DNAG_STAAM
ID DNAG_STAAM Reviewed; 605 AA.
AC P63964; Q99TT4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=SAV1562;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(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; BA000017; BAB57724.1; -; Genomic_DNA.
DR RefSeq; WP_001217257.1; NC_002758.2.
DR PDB; 2LZN; NMR; -; A=463-605.
DR PDBsum; 2LZN; -.
DR AlphaFoldDB; P63964; -.
DR BMRB; P63964; -.
DR SMR; P63964; -.
DR PaxDb; P63964; -.
DR EnsemblBacteria; BAB57724; BAB57724; SAV1562.
DR KEGG; sav:SAV1562; -.
DR HOGENOM; CLU_013501_3_3_9; -.
DR OMA; LMWPIRD; -.
DR PhylomeDB; P63964; -.
DR BioCyc; SAUR158878:SAV_RS08410-MON; -.
DR Proteomes; UP000002481; 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:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
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; IPR036185; DNA_heli_DnaB-like_N_sf.
DR InterPro; IPR007693; DNA_helicase_DnaB-like_N.
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; 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; PF00772; DnaB; 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 SUPFAM; SSF48024; SSF48024; 1.
DR TIGRFAMs; TIGR01391; dnaG; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA replication; DNA-binding; DNA-directed RNA polymerase;
KW Magnesium; Metal-binding; Nucleotidyltransferase; Primosome; Transcription;
KW Transferase; Zinc; Zinc-finger.
FT CHAIN 1..605
FT /note="DNA primase"
FT /id="PRO_0000180519"
FT DOMAIN 260..341
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT ZN_FING 38..62
FT /note="CHC2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 266
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 310
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 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT HELIX 468..476
FT /evidence="ECO:0007829|PDB:2LZN"
FT HELIX 484..493
FT /evidence="ECO:0007829|PDB:2LZN"
FT TURN 496..498
FT /evidence="ECO:0007829|PDB:2LZN"
FT HELIX 502..515
FT /evidence="ECO:0007829|PDB:2LZN"
FT HELIX 523..528
FT /evidence="ECO:0007829|PDB:2LZN"
FT STRAND 530..532
FT /evidence="ECO:0007829|PDB:2LZN"
FT HELIX 535..544
FT /evidence="ECO:0007829|PDB:2LZN"
FT STRAND 547..550
FT /evidence="ECO:0007829|PDB:2LZN"
FT HELIX 552..554
FT /evidence="ECO:0007829|PDB:2LZN"
FT HELIX 556..564
FT /evidence="ECO:0007829|PDB:2LZN"
FT STRAND 565..568
FT /evidence="ECO:0007829|PDB:2LZN"
FT HELIX 573..582
FT /evidence="ECO:0007829|PDB:2LZN"
FT TURN 583..585
FT /evidence="ECO:0007829|PDB:2LZN"
FT HELIX 590..602
FT /evidence="ECO:0007829|PDB:2LZN"
SQ SEQUENCE 605 AA; 70032 MW; 1B35AB0F4B4E01D8 CRC64;
MRIDQSIINE IKDKTDILDL VSEYVKLEKR GRNYIGLCPF HDEKTPSFTV SEDKQICHCF
GCKKGGNVFQ FTQEIKDISF VEAVKELGDR VNVAVDIEAT QSNSNVQIAS DDLQMIEMHE
LIQEFYYYAL TKTVEGEQAL TYLQERGFTD ALIKERGIGF APDSSHFCHD FLQKKGYDIE
LAYEAGLLSR NEENFSYYDR FRNRIMFPLK NAQGRIVGYS GRTYTGQEPK YLNSPETPIF
QKRKLLYNLD KARKSIRKLD EIVLLEGFMD VIKSDTAGLK NVVATMGTQL SDEHITFIRK
LTSNITLMFD GDFAGSEATL KTGQHLLQQG LNVFVIQLPS GMDPDEYIGK YGNDAFTTFV
KNDKKSFAHY KVSILKDEIA HNDLSYERYL KELSHDISLM KSSILQQKAI NDVAPFFNVS
PEQLANEIQF NQAPANYYPE DEYGGYDEYG GYIEPEPIGM AQFDNLSRQE KAERAFLKHL
MRDKDTFLNY YESVDKDNFT NQHFKYVFEV LHDFYAENDQ YNISDAVQYV NSNELRETLI
SLEQYNLNDE PYENEIDDYV NVINEKGQET IESLNHKLRE ATRIGDVELQ KYYLQQIVAK
NKERM
