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Database: UniProt
Entry: Q3YJY4_BPK1F
LinkDB: Q3YJY4_BPK1F
Original site: Q3YJY4_BPK1F 
ID   Q3YJY4_BPK1F            Unreviewed;       586 AA.
AC   Q3YJY4;
DT   27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2005, sequence version 1.
DT   24-JAN-2024, entry version 97.
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=4.0 {ECO:0000313|EMBL:AAZ72981.1};
OS   Escherichia phage K1F (Bacteriophage K1F).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Autographiviridae; Studiervirinae; Kayfunavirus; Kayfunavirus K1F.
OX   NCBI_TaxID=344021 {ECO:0000313|EMBL:AAZ72981.1, ECO:0000313|Proteomes:UP000001530};
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1] {ECO:0000313|EMBL:AAZ72981.1, ECO:0000313|Proteomes:UP000001530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16321955; DOI=10.1128/JB.187.24.8499-8503.2005;
RA   Scholl D., Merril C.;
RT   "The genome of bacteriophage K1F, a T7-like phage that has acquired the
RT   ability to replicate on K1 strains of Escherichia coli.";
RL   J. Bacteriol. 187:8499-8503(2005).
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; DQ111067; AAZ72981.1; -; Genomic_DNA.
DR   RefSeq; YP_338107.1; NC_007456.1.
DR   GeneID; 3707724; -.
DR   KEGG; vg:3707724; -.
DR   OrthoDB; 615at10239; -.
DR   Proteomes; UP000001530; 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 PROTEIN, MITOCHONDRIAL; 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.
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:AAZ72981.1};
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   ECO:0000313|EMBL:AAZ72981.1};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_04154};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_04154};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001530};
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          283..550
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
FT   ZN_FING         18..40
FT                   /note="C4-like; zinc ribbon fold"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT   BINDING         21
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT   BINDING         37
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT   BINDING         40
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT   BINDING         158
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         208
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         239
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT   BINDING         314..321
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT   SITE            362
FT                   /note="dTTP/dATP binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT   SITE            467
FT                   /note="dTTP/dATP binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT   SITE            506
FT                   /note="dTTP/dATP binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT   SITE            524
FT                   /note="dTTP/dATP binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT   SITE            537
FT                   /note="dTTP/dATP binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
SQ   SEQUENCE   586 AA;  64248 MW;  94B46EF91D4A1217 CRC64;
     MSYDDQDDES VFLYHTQCPD CGSSDANGVY SDGHQFCFAC DPSVAWKKGD MELTEGYTPS
     GGRKQVSNLL TFGENAGRYV PLPARSLSME ICKKYSYWVG NMGGKMVQVA DYYDRSGTKV
     GQKVRDAEKN FTAIGSVKSD MLFGSQLWNG GKKIVITEGE IDALSVAQVQ DGKYPVVSLP
     LGAKSAKKAM AANLEYLDQF EEIILMFDMD EPGRQAIEDA APVLPAGRVK VAFINGYKDA
     NAALQAKDFK AITDAIWNAK PFVPAGVVSA ASLKDRTREA MLKAETEGLM FSSCTTLNAM
     TLGARAGELI MVTSGSGMGK STFVRQLLLE WGRGGKRVGM AMLEEAVEET VQDLMGLDNN
     VRLRQSKELK QAILEDGRFD EWYDKLFGDD KFHLYDSFAE SEEDTLFAKL AYMVDGLDCD
     VILLDHISIV VSGMEDNSDE RKTIDRIMTR LKKFAKTKGV VVVVICHLKN PEKGKSHEEG
     RPVSITDLRG SGALRQLSDT ILALERNQQG DTPNVVQLRL LKCRFTGDTG VAGHLEYNKT
     TGWLEPISFT SSSGEEDSGS WENNGLLNVN ALSATGSHHT EDTISV
//
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