ID A0A5Q2W6A3_9CAUD Unreviewed; 504 AA. AC A0A5Q2W6A3; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 27-NOV-2024, entry version 19. 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}; OS Klebsiella phage 31. OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Autographiviridae; Studiervirinae; Teetrevirus. OX NCBI_TaxID=2601667 {ECO:0000313|EMBL:QGH73732.1, ECO:0000313|Proteomes:UP000358020}; RN [1] {ECO:0000313|EMBL:QGH73732.1, ECO:0000313|Proteomes:UP000358020} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Tan D.; RT "Characterization of Lytic Phages of Klebsiella pneumoniae and Its RT Application of Phage Therapy."; RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases. 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 + phosphate + H(+); 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 central core domain contains the primase activity. The C- CC terminus is responsible for the helicase activity. {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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MN149904; QGH73732.1; -; Genomic_DNA. DR Proteomes; UP000358020; Genome. DR GO; GO:1990077; C:primosome 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-UniRule. DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro. 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; 2.20.25.180; -; 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; 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; IPR034154; TOPRIM_DnaG/twinkle. DR InterPro; IPR006171; TOPRIM_dom. 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; SM00493; TOPRIM; 1. DR SUPFAM; SSF56731; DNA primase core; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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}; 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 Reference proteome {ECO:0000313|Proteomes:UP000358020}; 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 88..175 FT /note="Toprim" FT /evidence="ECO:0000259|PROSITE:PS50880" FT DOMAIN 218..485 FT /note="SF4 helicase" FT /evidence="ECO:0000259|PROSITE:PS51199" FT REGION 480..504 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 94 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 144 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 174 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154" FT BINDING 249..256 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154" FT SITE 298 FT /note="dTTP/dATP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154" FT SITE 402 FT /note="dTTP/dATP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154" FT SITE 441 FT /note="dTTP/dATP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154" FT SITE 459 FT /note="dTTP/dATP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154" FT SITE 472 FT /note="dTTP/dATP binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154" SQ SEQUENCE 504 AA; 55899 MW; 18CA0EA0E87F9D91 CRC64; MSYDVWNFGD SNGRYSDLTA RGISKETCQK AGYWLAKVDN RMYQVADYRD QNGSIVSQKV RDKDKNFKTT GSHKSDALFL KHLWSGGKKI VVTEGEIDAL TVMELQDCKY PVVSLGHGAS AAKKTCAANY EYFDQFEQII LMFDMDDAGR KAVEEAAQVL PAGKVRVAVL PYKDANECHL MGEDKAILEQ VWNANPWVPD GVVSALSLKD RVKEAMTSED AVGLLFDGCQ GLNDRTLGAR GGEVVMVTSG SGMGKSTFVR QQALAWGKRM GKRVGLAMLE ESVEDTIQDM MGLNNKVRLR QSDEVKKAIA EDGRFDEWYD ELFGDDTFHL YDSFAEAEAD RLLAKLAYMR TGLGCDVIVL DHISIVVSAS EESDERKMID RLMTKLKGFA KSTGVVLVVI CHLKNPEKGK PHEEGRAVSI TDLRGSGALR QLSDTIIALE RNQQGDMPNL VLVRLLKCRF TGDTGIAGYM EYNRETGWLE PSSYTGEEGE GDTGWTEQEG QSDF //