HLOAD_BPT4
ID HLOAD_BPT4 Reviewed; 217 AA.
AC P13342;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=DNA helicase assembly protein {ECO:0000255|HAMAP-Rule:MF_04156, ECO:0000303|PubMed:7806533};
DE AltName: Full=Gene product 59 {ECO:0000255|HAMAP-Rule:MF_04156};
DE Short=Gp59 {ECO:0000255|HAMAP-Rule:MF_04156};
DE AltName: Full=Helicase loader {ECO:0000255|HAMAP-Rule:MF_04156, ECO:0000303|PubMed:22427673};
DE AltName: Full=Helicase loading protein {ECO:0000255|HAMAP-Rule:MF_04156, ECO:0000303|PubMed:10871615};
GN Name=59 {ECO:0000255|HAMAP-Rule:MF_04156};
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].
RC STRAIN=BK536;
RX PubMed=2674900; DOI=10.1093/nar/17.16.6729;
RA Hahn S., Rueger W.;
RT "Organization of the bacteriophage T4 genome between map positions 150.745
RT and 145.824.";
RL Nucleic Acids Res. 17:6729-6729(1989).
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 PROTEIN SEQUENCE OF 1-7, AND CHARACTERIZATION.
RX PubMed=8288591; DOI=10.1016/s0021-9258(17)42255-1;
RA Yonesaki T.;
RT "The purification and characterization of gene 59 protein from
RT bacteriophage T4.";
RL J. Biol. Chem. 269:1284-1289(1994).
RN [4]
RP INTERACTION WITH THE SINGLE-STRANDED DNA-BINDING PROTEIN, FUNCTION, AND
RP INTERACTION WITH THE DNAB-LIKE REPLICATIVE HELICASE.
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 INTERACTION WITH THE DNAB-LIKE REPLICATIVE HELICASE, AND FUNCTION.
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 [6]
RP FUNCTION, INTERACTION WITH THE DNAB-LIKE REPLICATIVE HELICASE, AND
RP INTERACTION WITH THE SINGLE-STRANDED DNA-BINDING PROTEIN.
RX PubMed=11459967; DOI=10.1073/pnas.131007498;
RA Bleuit J.S., Xu H., Ma Y., Wang T., Liu J., Morrical S.W.;
RT "Mediator proteins orchestrate enzyme-ssDNA assembly during T4
RT recombination-dependent DNA replication and repair.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:8298-8305(2001).
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 INTERACTION WITH THE SINGLE-STRANDED DNA-BINDING PROTEIN.
RX PubMed=15507125; DOI=10.1186/1743-422x-1-4;
RA Borjac-Natour J.M., Petrov V.M., Karam J.D.;
RT "Divergence of the mRNA targets for the Ssb proteins of bacteriophages T4
RT and RB69.";
RL Virol. J. 1:4-4(2004).
RN [9]
RP INTERACTION WITH THE VIRAL DNA POLYMERASE.
RX PubMed=15909989; DOI=10.1021/bi047296w;
RA Xi J., Zhang Z., Zhuang Z., Yang J., Spiering M.M., Hammes G.G.,
RA Benkovic S.J.;
RT "Interaction between the T4 helicase loading protein (gp59) and the DNA
RT polymerase (gp43): unlocking of the gp59-gp43-DNA complex to initiate
RT assembly of a fully functional replisome.";
RL Biochemistry 44:7747-7756(2005).
RN [10]
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 [11]
RP SUBUNIT.
RX PubMed=19700405; DOI=10.1074/jbc.m109.029926;
RA Arumugam S.R., Lee T.H., Benkovic S.J.;
RT "Investigation of stoichiometry of T4 bacteriophage helicase loader protein
RT (gp59).";
RL J. Biol. Chem. 284:29283-29289(2009).
RN [12]
RP FUNCTION, AND MUTAGENESIS OF LYS-27; LYS-38; TYR-39; ASP-47; ILE-87;
RP TYR-122; PHE-132; TYR-138; ASN-139; TYR-193; VAL-207; LYS-216 AND TYR-217.
RX PubMed=22427673; DOI=10.1074/jbc.m111.332080;
RA Dolezal D., Jones C.E., Lai X., Brister J.R., Mueser T.C., Nossal N.G.,
RA Hinton D.M.;
RT "Mutational analysis of the T4 gp59 helicase loader reveals its sites for
RT interaction with helicase, single-stranded binding protein, and DNA.";
RL J. Biol. Chem. 287:18596-18607(2012).
