PRIM_BPT4
ID PRIM_BPT4 Reviewed; 342 AA.
AC P04520;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_04157};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_04157, ECO:0000269|PubMed:11735390, ECO:0000269|PubMed:22869700, ECO:0000269|PubMed:2422175};
DE AltName: Full=DNA priming protein {ECO:0000255|HAMAP-Rule:MF_04157};
GN Name=61; Synonyms=58 {ECO:0000303|PubMed:12626685};
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 [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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-211.
RA Nakanishi M., Alberts B.M.;
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 212-342.
RX PubMed=6098451; DOI=10.1002/j.1460-2075.1984.tb02221.x;
RA McDonald P.M., Mosig G.;
RT "Regulation of a new bacteriophage T4 gene, 69, that spans an origin of DNA
RT replication.";
RL EMBO J. 3:2863-2871(1984).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8.
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 [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=2422175; DOI=10.1016/s0021-9258(19)62714-6;
RA Cha T.A., Alberts B.M.;
RT "Studies of the DNA helicase-RNA primase unit from bacteriophage T4. A
RT trinucleotide sequence on the DNA template starts RNA primer synthesis.";
RL J. Biol. Chem. 261:7001-7010(1986).
RN [6]
RP FUNCTION.
RX PubMed=3038901; DOI=10.1016/s0021-9258(18)61046-4;
RA Nossal N.G., Hinton D.M.;
RT "Bacteriophage T4 DNA primase-helicase. Characterization of the DNA
RT synthesis primed by T4 61 protein in the absence of T4 41 protein.";
RL J. Biol. Chem. 262:10879-10885(1987).
RN [7]
RP REVIEW.
RX PubMed=11395406; DOI=10.1146/annurev.biochem.70.1.181;
RA Benkovic S.J., Valentine A.M., Salinas F.;
RT "Replisome-mediated DNA replication.";
RL Annu. Rev. Biochem. 70:181-208(2001).
RN [8]
RP DOMAIN, SUBUNIT, CATALYTIC ACTIVITY, INTERACTION WITH THE DNAB-LIKE
RP REPLICATIVE HELICASE, INTERACTION WITH THE SINGLE-STRANDED DNA-BINDING
RP PROTEIN, AND FUNCTION.
RX PubMed=11735390; DOI=10.1021/bi0108554;
RA Valentine A.M., Ishmael F.T., Shier V.K., Benkovic S.J.;
RT "A zinc ribbon protein in DNA replication: primer synthesis and
RT macromolecular interactions by the bacteriophage T4 primase.";
RL Biochemistry 40:15074-15085(2001).
RN [9]
RP SUBUNIT.
RX PubMed=15897200; DOI=10.1074/jbc.m501847200;
RA Yang J., Xi J., Zhuang Z., Benkovic S.J.;
RT "The oligomeric T4 primase is the functional form during replication.";
RL J. Biol. Chem. 280:25416-25423(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 FUNCTION, INTERACTION WITH THE DNAB-LIKE REPLICATIVE HELICASE, SUBUNIT, AND
RP CATALYTIC ACTIVITY.
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 [12]
RP FUNCTION, INTERACTION WITH THE DNAB-LIKE REPLICATIVE HELICASE, AND SUBUNIT.
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).
RN [13]
RP STRUCTURE BY ELECTRON MICROSCOPY, AND SUBUNIT.
RX PubMed=15738414; DOI=10.1073/pnas.0500713102;
RA Norcum M.T., Warrington J.A., Spiering M.M., Ishmael F.T., Trakselis M.A.,
RA Benkovic S.J.;
RT "Architecture of the bacteriophage T4 primosome: electron microscopy
RT studies of helicase (gp41) and primase (gp61).";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3623-3626(2005).
