TERL_BPG20
ID TERL_BPG20 Reviewed; 485 AA.
AC A0A1L4BKS3; A0A1L1QK41; A0A1L1QK45;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Terminase, large subunit {ECO:0000255|HAMAP-Rule:MF_04146};
DE AltName: Full=DNA-packaging protein {ECO:0000255|HAMAP-Rule:MF_04146};
DE AltName: Full=DNA-packaging protein gp80 {ECO:0000305};
DE AltName: Full=Gene product 80 {ECO:0000305};
DE Short=gp80 {ECO:0000305};
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:0000255|HAMAP-Rule:MF_04146, ECO:0000305|PubMed:28100693};
GN ORFNames=G20c_80 {ECO:0000312|EMBL:API81888.1};
OS Thermus phage G20c (Thermus thermophilus phage G20c).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae; Oshimavirus; unclassified Oshimavirus.
OX NCBI_TaxID=1406341;
OH NCBI_TaxID=274; Thermus thermophilus.
RN [1] {ECO:0000312|PDB:5M1K, ECO:0000312|PDB:5M1N, ECO:0000312|PDB:5M1O, ECO:0000312|PDB:5M1Q, ECO:0007744|PDB:5M1F}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (1.20
RP ANGSTROMS) OF 257-443 IN COMPLEX WITH MAGNESIUM AND OTHER IONS, CATALYTIC
RP ACTIVITY, COFACTOR, MUTAGENESIS OF ASP-294; ASP-300; ASP-347; HIS-427;
RP ASP-428 AND ASP-429, AND FUNCTION.
RX PubMed=28100693; DOI=10.1093/nar/gkw1354;
RA Xu R.G., Jenkins H.T., Chechik M., Blagova E.V., Lopatina A., Klimuk E.,
RA Minakhin L., Severinov K., Greive S.J., Antson A.A.;
RT "Viral genome packaging terminase cleaves DNA using the canonical RuvC-like
RT two-metal catalysis mechanism.";
RL Nucleic Acids Res. 45:3580-3590(2017).
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:28100693}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:28100693};
CC Note=Nuclease activity requires 2 Mg(2+) ions per subunit
CC (PubMed:28100693). Also active in the presence of Mn(2+) or Co(2+) but
CC inactive with Ni(2+), Zn(2+) or Ca(2+) (PubMed:28100693). Cu(2+),
CC Cd(2+) and Cs(2+) do not support catalysis (PubMed:28100693).
CC {ECO:0000269|PubMed:28100693};
CC -!- SUBUNIT: Interacts with the terminase small subunit; the active complex
CC is probably heterooligomeric. Interacts with the portal protein.
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; KX987127; API81888.1; -; Genomic_DNA.
DR PDB; 5M1F; X-ray; 2.15 A; A=257-443.
DR PDB; 5M1K; X-ray; 1.20 A; A/B=1-191.
DR PDB; 5M1N; X-ray; 1.20 A; A/B=1-191.
DR PDB; 5M1O; X-ray; 1.60 A; A/B=1-191.
DR PDB; 5M1P; X-ray; 1.10 A; A/B=1-191.
DR PDB; 5M1Q; X-ray; 1.45 A; A=1-187.
DR PDBsum; 5M1F; -.
DR PDBsum; 5M1K; -.
DR PDBsum; 5M1N; -.
DR PDBsum; 5M1O; -.
DR PDBsum; 5M1P; -.
DR PDBsum; 5M1Q; -.
DR SMR; A0A1L4BKS3; -.
