF SGLDMLILLP YERRGTRLVV EDYRPDHIYC IGADFGKNQD
YSVFSVLDLD TGAIVCLERM NGATWSDQVA RLKALSEDYG HAYVVADTWG VGDAIAEELD
AQGINYTPLP VKSSSVKEQL ISNLALLMEK GQVAVPNDKT ILDELRNFRY YRTASGNQVM
RAYGRGHDDI VMSLALAYSQ YEGKDGYKFE LAEERPSKLK HEESVMSLVE DDFTDLELAN
RAFSA
