ID A0A159B7V9_9CAUD Unreviewed; 479 AA.
AC A0A159B7V9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 08-NOV-2023, entry version 23.
DE RecName: Full=DnaB-like replicative helicase {ECO:0000256|HAMAP-Rule:MF_04155};
DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_04155};
GN ORFNames=PKO111_109 {ECO:0000313|EMBL:AKJ73164.1};
OS Klebsiella phage PKO111.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Straboviridae; Tevenvirinae; Jiaodavirus; Jiaodavirus pko111.
OX NCBI_TaxID=1654928 {ECO:0000313|EMBL:AKJ73164.1, ECO:0000313|Proteomes:UP000202948};
RN [1] {ECO:0000313|EMBL:AKJ73164.1, ECO:0000313|Proteomes:UP000202948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lee J.-H., Park E.-A., Lee D.-H.;
RT "Complete Genome Sequence of K. oxytoca Bacteriophage PKO111.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent DNA helicase essential for viral DNA
CC 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. Interaction with the primase
CC allows the primase to initiate lagging strand synthesis and fully
CC activates the helicase. Loaded by the helicase assembly factor on
CC replication forks that begin at discrete replication origin sequences,
CC as well as on forks that are created during recombination.
CC {ECO:0000256|HAMAP-Rule:MF_04155}.
CC -!- SUBUNIT: Homohexamer. The homohexamer is a trimer of asymmetric dimers.
CC Interacts with the DNA primase; this interaction forms the active
CC primosome complex, which is composed of 6 helicase and 1 primase
CC subunits and expresses full helicase and primase activities. Interacts
CC (via C-terminus) with the helicase assembly factor; this interaction
CC brings about the rapid assembly of the helicase onto ssDNA. Part of the
CC replicase complex that includes the DNA polymerase, the polymerase
CC clamp, the clamp loader complex, the single-stranded DNA binding
CC protein, the primase, the DnaB-like replicative helicase and the
CC helicase assembly factor. {ECO:0000256|HAMAP-Rule:MF_04155}.
CC -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_04155}.
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DR EMBL; KR269720; AKJ73164.1; -; Genomic_DNA.
DR RefSeq; YP_009289510.1; NC_031095.1.
DR GeneID; 29080621; -.
DR KEGG; vg:29080621; -.
DR Proteomes; UP000202948; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_04155; Helic_T4; 1.
DR InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR InterPro; IPR046393; Helic_T4.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR30153:SF2; REPLICATIVE DNA HELICASE; 1.
DR PANTHER; PTHR30153; REPLICATIVE DNA HELICASE DNAB; 1.
DR Pfam; PF03796; DnaB_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51199; SF4_HELICASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_04155};
KW DNA replication {ECO:0000256|HAMAP-Rule:MF_04155};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_04155};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_04155, ECO:0000313|EMBL:AKJ73164.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04155};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04155};
KW Reference proteome {ECO:0000313|Proteomes:UP000202948};
KW Viral DNA replication {ECO:0000256|HAMAP-Rule:MF_04155}.
FT DOMAIN 165..435
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT REGION 432..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 197..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04155"
SQ SEQUENCE 479 AA; 53951 MW; 1E3E1E263CF4DA25 CRC64;
MVETILANLI YNQAFFTKVW PYMDKEYFEQ GPAQTVFNII KKHVNEYTAI PSKTALCVAL
DNSSITETEH EGAKKLIDKL SDAPEDLNWL VKETEKYVQE KAMYNATSRI IEIQTNAQLE
PNKRDKRLPD MGAIPDIMRE ALSVSFDSYI GHDWMEDYEA RWLSYQNKAR KVPFKLSILN
KITKGGAETG TLNVLMAGVN VGKSLGLCSL AADYLQMGHN VLYISMEMAE EVCAKRIDAN
LLDVSLDDID DGCVSYAEYK GKMEKWRSSS TLGRLIIKQY PTGGANANTF RALLNELKLK
KNFKPTVIII DYLGICASCR IRQYTENSYT LVKAIAEELR ALAVESETVL WTAAQVGRSA
WDASDMDMSD IAESAGLPAT ADFMLAVIET PELAQMKQQL IKQIKSRYGD KNINNKFFMG
VHKANQRWVE IEKQNDPTKP NPSNTVREGA GAQNRVAESN RQERVSRSKL DALAEELKF
//
