DNAG_LISMO
ID DNAG_LISMO Reviewed; 626 AA.
AC P47762;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 05-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 138.
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}; OrderedLocusNames=lmo1455;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13932 / LMG 21264 / NCTC 10527 / SLCC 2375;
RX PubMed=7828867; DOI=10.1016/0378-1119(94)90649-1;
RA Metzger R., Brown D.P., Grealish P., Staver M.J., Versalovic J.,
RA Lupski J.R., Katz L.;
RT "Characterization of the macromolecular synthesis (MMS) operon from
RT Listeria monocytogenes.";
RL Gene 151:161-166(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; U13165; AAC43305.1; -; Genomic_DNA.
DR EMBL; AL591979; CAC99533.1; -; Genomic_DNA.
DR PIR; AG1256; AG1256.
DR RefSeq; NP_464980.1; NC_003210.1.
DR RefSeq; WP_010990130.1; NZ_CP023861.1.
DR AlphaFoldDB; P47762; -.
DR SMR; P47762; -.
DR STRING; 169963.lmo1455; -.
DR PaxDb; P47762; -.
DR EnsemblBacteria; CAC99533; CAC99533; CAC99533.
DR GeneID; 986564; -.
DR KEGG; lmo:lmo1455; -.
DR PATRIC; fig|169963.11.peg.1494; -.
DR eggNOG; COG0305; Bacteria.
DR eggNOG; COG0358; Bacteria.
DR HOGENOM; CLU_013501_3_3_9; -.
DR OMA; LMWPIRD; -.
DR PhylomeDB; P47762; -.
DR BioCyc; LMON169963:LMO1455-MON; -.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IBA:GO_Central.
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..626
FT /note="DNA primase"
FT /id="PRO_0000180500"
FT DOMAIN 264..346
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT ZN_FING 39..63
FT /note="CHC2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 270
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 314
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 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT CONFLICT 57
FT /note="I -> M (in Ref. 1; AAC43305)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="S -> A (in Ref. 1; AAC43305)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="A -> R (in Ref. 1; AAC43305)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="K -> R (in Ref. 1; AAC43305)"
FT /evidence="ECO:0000305"
FT CONFLICT 391
FT /note="E -> D (in Ref. 1; AAC43305)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="G -> S (in Ref. 1; AAC43305)"
FT /evidence="ECO:0000305"
FT CONFLICT 467..468
FT /note="GA -> ET (in Ref. 1; AAC43305)"
FT /evidence="ECO:0000305"
FT CONFLICT 478
FT /note="A -> T (in Ref. 1; AAC43305)"
FT /evidence="ECO:0000305"
FT CONFLICT 486
FT /note="I -> T (in Ref. 1; AAC43305)"
FT /evidence="ECO:0000305"
FT CONFLICT 520
FT /note="E -> K (in Ref. 1; AAC43305)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="A -> T (in Ref. 1; AAC43305)"
FT /evidence="ECO:0000305"
FT CONFLICT 569
FT /note="P -> T (in Ref. 1; AAC43305)"
FT /evidence="ECO:0000305"
FT CONFLICT 581
FT /note="Y -> F (in Ref. 1; AAC43305)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="Y -> L (in Ref. 1; AAC43305)"
FT /evidence="ECO:0000305"
FT CONFLICT 603..604
FT /note="NE -> KD (in Ref. 1; AAC43305)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 626 AA; 71756 MW; F38C75AE34CA5709 CRC64;
MARIPEEVID QVRNQADIVD IIGNYVQLKK QGRNYSGLCP FHGEKTPSFS VSPEKQIFHC
FGCGKGGNVF SFLMEHDGLT FVESVKKVAD MSHLDVAIEL PEERDTSNLP KETSETAKMV
EMHQLTAKLY HYILMETEEG TAALTYLKER GMSEQMMTTF QIGFAPNHHA TITSFLEKRG
MDLQLAGAAG LLSERDDGQM VDRFRNRIMF PITNDRGQII AFSGRLFDRD DGPKYLNSPE
TPVFNKRRIL FHFSEARQAI RKQEEITLME GFMDVISAEE AGVQNAVASM GTSLTEEHAD
LIKRLTNRAI ICYDGDRAGI EAAYKAGTLL VERNRLDVFV LQLPAGKDPD DFIRASGPEK
FKEVYKQQRM TWTAFKIHYL RKERNLQNET EQIGYIDDCL REIAKLDQAV ERELYLKQLA
DEFELTIETL KQQLQQSLKN SQKSRQMASY NEPPIDDSFM GMMPQEGAEM LFSFEQPAQK
LSAHTISEQQ LMKAMMESRD NFLLIKQLLG DTTFYHDNYE ALYTYLIGYF AEGNDADPTK
FMDSVPDAAM KGLISSLEMV ISPDEQGKPQ FEDYIRSLKR YKLEQKKKEL EQELATYNRE
NDNENEIRVM LEIVQLNRQL NSGQLD
