TERL_BPT5
ID TERL_BPT5 Reviewed; 438 AA.
AC Q6QGD2; Q66LR2;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 71.
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 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:16377618};
GN ORFNames=ORF144 {ECO:0000312|EMBL:AAX12081.1},
GN T5.155 {ECO:0000312|EMBL:AAS77194.1}, T5p151 {ECO:0000312|EMBL:AAU05290.1};
OS Escherichia phage T5 (Enterobacteria phage T5).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Demerecviridae; Markadamsvirinae; Tequintavirus.
OX NCBI_TaxID=2695836;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ksenzenko V.N., Kaliman A.V., Krutilina A.I., Shlyapnikov M.G.;
RT "Bacteriophage T5 complete genome.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC STRAIN=ATCC 11303-B5 {ECO:0000312|EMBL:AAX12081.1};
RX PubMed=15661140; DOI=10.1016/j.virol.2004.10.049;
RA Wang J., Jiang Y., Vincent M., Sun Y., Yu H., Wang J., Bao Q., Kong H.,
RA Hu S.;
RT "Complete genome sequence of bacteriophage T5.";
RL Virology 332:45-65(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=St0 deletion mutant;
RX PubMed=24198424; DOI=10.1128/jvi.02262-13;
RA Zivanovic Y., Confalonieri F., Ponchon L., Lurz R., Chami M., Flayhan A.,
RA Renouard M., Huet A., Decottignies P., Davidson A.R., Breyton C.,
RA Boulanger P.;
RT "Insights into bacteriophage T5 structure from analysis of its
RT morphogenesis genes and protein components.";
RL J. Virol. 88:1162-1174(2014).
RN [4]
RP CATALYTIC ACTIVITY, ACTIVE SITE, AND MUTAGENESIS OF ASP-286; ASP-342 AND
RP ASP-425.
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).
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04146,
CC ECO:0000305|PubMed:16377618};
CC Note=ATPase activity requires 1 Mg(2+) ion per subunit. Nuclease
CC activity probably requires 2 Mg(2+) ions per subunit.
CC {ECO:0000255|HAMAP-Rule:MF_04146, ECO:0000305|PubMed:16377618};
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 -!- INDUCTION: Expressed in the late phase of the viral replicative cycle.
CC {ECO:0000305|PubMed:15661140}.
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; AY543070; AAS77194.1; -; Genomic_DNA.
DR EMBL; AY692264; AAU05290.1; -; Genomic_DNA.
DR EMBL; AY587007; AAX12081.1; -; Genomic_DNA.
DR RefSeq; YP_006983.1; NC_005859.1.
DR SMR; Q6QGD2; -.
DR GeneID; 2777679; -.
DR KEGG; vg:2777679; -.
DR Proteomes; UP000002107; Genome.
DR Proteomes; UP000002141; Genome.
DR Proteomes; UP000002503; 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:0004518; F:nuclease activity; IDA:UniProtKB.
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.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
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..438
FT /note="Terminase, large subunit"
FT /id="PRO_0000434542"
FT MOTIF 62..68
FT /note="Walker A motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146,
FT ECO:0000305|PubMed:16377618"
FT MOTIF 150..155
FT /note="Walker B motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146,
FT ECO:0000305|PubMed:16377618"
FT ACT_SITE 155
FT /note="For ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04146"
FT BINDING 286
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_04146,
FT ECO:0000305|PubMed:16377618"
FT BINDING 286
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_04146,
FT ECO:0000305|PubMed:16377618"
FT BINDING 342
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_04146,
FT ECO:0000305|PubMed:16377618"
FT BINDING 418
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_04146,
FT ECO:0000305|PubMed:16377618"
FT MUTAGEN 286
FT /note="D->N: 50% loss of endonuclease activity."
FT /evidence="ECO:0000269|PubMed:16377618"
FT MUTAGEN 342
FT /note="D->N: Almost complete loss of endonuclease
FT activity."
FT /evidence="ECO:0000269|PubMed:16377618"
FT MUTAGEN 425
FT /note="D->N: 50% loss of endonuclease activity."
FT /evidence="ECO:0000269|PubMed:16377618"
FT CONFLICT 260
FT /note="I -> T (in Ref. 3; AAU05290)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 438 AA; 49717 MW; 2BF5B121DEC69102 CRC64;
MEVSRPYVNT VDVIDFGIDK RFFRLPVSGI LAQEGITPNG PQIAIINALE DPRHRFVTAC
VSRRVGKSFI AYTLGFLKLL EPNVKVLVVA PNYSLANIGW SQIRGLIKKY GLQTERENAK
DKEIELANGS LFKLASAAQA DSAVGRSYDF IIFDEAAISD VGGDAFRVQL RPTLDKPNSK
ALFISTPRGG NWFKEFYAYG FDDTLPNWVS IHGTYRDNPR ADLNDIEEAR RTVSKNYFRQ
EYEADFSVFE GQIFDTFNAI DHVKDLKGMR HFFKDDEAFE TLLGIDVGYR DPTAVLTIKY
HYDTDTYYVL EEYQQAEKTT AQHAAYIQHC IDRYKVDRIF VDSAAAQFRQ DLAYEHEIAS
APAKKSVLDG LACLQALFQQ GKIIVDASCS SLIHALQNYK WDFQEGEEKL SREKPRHDAN
SHLCDALRYG IYSISRGK
