DNAG_STAAU
ID DNAG_STAAU Reviewed; 605 AA.
AC O05338;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 108.
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};
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=912;
RA Owada J., Ideno H., Ohta T.;
RT "Sigma70 operon in Staphylococcus aureus.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA19493.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB001896; BAA19493.1; ALT_FRAME; Genomic_DNA.
DR PDB; 4E2K; X-ray; 2.15 A; A=111-436.
DR PDB; 4EDG; X-ray; 2.00 A; A=111-436.
DR PDB; 4EDK; X-ray; 2.00 A; A=111-436.
DR PDB; 4EDR; X-ray; 2.01 A; A=111-436.
DR PDB; 4EDT; X-ray; 2.00 A; A=111-436.
DR PDB; 4EDV; X-ray; 2.01 A; A=111-436.
DR PDB; 4EE1; X-ray; 2.02 A; A=111-436.
DR PDBsum; 4E2K; -.
DR PDBsum; 4EDG; -.
DR PDBsum; 4EDK; -.
DR PDBsum; 4EDR; -.
DR PDBsum; 4EDT; -.
DR PDBsum; 4EDV; -.
DR PDBsum; 4EE1; -.
DR AlphaFoldDB; O05338; -.
DR BMRB; O05338; -.
DR SMR; O05338; -.
DR BRENDA; 2.7.7.101; 3352.
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_0000180523"
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 111..132
FT /evidence="ECO:0007829|PDB:4EDK"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:4EDK"
FT HELIX 150..156
FT /evidence="ECO:0007829|PDB:4EDK"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:4EDK"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:4EDK"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:4EDK"
FT HELIX 179..184
FT /evidence="ECO:0007829|PDB:4EDK"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:4EDK"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:4EDK"
FT STRAND 197..200
FT /evidence="ECO:0007829|PDB:4EDK"
FT STRAND 203..210
FT /evidence="ECO:0007829|PDB:4EDK"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:4EDK"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:4EDK"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:4EDK"
FT TURN 242..244
FT /evidence="ECO:0007829|PDB:4EDK"
FT HELIX 249..259
FT /evidence="ECO:0007829|PDB:4EDK"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:4EDK"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:4EDK"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:4EDK"
FT STRAND 286..288
FT /evidence="ECO:0007829|PDB:4EDK"
FT HELIX 292..299
FT /evidence="ECO:0007829|PDB:4EDK"
FT STRAND 303..308
FT /evidence="ECO:0007829|PDB:4EDK"
FT HELIX 313..328
FT /evidence="ECO:0007829|PDB:4EDK"
FT STRAND 332..336
FT /evidence="ECO:0007829|PDB:4EDK"
FT HELIX 344..351
FT /evidence="ECO:0007829|PDB:4EDK"
FT HELIX 353..362
FT /evidence="ECO:0007829|PDB:4EDK"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:4EDK"
FT HELIX 367..374
FT /evidence="ECO:0007829|PDB:4EDK"
FT HELIX 376..381
FT /evidence="ECO:0007829|PDB:4EDK"
FT HELIX 383..399
FT /evidence="ECO:0007829|PDB:4EDK"
FT HELIX 403..413
FT /evidence="ECO:0007829|PDB:4EDK"
FT HELIX 414..417
FT /evidence="ECO:0007829|PDB:4EDK"
FT HELIX 421..427
FT /evidence="ECO:0007829|PDB:4EDK"
SQ SEQUENCE 605 AA; 70002 MW; 199438C3484E0217 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 AQFDNLSRRE KAERAFLKHL
MRDKDTFLNY YESVDKDNFT NQHFKYVFEV LHDFYAENDQ YNISDAVQYV NSNELRETLI
SLEQYNLNGE PYENEIDDYV NVINEKGQET IESLNHKLRE ATRIGDVELQ KYYLQQIVAK
NKERM
