DNAG_ENTFA
ID DNAG_ENTFA Reviewed; 628 AA.
AC P52308;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_00974};
DE EC=2.7.7.101 {ECO:0000255|HAMAP-Rule:MF_00974};
GN Name=dnaG {ECO:0000255|HAMAP-Rule:MF_00974}; Synonyms=dnaE;
GN OrderedLocusNames=EF_1521;
OS Enterococcus faecalis (strain ATCC 700802 / V583).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=226185;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700802 / V583;
RX PubMed=12663927; DOI=10.1126/science.1080613;
RA Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT faecalis.";
RL Science 299:2071-2074(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 365-628.
RC STRAIN=ATCC 19433 / DSM 20478 / JCM 8726 / NBRC 100481 / NCIMB 775;
RX PubMed=8914262; DOI=10.1002/jobm.3620360503;
RA Frere J., Gansel X., Benachour A., Auffray Y.;
RT "Molecular analysis of the rpoD gene of Enterococcus faecalis.";
RL J. Basic Microbiol. 36:305-310(1996).
CC -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC molecules used as primers for DNA polymerase during DNA replication.
CC {ECO:0000255|HAMAP-Rule:MF_00974}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.;
CC EC=2.7.7.101; Evidence={ECO:0000255|HAMAP-Rule:MF_00974};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00974};
CC Note=Binds 1 zinc ion per monomer. {ECO:0000255|HAMAP-Rule:MF_00974};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00974};
CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP-Rule:MF_00974};
CC -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000255|HAMAP-
CC Rule:MF_00974}.
CC -!- DOMAIN: Contains an N-terminal zinc-binding domain, a central core
CC domain that contains the primase activity, and a C-terminal DnaB-
CC binding domain. {ECO:0000255|HAMAP-Rule:MF_00974}.
CC -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000255|HAMAP-
CC Rule:MF_00974}.
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DR EMBL; AE016830; AAO81310.1; -; Genomic_DNA.
DR EMBL; X86176; CAA60112.1; -; Genomic_DNA.
DR PIR; S54113; S54113.
DR RefSeq; NP_815240.1; NC_004668.1.
DR RefSeq; WP_002361790.1; NZ_KE136528.1.
DR AlphaFoldDB; P52308; -.
DR SMR; P52308; -.
DR STRING; 226185.EF_1521; -.
DR PRIDE; P52308; -.
DR EnsemblBacteria; AAO81310; AAO81310; EF_1521.
DR KEGG; efa:EF1521; -.
DR PATRIC; fig|226185.45.peg.1981; -.
DR eggNOG; COG0358; Bacteria.
DR HOGENOM; CLU_013501_3_3_9; -.
DR OMA; LMWPIRD; -.
DR Proteomes; UP000001415; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR CDD; cd03364; TOPRIM_DnaG_primases; 1.
DR Gene3D; 1.10.860.10; -; 1.
DR Gene3D; 3.90.580.10; -; 1.
DR Gene3D; 3.90.980.10; -; 1.
DR HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR InterPro; IPR016136; DNA_helicase_N/primase_C.
DR InterPro; IPR013264; DNA_primase_core_N.
DR InterPro; IPR037068; DNA_primase_core_N_sf.
DR InterPro; IPR019475; DNA_primase_DnaB-bd.
DR InterPro; IPR006295; DNA_primase_DnaG.
DR InterPro; IPR036977; DNA_primase_Znf_CHC2.
DR InterPro; IPR030846; DnaG_bac.
DR InterPro; IPR034151; TOPRIM_DnaG_bac.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR002694; Znf_CHC2.
DR Pfam; PF10410; DnaB_bind; 1.
DR Pfam; PF08275; Toprim_N; 1.
DR Pfam; PF01807; zf-CHC2; 1.
DR PIRSF; PIRSF002811; DnaG; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SMART; SM00400; ZnF_CHCC; 1.
DR TIGRFAMs; TIGR01391; dnaG; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW DNA replication; DNA-binding; DNA-directed RNA polymerase; Magnesium;
KW Metal-binding; Nucleotidyltransferase; Primosome; Reference proteome;
KW Transcription; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..628
FT /note="DNA primase"
FT /id="PRO_0000180493"
FT DOMAIN 269..351
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT ZN_FING 40..64
FT /note="CHC2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 321
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT CONFLICT 507
FT /note="I -> V (in Ref. 2; CAA60112)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 628 AA; 73058 MW; A582385BBE47DC21 CRC64;
MAQRIPQEVI EEVRHRTNIV DIIGQYVQLK KSGKNYMGLC PFHEERSPSF SVAEDKQIFH
CFGCGKGGTV FNFLQEIEGI SFPESVKRVA DLEHLSVDFD WSEPREVADT PENQQRRSLL
QLHSKAAELY HHILVNTKIG EPALNYLLER GLTQELIETF QIGFAPQKRD FLSQVFKNEQ
LDETLFEPSG LFVQRDNGTF LDRFYQRIMF PINDPQGNVI AFSGRLLKTA DFPGDEMPKY
LNSPETTLFN KRETLFNFDR ARKEIRKENT VLLFEGFMDV IAAWQSGVKS GVASMGTSLT
NEQIRRLERV AKEVVICYDG DNAGVQATNR AIQLLQENSH FDLSIVSIPE KLDPDEYVRK
YGAEAFQNLA NHGRETVFSF KMNYHRLTRN MNNEKEQLDY VNELLRELTN VQSPLERDRY
LNQIAQEFQL SVHSLEEQFN QLKQEQRSVQ RQERQQFYQD EMMPPPMEEP VFEENHVQNK
LPLTQVQKAE RSLLFRLMNE QGVRQTIQQL PDFSFAHDEY QELYFLLESY ATLHQSFDIA
DFINFLQDNQ TKQLAIEIAY QNLSEESSER EVADLLHVIA LSSIAEAIEQ KKIQQQEAKR
VGNQQLEAEL TMEIIQLARQ LKAQRTFT