RN [13]
RP INTERACTION WITH THE SINGLE-STRANDED DNA-BINDING PROTEIN, AND MUTAGENESIS
RP OF ILE-87.
RX PubMed=24338568; DOI=10.1074/jbc.m113.505842;
RA Branagan A.M., Klein J.A., Jordan C.S., Morrical S.W.;
RT "Control of helicase loading in the coupled DNA replication and
RT recombination systems of bacteriophage T4.";
RL J. Biol. Chem. 289:3040-3054(2014).
RN [14] {ECO:0007744|PDB:1C1K}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS), AND DNA-BINDING.
RX PubMed=10669611; DOI=10.1006/jmbi.1999.3438;
RA Mueser T.C., Jones C.E., Nossal N.G., Hyde C.C.;
RT "Bacteriophage T4 gene 59 helicase assembly protein binds replication fork
RT DNA. The 1.45 A resolution crystal structure reveals a novel alpha-helical
RT two-domain fold.";
RL J. Mol. Biol. 296:597-612(2000).
CC -!- FUNCTION: DNA helicase loader protein that participates in viral DNA
CC replication, recombination, and repair (PubMed:10871615). At the fork,
CC required for loading of the replicative helicase onto DNA protected by
CC the ssDNA-binding protein (PubMed:11459967, PubMed:7806533,
CC PubMed:10871615, PubMed:22427673). Coordinates simultaneous synthesis
CC of leading- and lagging-strands (PubMed:11459969). {ECO:0000255|HAMAP-
CC Rule:MF_04156, ECO:0000269|PubMed:10871615,
CC ECO:0000269|PubMed:11459967, ECO:0000269|PubMed:22427673,
CC ECO:0000269|PubMed:7806533, ECO:0000303|PubMed:11459969}.
CC -!- SUBUNIT: Monomer (PubMed:19700405). Homohexamer; when associated with
CC DNA (PubMed:19700405). Interacts (via C-terminus) with the DnaB-like
CC replicative helicase (via C-terminus); this interaction brings about
CC the rapid assembly of the helicase onto ssDNA (PubMed:11459967,
CC PubMed:7806533, PubMed:10871615, PubMed:22427673). Interacts (via C-
CC terminus) with the single-stranded DNA-binding protein; a ternary
CC complex between the helicase assembly protein, the single-stranded DNA-
CC binding protein and ssDNA is an obligatory intermediate in the helicase
CC loading mechanism (PubMed:11459967, PubMed:24338568, PubMed:15507125,
CC PubMed:7806533, PubMed:22427673). Interacts with the viral DNA
CC polymerase (PubMed:15909989). Binds to single and double-stranded DNA
CC (PubMed:10669611). Part of the replicase complex that includes the DNA
CC polymerase, the polymerase clamp, the clamp loader complex, the single-
CC stranded DNA binding protein (SSB), the primase, the DnaB-like
CC replicative helicase and the helicase assembly factor
CC (PubMed:16800624). {ECO:0000255|HAMAP-Rule:MF_04156,
CC ECO:0000269|PubMed:10669611, ECO:0000269|PubMed:10871615,
CC ECO:0000269|PubMed:11459967, ECO:0000269|PubMed:15507125,
CC ECO:0000269|PubMed:15909989, ECO:0000269|PubMed:16800624,
CC ECO:0000269|PubMed:19700405, ECO:0000269|PubMed:22427673,
CC ECO:0000269|PubMed:24338568, ECO:0000269|PubMed:7806533}.
CC -!- SIMILARITY: Belongs to the Tequatrovirus DNA helicase assembly protein
CC family. {ECO:0000255|HAMAP-Rule:MF_04156, ECO:0000305}.
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; X15818; CAA33815.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42503.1; -; Genomic_DNA.
DR PIR; S05559; GMBPT4.
DR RefSeq; NP_049856.1; NC_000866.4.
DR PDB; 1C1K; X-ray; 1.45 A; A=1-217.
DR PDBsum; 1C1K; -.
DR SMR; P13342; -.
DR GeneID; 1258623; -.
DR KEGG; vg:1258623; -.
DR EvolutionaryTrace; P13342; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IDA:UniProtKB.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR Gene3D; 1.10.220.50; -; 1.
DR HAMAP; MF_04156; HELIC_LOADER_T4; 1.
DR InterPro; IPR008944; Phage_T4_Gp59.
DR InterPro; IPR015086; Phage_T4_Gp59_C.
DR InterPro; IPR037082; Phage_T4_Gp59_C_sf.
DR InterPro; IPR023197; Phage_T4_Gp59_dom_sf.
