ID A0A2Z5HL93_9CAUD Unreviewed; 474 AA.
AC A0A2Z5HL93;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=DnaB-like replicative helicase {ECO:0000256|HAMAP-Rule:MF_04155};
DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_04155};
OS Salmonella phage S118.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Ackermannviridae; Cvivirinae; Kuttervirus; Kuttervirus S118.
OX NCBI_TaxID=2231347 {ECO:0000313|EMBL:AXC40965.1, ECO:0000313|Proteomes:UP000252592};
RN [1] {ECO:0000313|Proteomes:UP000252592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Gencay Y.E.;
RT "Host range determinants of Salmonella infecting bacteriophages.";
RL Submitted (MAY-2018) 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}.
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; MH370371; AXC40965.1; -; Genomic_DNA.
DR Proteomes; UP000252592; 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.
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:AXC40965.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04155};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04155};
KW Viral DNA replication {ECO:0000256|HAMAP-Rule:MF_04155}.
FT DOMAIN 179..409
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|Pfam:PF03796"
FT BINDING 191..198
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04155"
SQ SEQUENCE 474 AA; 54165 MW; FCE940A6D4178B93 CRC64;
MLLESVVLSQ LIYNEEYQRK IQPYLKADYF DNEGEKIIFG LIDHYTCEYN ARPSVEALSI
MLEKTSLNEH VFEQAISALE NINDNTFHQE WLVKETESWA RQKAVHNAIK HAVNIYGDEK
RKDEMNTIPT LLQEALAISF DSYLGHIYWE MAEQQYDHMN SNEAKIPFAV EIFNKATRGG
VGKKTLNIVT GAINAGKTTT LIDLAAGYAE QGLNVFVFTL EVAENVWRHR LDARMMRRDF
ESLEKLSRHE YIATIQKLRT RQDGSMKGDI VIKEYPSGAG HTGLYRRDIL DYATATGITP
DVIIIDYLGE SASSRLPAHL MQNTNVYYTS VAREFRALGF EFDCPVWTGM QFNREKQSAT
DGDISDLADA IGIPKVADFI MAFYAPDELA AVKKARASIL KNRYANKQKL KSFLFGMDQD
KQILFDLDWN EVKRDLTDEE ARYVENVHIK HDLNKTGDSN DVKKAETVNS WNFG
//