CC -!- FUNCTION: Synthesizes short RNA primers for the lagging strand DNA
CC replication (PubMed:2422175, PubMed:3038901, PubMed:11735390,
CC PubMed:22869700). The primase synthesizes short RNA primers on the
CC lagging strand that the polymerase elongates using dNTPs
CC (PubMed:2422175, PubMed:3038901). Recognizes two trinucleotide
CC sequences 5'-GTT-3' and 5'-GCT-3' in vitro, but uses only the first as
CC the priming site in vivo (PubMed:2422175). {ECO:0000255|HAMAP-
CC Rule:MF_04157, ECO:0000269|PubMed:11735390,
CC ECO:0000269|PubMed:22869700, ECO:0000269|PubMed:2422175,
CC ECO:0000269|PubMed:3038901}.
CC -!- SUBUNIT: Monomer (PubMed:11735390). Hexamer (PubMed:11735390,
CC PubMed:15897200, PubMed:15738414). Interacts with the DnaB-like
CC replicative helicase; this interaction forms the active primosome
CC complex, which is composed of 6 helicase and 1 primase subunits and
CC expresses full helicase and primase activities (PubMed:22869700,
CC PubMed:23578280, PubMed:11735390). Interacts (via C-terminus) with the
CC single-stranded DNA-binding protein (PubMed:11735390). 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 (PubMed:16800624). {ECO:0000255|HAMAP-
CC Rule:MF_04157, ECO:0000269|PubMed:11735390,
CC ECO:0000269|PubMed:15738414, ECO:0000269|PubMed:15897200,
CC ECO:0000269|PubMed:16800624, ECO:0000269|PubMed:22869700,
CC ECO:0000269|PubMed:23578280}.
CC -!- SIMILARITY: Belongs to the Tequatrovirus DNA primase family.
CC {ECO:0000255|HAMAP-Rule:MF_04157}.
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DR EMBL; AF158101; AAD42502.1; -; Genomic_DNA.
DR EMBL; X01416; CAA25659.1; -; Genomic_DNA.
DR EMBL; K03113; AAA32554.1; -; Genomic_DNA.
DR EMBL; S57514; AAB25713.1; -; Genomic_DNA.
DR PIR; A94456; Z8BPT4.
DR RefSeq; NP_049648.1; NC_000866.4.
DR SMR; P04520; -.
DR GeneID; 1258798; -.
DR KEGG; vg:1258798; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0003896; F:DNA primase activity; IDA:UniProtKB.
DR GO; GO:0039693; P:viral DNA genome replication; IDA:CACAO.
DR HAMAP; MF_04157; PRIMASE_T4; 1.
DR InterPro; IPR013264; DNA_primase_core_N.
DR InterPro; IPR046392; PRIMASE_T4.
DR Pfam; PF08275; Toprim_N; 1.
PE 1: Evidence at protein level;
KW DNA replication; Early protein; Metal-binding; Reference proteome;
KW Transferase; Viral DNA replication; Zinc.
FT CHAIN 1..342
FT /note="DNA primase"
FT /id="PRO_0000164926"
FT BINDING 37
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:11735390"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:11735390"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:11735390"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305|PubMed:11735390"
SQ SEQUENCE 342 AA; 39778 MW; 46BD652C665B8EAB CRC64;
MSSIPWIDNE FAYRALAHLP KFTQVNNSST FKLRFRCPVC GDSKTDQNKA RGWYYGDNNE
GNIHCYNCNY HAPIGIYLKE FEPDLYREYI FEIRKEKGKS RPIEKPKELP KQPEKKIIKS
LPSCVRLDKL AEDHPIIKYV KARCIPKDKW KYLWFTTEWP KLVNSIAPGT YKKEISEPRL
VIPIYNANGK AESFQGRALK KDAPQKYITI EAYPEATKIY GVERVKDGDV YVLEGPIDSL
FIENGIAITG GQLDLEVVPF KDRRVWVLDN EPRHPDTIKR MTKLVDAGER VMFWDKSPWK
SKDVNDMIRK EGATPEQIME YMKNNIAQGL MAKMRLSKYA KI
