DNAG_LACLA
ID DNAG_LACLA Reviewed; 637 AA.
AC Q04505; Q9CI14;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 3.
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}; Synonyms=dnaE;
GN OrderedLocusNames=LL0552; ORFNames=L0269;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-393.
RC STRAIN=ATCC 19435 / DSM 20481 / NCDO 604 / NCIB 6681 / NCTC 6681;
RX PubMed=7765979; DOI=10.1271/bbb.59.73;
RA Kojima T., Ishibashi N., Tanaka K., Takahashi H.;
RT "Identification and molecular analysis of Lactococcus lactis rpoD operon.";
RL Biosci. Biotechnol. Biochem. 59:73-77(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 338-637.
RC STRAIN=ATCC 19435 / DSM 20481 / NCDO 604 / NCIB 6681 / NCTC 6681;
RX PubMed=7503808; DOI=10.1271/bbb.57.88;
RA Araya T., Ishibashi N., Shimamura S., Tanaka K., Takahashi H.;
RT "Genetic and molecular analysis of the rpoD gene from Lactococcus lactis.";
RL Biosci. Biotechnol. Biochem. 57:88-92(1993).
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; AE005176; AAK04650.1; -; Genomic_DNA.
DR EMBL; D14690; BAA03516.1; -; Genomic_DNA.
DR EMBL; D10168; BAA01037.1; -; Genomic_DNA.
DR PIR; H86693; H86693.
DR PIR; JC2485; JC2485.
DR RefSeq; NP_266708.1; NC_002662.1.
DR RefSeq; WP_003130831.1; NC_002662.1.
DR AlphaFoldDB; Q04505; -.
DR SMR; Q04505; -.
DR STRING; 272623.L0269; -.
DR PaxDb; Q04505; -.
DR PRIDE; Q04505; -.
DR EnsemblBacteria; AAK04650; AAK04650; L0269.
DR KEGG; lla:L0269; -.
DR PATRIC; fig|272623.7.peg.590; -.
DR eggNOG; COG0358; Bacteria.
DR HOGENOM; CLU_013501_3_3_9; -.
DR OMA; LMWPIRD; -.
DR Proteomes; UP000002196; 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..637
FT /note="DNA primase"
FT /id="PRO_0000180497"
FT DOMAIN 257..338
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 263
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 307
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 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 309
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT CONFLICT 190
FT /note="N -> K (in Ref. 2; BAA03516)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="H -> Q (in Ref. 2; BAA03516)"
FT /evidence="ECO:0000305"
FT CONFLICT 271
FT /note="A -> S (in Ref. 2; BAA03516)"
FT /evidence="ECO:0000305"
FT CONFLICT 292
FT /note="I -> V (in Ref. 2; BAA03516)"
FT /evidence="ECO:0000305"
FT CONFLICT 432
FT /note="T -> K (in Ref. 3; BAA01037)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="A -> T (in Ref. 3; BAA01037)"
FT /evidence="ECO:0000305"
FT CONFLICT 589
FT /note="K -> N (in Ref. 3; BAA01037)"
FT /evidence="ECO:0000305"
FT CONFLICT 634..637
FT /note="KKKL -> NEKIMIIFY (in Ref. 3; BAA01037)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 637 AA; 72751 MW; 8EF5301EBAFF3B21 CRC64;
MVSLDTEVVN DLKSKVNIAD LISQYVALSR TGKNYIGLCP FHGEKTPSFN VNAEKGFYHC
FGCGRSGDAI EFLKEYNQVG FVDAVKELAD FAGVTLNISD DREEKNNPNA PLFEINNQAA
RLYNILLMST ELGERARKYL EERGITDDVI KRFNIGLAPE ENDFIFKNLS NKFDEEIMAK
SGLFHFSNNN VFDAFTNRIM FPITNEYGHT IGFSGRKWQE NDDSKAKYIN TSATTIFDKS
YELWNLDKAK PTISKQHEVY LMEGFMDVIA AYKAGINNVV ASMGTALTEK HIRRLKQMAK
KFVLVYDGDS AGQNAIYKAI DLIGESAVQI VKVPEGLDPD EYSKNYGLKG LSALMETGRI
QPIEFLIDYL RPENLANLQT QLDFIEQISP MIAKLPSITA QDAYIRKLVE ILPDFEYNQV
EQAVNLRREN MTITDHPVSN LDASSLTESF TDENDYSSLE SVMPVDFEEA YYENNVKTQQ
TYRRSESAQV VQPSVQVPKL SRSEKAEEML LHRMIYHSSV LKKFSQDENF RFVHKRYQDL
FDKILLEAMV YEQIDESHLA SELSDEERSL FYQIISLDLP DTASSQEIKD LVSIFSNEME
QIKFEELIQQ LATAEKAGNK ERVLELTLQI INQKKKL
