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Database: UniProt
Entry: A0A0A3Z6C6_9GAMM
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ID   A0A0A3Z6C6_9GAMM        Unreviewed;       581 AA.
AC   A0A0A3Z6C6;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   11-DEC-2019, entry version 28.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00993443};
DE            EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00993444};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974,
GN   ECO:0000313|EMBL:KGT94622.1};
GN   ORFNames=NG99_08405 {ECO:0000313|EMBL:KGT94622.1};
OS   Erwinia typographi.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=371042 {ECO:0000313|EMBL:KGT94622.1, ECO:0000313|Proteomes:UP000030351};
RN   [1] {ECO:0000313|EMBL:KGT94622.1, ECO:0000313|Proteomes:UP000030351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M043b {ECO:0000313|EMBL:KGT94622.1,
RC   ECO:0000313|Proteomes:UP000030351};
RA   Chan K.-G., Tan W.-S.;
RT   "Genome sequence of Erwinia typographi M043b.";
RL   Submitted (OCT-2014) 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:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00709340}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00709317};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00974};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-Rule:MF_00974};
CC   -!- SUBUNIT: Monomer. Interacts with DnaB. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00974}.
CC   -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00974, ECO:0000256|SAAS:SAAS00709351}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGT94622.1}.
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DR   EMBL; JRUQ01000027; KGT94622.1; -; Genomic_DNA.
DR   RefSeq; WP_034890767.1; NZ_JRUQ01000027.1.
DR   STRING; 371042.NG99_08405; -.
DR   EnsemblBacteria; KGT94622; KGT94622; NG99_08405.
DR   OrthoDB; 1071997at2; -.
DR   BioCyc; GCF_000773975:G1EJM-1492-MONOMER; -.
DR   Proteomes; UP000030351; Unassembled WGS sequence.
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; IPR013173; DNA_primase_DnaG_DnaB-bd_dom.
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; PF08278; DnaG_DnaB_bind; 1.
DR   Pfam; PF08275; Toprim_N; 1.
DR   Pfam; PF01807; zf-CHC2; 1.
DR   SMART; SM00766; DnaG_DnaB_bind; 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 {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00740714};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00740674};
KW   DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709327}; Magnesium {ECO:0000256|SAAS:SAAS00709345};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709338};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709339, ECO:0000313|EMBL:KGT94622.1};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00709304};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709341};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00993442, ECO:0000313|EMBL:KGT94622.1};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|SAAS:SAAS00709300};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709301}.
FT   DOMAIN          259..341
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   ZN_FING         40..64
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00974"
SQ   SEQUENCE   581 AA;  65387 MW;  13A14E55F8D0A2EA CRC64;
     MAGRIPRVFI NDLLARTDIV DLIDARVKLK KQGKNYHACC PFHNEKTPSF TVNGEKQFYH
     CFGCGAHGNA VDFLMNYDRL EFVESIEELA TLYGLEVPYE SGTGPSQLER HQRQSLYQLM
     GGLSEFYQQA LSQSQASGAR DYLAKRGLSD AVIKHFSIGY APAGWDNALK RFGRNQDDRQ
     SLIDAGMLVT NDQGRSYDRF RDRVMFPIHD KRGRVIGFGG RVLGDAVPKY LNSPETDIFH
     KGRQLYGLFE AQKNHPEPSK LLVVEGYMDV VALAQFGIDY AVASLGTSTT PEHIQLLFRT
     TDSVICCYDG DRAGREAAWR ALETALPYMN DGRQLRFMFL PDGEDPDTLV RKEGKEAFEA
     RMEQAMPLSA FLFDSLLPQV DLRSPDGRAQ LSTLALPLIS QVPGETLRIY LRQELGNKLG
     ILDDSQLEKL MPKQGENAKP PQQPQLKRTT MRILIGLLIQ NPALANMVPP LDGLQASELA
     GFPLFVELVN TCVAHPGLTT GQLLELYRGT KFSQSLENLA TWNHMIVEDE VETMFKDSLA
     SMYDAALERR LEELIARDRT HVLNAEERRE FWTLSQALAK K
//
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