HELIC_BPT4
ID HELIC_BPT4 Reviewed; 475 AA.
AC P04530;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=DnaB-like replicative helicase {ECO:0000255|HAMAP-Rule:MF_04155};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_04155, ECO:0000269|PubMed:10871615, ECO:0000269|PubMed:7806533, ECO:0000269|PubMed:8107085};
DE AltName: Full=Gene product 41 {ECO:0000255|HAMAP-Rule:MF_04155};
DE Short=Gp41 {ECO:0000255|HAMAP-Rule:MF_04155};
GN Name=41 {ECO:0000255|HAMAP-Rule:MF_04155};
OS Enterobacteria phage T4 (Bacteriophage T4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10665;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8383243; DOI=10.1128/jvi.67.4.2305-2316.1993;
RA Selick H.E., Stormo G.D., Dyson R.L., Alberts B.M.;
RT "Analysis of five presumptive protein-coding sequences clustered between
RT the primosome genes, 41 and 61, of bacteriophages T4, T2, and T6.";
RL J. Virol. 67:2305-2316(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT "Bacteriophage T4 genome.";
RL Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN [3]
RP CATALYTIC ACTIVITY.
RX PubMed=8107085; DOI=10.1006/jmbi.1994.1100;
RA Young M.C., Schlutz D.E., Ring D., von Hippel P.H.;
RT "Kinetic parameters of the translocation of bacteriophage T4 gene 41
RT protein helicase on single-stranded DNA.";
RL J. Mol. Biol. 235:1447-1458(1994).
RN [4]
RP INTERACTION WITH THE DNA HELICASE ASSEMBLY PROTEIN, AND CATALYTIC ACTIVITY.
RX PubMed=7806533; DOI=10.1016/s0021-9258(20)30096-x;
RA Barry J., Alberts B.;
RT "Purification and characterization of bacteriophage T4 gene 59 protein. A
RT DNA helicase assembly protein involved in DNA replication.";
RL J. Biol. Chem. 269:33049-33062(1994).
RN [5]
RP SUBUNIT.
RX PubMed=7706292; DOI=10.1074/jbc.270.13.7462;
RA Dong F., Gogol E.P., von Hippel P.H.;
RT "The phage T4-coded DNA replication helicase (gp41) forms a hexamer upon
RT activation by nucleoside triphosphate.";
RL J. Biol. Chem. 270:7462-7473(1995).
RN [6]
RP INTERACTION WITH THE DNA HELICASE ASSEMBLY PROTEIN, FUNCTION, AND CATALYTIC
RP ACTIVITY.
RX PubMed=10871615; DOI=10.1074/jbc.m003808200;
RA Jones C.E., Mueser T.C., Nossal N.G.;
RT "Interaction of the bacteriophage T4 gene 59 helicase loading protein and
RT gene 41 helicase with each other and with fork, flap, and cruciform DNA.";
RL J. Biol. Chem. 275:27145-27154(2000).
RN [7]
RP REVIEW.
RX PubMed=11459969; DOI=10.1073/pnas.121009398;
RA Jones C.E., Mueser T.C., Dudas K.C., Kreuzer K.N., Nossal N.G.;
RT "Bacteriophage T4 gene 41 helicase and gene 59 helicase-loading protein: a
RT versatile couple with roles in replication and recombination.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8312-8318(2001).
RN [8]
RP IDENTIFICATION IN THE REPLICASE COMPLEX.
RX PubMed=16800624; DOI=10.1021/bi0603322;
RA Smiley R.D., Zhuang Z., Benkovic S.J., Hammes G.G.;
RT "Single-molecule investigation of the T4 bacteriophage DNA polymerase
RT holoenzyme: multiple pathways of holoenzyme formation.";
RL Biochemistry 45:7990-7997(2006).
RN [9]
RP INTERACTION WITH THE DNA PRIMASE, AND SUBUNIT.
RX PubMed=22869700; DOI=10.1073/pnas.1210040109;
RA Jose D., Weitzel S.E., Jing D., von Hippel P.H.;
RT "Assembly and subunit stoichiometry of the functional helicase-primase
RT (primosome) complex of bacteriophage T4.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:13596-13601(2012).
RN [10]
RP INTERACTION WITH THE DNA PRIMASE, SUBUNIT, AND FUNCTION.
RX PubMed=23578280; DOI=10.1021/bi400231s;
RA Lee W., Jose D., Phelps C., Marcus A.H., von Hippel P.H.;
RT "A single-molecule view of the assembly pathway, subunit stoichiometry, and
RT unwinding activity of the bacteriophage T4 primosome (helicase-primase)
RT complex.";
RL Biochemistry 52:3157-3170(2013).