DR InterPro; IPR015085; Phage_T4_Gp59_N.
DR Pfam; PF08994; T4_Gp59_C; 1.
DR Pfam; PF08993; T4_Gp59_N; 1.
DR PIRSF; PIRSF004374; Phage-associated_Gp59; 1.
DR SUPFAM; SSF48493; SSF48493; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA replication; DNA-binding;
KW Reference proteome; Viral DNA replication.
FT CHAIN 1..217
FT /note="DNA helicase assembly protein"
FT /id="PRO_0000165046"
FT MUTAGEN 27
FT /note="K->E: Impaired DNA-binding."
FT /evidence="ECO:0000269|PubMed:22427673"
FT MUTAGEN 38
FT /note="K->A: Impaired DNA-binding."
FT /evidence="ECO:0000269|PubMed:22427673"
FT MUTAGEN 39
FT /note="Y->A: Impaired DNA-binding."
FT /evidence="ECO:0000269|PubMed:22427673"
FT MUTAGEN 47
FT /note="D->G: Impaired DNA-binding."
FT /evidence="ECO:0000269|PubMed:22427673"
FT MUTAGEN 87
FT /note="I->A: Impaired DNA-binding but loads helicase
FT normally onto ssDNA covered with SSB."
FT /evidence="ECO:0000269|PubMed:22427673,
FT ECO:0000269|PubMed:24338568"
FT MUTAGEN 122
FT /note="Y->A: Impaired interaction with the DnaB-like
FT replicative helicase."
FT /evidence="ECO:0000269|PubMed:22427673"
FT MUTAGEN 138
FT /note="Y->A: Impaired interaction with SSB."
FT /evidence="ECO:0000269|PubMed:22427673"
FT MUTAGEN 139
FT /note="N->A: Impaired interaction with SSB."
FT /evidence="ECO:0000269|PubMed:22427673"
FT MUTAGEN 193
FT /note="Y->A: Impaired DNA-binding."
FT /evidence="ECO:0000269|PubMed:22427673"
FT MUTAGEN 207
FT /note="V->A: Impaired DNA-binding."
FT /evidence="ECO:0000269|PubMed:22427673"
FT MUTAGEN 216
FT /note="K->A: Impaired interaction with SSB."
FT /evidence="ECO:0000269|PubMed:22427673"
FT MUTAGEN 217
FT /note="Y->A: Impaired interaction with SSB."
FT /evidence="ECO:0000269|PubMed:22427673"
FT STRAND 2..4
FT /evidence="ECO:0007829|PDB:1C1K"
FT HELIX 16..30
FT /evidence="ECO:0007829|PDB:1C1K"
FT TURN 36..41
FT /evidence="ECO:0007829|PDB:1C1K"
FT HELIX 47..52
FT /evidence="ECO:0007829|PDB:1C1K"
FT HELIX 56..65
FT /evidence="ECO:0007829|PDB:1C1K"
FT HELIX 68..81
FT /evidence="ECO:0007829|PDB:1C1K"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1C1K"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1C1K"
FT HELIX 95..107
FT /evidence="ECO:0007829|PDB:1C1K"
FT HELIX 109..126
FT /evidence="ECO:0007829|PDB:1C1K"
FT HELIX 132..135
FT /evidence="ECO:0007829|PDB:1C1K"
FT TURN 140..143
FT /evidence="ECO:0007829|PDB:1C1K"
FT HELIX 146..152
FT /evidence="ECO:0007829|PDB:1C1K"
FT HELIX 158..168
FT /evidence="ECO:0007829|PDB:1C1K"
FT HELIX 170..177
FT /evidence="ECO:0007829|PDB:1C1K"
FT HELIX 181..196
FT /evidence="ECO:0007829|PDB:1C1K"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:1C1K"
FT HELIX 201..216
FT /evidence="ECO:0007829|PDB:1C1K"
SQ SEQUENCE 217 AA; 25997 MW; B9E7DDE80DCF978C CRC64;
MIKLRMPAGG ERYIDGKSVY KLYLMIKQHM NGKYDVIKYN WCMRVSDAAY QKRRDKYFFQ
KLSEKYKLKE LALIFISNLV ANQDAWIGDI SDADALVFYR EYIGRLKQIK FKFEEDIRNI
YYFSKKVEVS AFKEIFEYNP KVQSSYIFKL LQSNIISFET FILLDSFLNI IDKHDEQTDN
LVWNNYSIKL KAYRKILNID SQKAKNVFIE TVKSCKY
