HELIC_BPT3
ID HELIC_BPT3 Reviewed; 566 AA.
AC P20315;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=DNA helicase/primase {ECO:0000255|HAMAP-Rule:MF_04154};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_04154};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_04154};
DE AltName: Full=Gene product 4;
DE Short=Gp4;
GN Name=4;
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], AND ALTERNATIVE INITIATION.
RC STRAIN=Luria;
RX PubMed=2614843; DOI=10.1016/0022-2836(89)90102-2;
RA Beck P.J., Gonzalez S., Ward C.L., Molineux I.J.;
RT "Sequence of bacteriophage T3 DNA from gene 2.5 through gene 9.";
RL J. Mol. Biol. 210:687-701(1989).
CC -!- FUNCTION: ATP-dependent DNA helicase and primase essential for viral
CC DNA replication and recombination. The helicase moves 5' -> 3' on the
CC lagging strand template, unwinding the DNA duplex ahead of the leading
CC strand polymerase at the replication fork and generating ssDNA for both
CC leading and lagging strand synthesis. ATP or dTTP hydrolysis propels
CC each helicase domain to translocate sequentially along DNA. Mediates
CC strand transfer when a joint molecule is available and participates in
CC recombinational DNA repair through its role in strand exchange. Primase
CC activity synthesizes short RNA primers at the sequence 5'-GTC-3' on the
CC lagging strand that the polymerase elongates using dNTPs and providing
CC the primase is still present. {ECO:0000255|HAMAP-Rule:MF_04154}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04154};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04154};
CC Note=Binds 2 Mg(2+), one of which is catalytic. {ECO:0000255|HAMAP-
CC Rule:MF_04154};
CC -!- SUBUNIT: Homohexamer. Assembles as a hexamer onto linear or circular
CC ssDNA in the presence of ATP or dTTP. Interacts (via C-terminus) with
CC the viral DNA polymerase that is bound to DNA; this interaction is
CC essential to initiate leading-strand DNA synthesis. The priming complex
CC consists of 2 DNA polymerases and 1 helicase-primase hexamer that
CC assemble on the DNA template. Interacts with the single-stranded DNA-
CC binding protein. Part of the replicase complex that includes the DNA
CC polymerase, the primase/helicase and the single-stranded DNA binding
CC protein. {ECO:0000255|HAMAP-Rule:MF_04154}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Comment=Isoform 4A contains the primase/helicase region, whereas
CC isoform 4B contains only the helicase region.
CC {ECO:0000250|UniProtKB:P03692};
CC Name=4A;
CC IsoId=P20315-1; Sequence=Displayed;
CC Name=4B;
CC IsoId=P20315-2; Sequence=VSP_018682;
CC -!- DOMAIN: The N-terminus zinc finger domain is essential for delivering
CC the primed DNA template to the DNA polymerase. The central core domain
CC contains the primase activity. The C-terminus region is responsible for
CC the helicase activity and binds 1 Mg(2+)-dTTP. {ECO:0000255|HAMAP-
CC Rule:MF_04154}.
CC -!- SIMILARITY: Belongs to the Teseptimavirus DNA helicase/primase family.
CC {ECO:0000255|HAMAP-Rule:MF_04154}.
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DR EMBL; X17255; CAA35135.1; -; Genomic_DNA.
DR EMBL; X17255; CAA35136.1; -; Genomic_DNA.
DR PIR; S07508; S07508.
DR RefSeq; NP_523315.1; NC_003298.1. [P20315-1]
DR RefSeq; NP_523316.1; NC_003298.1. [P20315-2]
DR SMR; P20315; -.
DR GeneID; 927429; -.
DR GeneID; 927458; -.
DR KEGG; vg:927429; -.
DR KEGG; vg:927458; -.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003896; F:DNA primase activity; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR CDD; cd01029; TOPRIM_primases; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_04154; Helic_Prim_T7; 1.
DR InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR InterPro; IPR046394; Helic_Prim_T7.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013237; Phage_T7_Gp4_N.
DR InterPro; IPR034154; TOPRIM_DnaG/twinkle.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR027032; Twinkle-like.
DR PANTHER; PTHR12873; PTHR12873; 1.
DR Pfam; PF03796; DnaB_C; 1.
DR SMART; SM00778; Prim_Zn_Ribbon; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51199; SF4_HELICASE; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW Alternative initiation; ATP-binding; DNA replication; DNA-binding;
KW DNA-directed RNA polymerase; Helicase; Hydrolase; Late protein; Magnesium;
KW Metal-binding; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; Primosome; Transcription; Transferase;
KW Viral DNA replication; Zinc; Zinc-finger.
FT CHAIN 1..566
FT /note="DNA helicase/primase"
FT /id="PRO_0000003353"
FT DOMAIN 150..237
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT DOMAIN 280..547
FT /note="SF4 helicase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154"
FT ZN_FING 15..37
FT /note="C4-like; zinc ribbon fold"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154"
FT REGION 542..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..566
FT /note="Binding to viral DNA polymerase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154"
FT BINDING 18
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154"
FT BINDING 156
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154"
FT BINDING 206
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154"
FT BINDING 311..318
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154"
FT SITE 360
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154"
FT SITE 464
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154"
FT SITE 503
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154"
FT SITE 521
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154"
FT SITE 534
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154"
FT VAR_SEQ 1..62
FT /note="Missing (in isoform 4B)"
FT /evidence="ECO:0000305"
FT /id="VSP_018682"
SQ SEQUENCE 566 AA; 62741 MW; 7553913C43DDFEBE CRC64;
MEREDDSIFL FHAPCENCGS SDGNSVYSDG HEWCFVCEHR VPANEEREAK LSTRRRTGGS
KPMSYDVWNF GDSNGRYSDL TARGISKETC QKAGYWLAKV DNRMYQVADY RDQNGSIVSQ
KVRDKDKNFK TTGSHKSDAL FLKHLWSGGK KIVVTEGEID ALTVMELQDC KYPVVSLGHG
ASAAKKTCAA NYEYFDQFEQ IILMFDMDDA GRKAVEEAAQ VLPAGKVRVA VLPCKDANEC
HIMGEDKAIL EQVWNANPWV PDGVVSALSL KDRVKEAMTS EDAVGLLFDG CQGLNDRTLG
ARGGEVVMVT SGSGMGKSTF VRQQALAWGK RMGKRVGLAM LEESVEDTIQ DMMGLNNKVR
LRQSDEVKKA IAEDGRFDEW YDELFGDDTF HLYDSFAEAE ADRLLAKLAY MRTGLGCDVI
VLDHISIVVS ASEESDERKM IDRLMTKLKG FAKSTGVVLV VICHLKNPEK GKAHEEGRAV
SITDLRGSGA LRQLSDTIIA LERNQQGDMP NLVLVRLLKC RFTGDTGIAG YMEYNRETGW
LEPSSYTGGE GEGDTGWTEQ DGQSDF