DR Proteomes; UP000223104; 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 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..485
FT /note="Terminase, large subunit"
FT /id="PRO_0000447195"
FT REGION 256..438
FT /note="Nuclease"
FT /evidence="ECO:0000250|UniProtKB:P17312"
FT MOTIF 124..131
FT /note="Walker A motif"
FT /evidence="ECO:0000250|UniProtKB:P17312"
FT MOTIF 145..150
FT /note="Walker B motif"
FT /evidence="ECO:0000250|UniProtKB:P17312"
FT ACT_SITE 150
FT /note="For ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146"
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:0000269|PubMed:28100693"
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:0000269|PubMed:28100693"
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:0000269|PubMed:28100693"
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:0000269|PubMed:28100693"
FT SITE 300
FT /note="Modulates nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146"
FT SITE 428
FT /note="Possible stabilization of Magnesium 1"
FT /evidence="ECO:0000269|PubMed:28100693"
FT MUTAGEN 294
FT /note="D->N: Complete loss of nuclease activity."
FT /evidence="ECO:0000269|PubMed:28100693"
FT MUTAGEN 300
FT /note="D->N: No effect on nuclease activity."
FT /evidence="ECO:0000269|PubMed:28100693"
FT MUTAGEN 347
FT /note="D->N: Complete loss of nuclease activity."
FT /evidence="ECO:0000269|PubMed:28100693"
FT MUTAGEN 427
FT /note="H->N: Reduced nuclease activity."
FT /evidence="ECO:0000269|PubMed:28100693"
FT MUTAGEN 428
FT /note="D->N: Reduced nuclease activity."
FT /evidence="ECO:0000269|PubMed:28100693"
FT MUTAGEN 429
FT /note="D->N: Almost complete loss of nuclease activity."
FT /evidence="ECO:0000269|PubMed:28100693"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:5M1P"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:5M1P"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:5M1P"
FT STRAND 277..280
FT /evidence="ECO:0007829|PDB:5M1P"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:5M1P"
FT STRAND 298..308
FT /evidence="ECO:0007829|PDB:5M1P"
FT TURN 309..312
FT /evidence="ECO:0007829|PDB:5M1P"
FT STRAND 313..322
FT /evidence="ECO:0007829|PDB:5M1P"
FT HELIX 325..338
FT /evidence="ECO:0007829|PDB:5M1P"
FT STRAND 343..346
FT /evidence="ECO:0007829|PDB:5M1P"
FT HELIX 353..361
FT /evidence="ECO:0007829|PDB:5M1P"
FT STRAND 366..368
FT /evidence="ECO:0007829|PDB:5M1P"
FT HELIX 374..389
FT /evidence="ECO:0007829|PDB:5M1P"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:5M1P"
FT HELIX 399..406
FT /evidence="ECO:0007829|PDB:5M1P"
FT STRAND 408..412
FT /evidence="ECO:0007829|PDB:5M1P"
FT STRAND 418..423
FT /evidence="ECO:0007829|PDB:5M1P"
FT HELIX 429..438
FT /evidence="ECO:0007829|PDB:5M1P"
SQ SEQUENCE 485 AA; 55156 MW; 972DE31605B492C2 CRC64;
MKRLRPSDKF FELLGYKPHH VQLAIHRSTA KRRVACLGRQ SGKSEAASVE AVFELFARPG
SQGWIIAPTY DQAEIIFGRV VEKVERLSEV FPTTEVQLQR RRLRLLVHHY DRPVNAPGAK
RVATSEFRGK SADRPDNLRG ATLDFVILDE AAMIPFSVWS EAIEPTLSVR DGWALIISTP
KGLNWFYEFF LMGWRGGLKE GIPNSGINQT HPDFESFHAA SWDVWPERRE WYMERRLYIP
DLEFRQEYGA EFVSHSNSVF SGLDMLILLP YERRGTRLVV EDYRPDHIYC IGADFGKNQD
YSVFSVLDLD TGAIACLERM NGATWSDQVA RLKALSEDYG HAYVVADTWG VGDAIAEELD
AQGINYTPLP VKSSSVKEQL ISNLALLMEK GQVAVPNDKT ILDELRNFRY YRTASGNQVM
RAYGRGHDDI VMSLALAYSQ YEGKDGYKFE LAEERPSKLK HEESVMSLVE DDFTDLELAN
RAFSA
