ID W6PE46_9CAUD Unreviewed; 567 AA.
AC W6PE46;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=DNA helicase/primase {ECO:0000256|HAMAP-Rule:MF_04154};
DE EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_04154};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_04154};
GN Name=gp4 {ECO:0000313|EMBL:CDM12543.1};
OS Cronobacter phage Dev2.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Autographiviridae; Studiervirinae; Kayfunavirus; Kayfunavirus Dev2.
OX NCBI_TaxID=1410331 {ECO:0000313|EMBL:CDM12543.1, ECO:0000313|Proteomes:UP000019163};
RN [1] {ECO:0000313|EMBL:CDM12543.1, ECO:0000313|Proteomes:UP000019163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=25023334; DOI=10.1007/s00705-014-2173-5;
RA Kajsik M., Oslanecova L., Szemes T., Hyblova M., Bilkova A., Drahovska H.,
RA Turna J.;
RT "Characterization and genome sequence of Dev2, a new T7-like bacteriophage
RT infecting Cronobacter turicensis.";
RL Arch. Virol. 159:3013-3019(2014).
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:0000256|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:0000256|HAMAP-Rule:MF_04154};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_04154};
CC Note=Binds 2 Mg(2+), one of which is catalytic. {ECO:0000256|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:0000256|HAMAP-Rule:MF_04154}.
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:0000256|HAMAP-
CC Rule:MF_04154}.
CC -!- SIMILARITY: Belongs to the Teseptimavirus DNA helicase/primase family.
CC {ECO:0000256|HAMAP-Rule:MF_04154}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04154}.
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DR EMBL; HG813241; CDM12543.1; -; Genomic_DNA.
DR RefSeq; YP_009005129.1; NC_023558.1.
DR GeneID; 19619615; -.
DR KEGG; vg:19619615; -.
DR OrthoDB; 615at10239; -.
DR Proteomes; UP000019163; Genome.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-UniRule.
DR CDD; cd19483; RecA-like_Gp4D_helicase; 1.
DR CDD; cd01029; TOPRIM_primases; 1.
DR Gene3D; 2.20.25.10; -; 1.
DR Gene3D; 2.20.25.180; -; 1.
DR Gene3D; 3.40.1360.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_04154; Helic_Prim_T7; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR InterPro; IPR048774; Helic-prim_T7_N.
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; T7-LIKE MITOCHONDRIAL DNA HELICASE; 1.
DR PANTHER; PTHR12873:SF0; TWINKLE MTDNA HELICASE; 1.
DR Pfam; PF03796; DnaB_C; 1.
DR Pfam; PF21268; Helic-prim_T7_N; 1.
DR Pfam; PF13155; Toprim_2; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00778; Prim_Zn_Ribbon; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56731; DNA primase core; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS51199; SF4_HELICASE; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_04154};
KW DNA replication {ECO:0000256|HAMAP-Rule:MF_04154};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_04154, ECO:0000313|EMBL:CDM12543.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04154};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_04154};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_04154};
KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_04154};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04154};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_04154};
KW Primosome {ECO:0000256|HAMAP-Rule:MF_04154};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_04154};
KW Viral DNA replication {ECO:0000256|HAMAP-Rule:MF_04154};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_04154};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_04154}.
FT DOMAIN 153..245
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 284..551
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT ZN_FING 19..41
FT /note="C4-like; zinc ribbon fold"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 209
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 315..322
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 363
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 468
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 507
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 525
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 538
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
SQ SEQUENCE 567 AA; 62656 MW; 8942C495E0822764 CRC64;
MSYEDQERDD SVFLYHTECP DCGSSDANGV YSDGHMYCFA CDPSVAWKKG DMELTEGYTP
SGGKKQVSNL LTWGENSGRY VPLPARGLSA DICKKYSYWV GMMQGKMVQI ADYYDRSGTK
VGQKVRDADK NFTAIGSVKN DLLFGSQLWS GGKKIVITEG EIDCLSVAQV QDGKYPVVSL
PLGAKSAKKT LAANLEYLDQ FEEIILMFDM DEPGREAVEQ AAPVLPAGKV KVAFINGYKD
ANAALQAKDF RAIQDAIWNA KPFVPAGVVS AKSLKDRTRE AMLKAETEGL LFSSCTTLNA
MTLGARSGEL IMVTSGSGMG KSTFVRQLLL EWGRQGKRVG MAMLEEAVEE TVQDLIGLDN
NVRLRQSKEL KEAILKDGRF DEWYDKLFND DKFHLYDSFA ESEEDTLFAK LGYMVDGLDC
DVILLDHISI VVSGMEDNSD ERKTIDRIMT RLKKFAKTKG VVVVVICHLK NPEKGKSHEE
GRPVSITDLR GSGALRQLSD TIIALERNQQ GDTPNVVQLR LLKCRFTGDT GIAGHLEYNK
LTGWLEPIVL TGGSGEEDSG SWEDQDF
//