CC -!- FUNCTION: ATP-dependent DNA helicase essential for viral DNA
CC replication and recombination (PubMed:10871615). The helicase moves 5'
CC -> 3' on the lagging strand template, unwinding the DNA duplex ahead of
CC the leading strand polymerase at the replication fork and generating
CC ssDNA for both leading and lagging strand synthesis (PubMed:11459969,
CC PubMed:23578280). Interaction with the primase allows the primase to
CC initiate lagging strand synthesis and fully activates the helicase
CC (PubMed:22869700, PubMed:23578280). Loaded by the helicase assembly
CC factor on replication forks that begin at discrete replication origin
CC sequences, as well as on forks that are created during recombination
CC (PubMed:10871615). {ECO:0000255|HAMAP-Rule:MF_04155,
CC ECO:0000269|PubMed:10871615, ECO:0000269|PubMed:22869700,
CC ECO:0000269|PubMed:23578280, ECO:0000303|PubMed:11459969}.
CC -!- SUBUNIT: Homohexamer (PubMed:7706292, PubMed:22869700,
CC PubMed:23578280). The homohexamer is a trimer of asymmetric dimers
CC (PubMed:7706292). Interacts with the DNA primase; this interaction
CC forms the active primosome complex, which is composed of 6 helicase and
CC 1 primase subunits and expresses full helicase and primase activities
CC (PubMed:22869700, PubMed:23578280). Interacts (via C-terminus) with the
CC helicase assembly factor; this interaction brings about the rapid
CC assembly of the helicase onto ssDNA (PubMed:7806533, PubMed:10871615).
CC Part of the replicase complex that includes the DNA polymerase, the
CC polymerase clamp, the clamp loader complex, the single-stranded DNA
CC binding protein, the primase, the DnaB-like replicative helicase and
CC the helicase assembly factor (PubMed:16800624). {ECO:0000255|HAMAP-
CC Rule:MF_04155, ECO:0000269|PubMed:10871615,
CC ECO:0000269|PubMed:16800624, ECO:0000269|PubMed:22869700,
CC ECO:0000269|PubMed:23578280, ECO:0000269|PubMed:7706292,
CC ECO:0000269|PubMed:7806533}.
CC -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_04155}.
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DR EMBL; K03113; AAA32553.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42466.1; -; Genomic_DNA.
DR PIR; A04308; Z4BPT4.
DR RefSeq; NP_049654.1; NC_000866.4.
DR SMR; P04530; -.
DR PRIDE; P04530; -.
DR GeneID; 1258700; -.
DR KEGG; vg:1258700; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IDA:GO_Central.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IDA:GO_Central.
DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF03796; DnaB_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51199; SF4_HELICASE; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Primosome; Reference proteome; Viral DNA replication.
FT CHAIN 1..475
FT /note="DnaB-like replicative helicase"
FT /id="PRO_0000165038"
FT DOMAIN 165..444
FT /note="SF4 helicase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04155"
FT REGION 456..475
FT /note="Interaction with the helicase assembly factor"
FT /evidence="ECO:0000269|PubMed:10871615"
FT BINDING 197..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04155"
SQ SEQUENCE 475 AA; 53601 MW; A544B1F9CFC90B4C CRC64;
MVEIILSHLI FDQAYFSKVW PYMDSEYFES GPAKNTFKLI KSHVNEYHSV PSINALNVAL
ENSSFTETEY SGVKTLISKL ADSPEDHSWL VKETEKYVQQ RAMFNATSKI IEIQTNAELP
PEKRNKKMPD VGAIPDIMRQ ALSISFDSYV GHDWMDDYEA RWLSYMNKAR KVPFKLRILN
KITKGGAETG TLNVLMAGVN VGKSLGLCSL AADYLQLGHN VLYISMEMAE EVCAKRIDAN
MLDVSLDDID DGHISYAEYK GKMEKWREKS TLGRLIVKQY PTGGADANTF RSLLNELKLK
KNFVPTIIIV DYLGICKSCR IRVYSENSYT TVKAIAEELR ALAVETETVL WTAAQVGKQA
WDSSDVNMSD IAESAGLPAT ADFMLAVIET EELAAAEQQL IKQIKSRYGD KNKWNKFLMG
VQKGNQKWVE IEQDSTPTEV NEVAGSQQIQ AEQNRYQRNE STRAQLDALA NELKF
