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Database: UniProt
Entry: N6ULX0_9RHIZ
LinkDB: N6ULX0_9RHIZ
Original site: N6ULX0_9RHIZ 
ID   N6ULX0_9RHIZ            Unreviewed;       645 AA.
AC   N6ULX0;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   10-APR-2019, entry version 42.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993443};
DE            EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993444};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974,
GN   ECO:0000313|EMBL:ENN91213.1};
GN   ORFNames=BBbe_09080 {ECO:0000313|EMBL:ENN91213.1};
OS   Bartonella bovis 91-4.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=1094491 {ECO:0000313|EMBL:ENN91213.1, ECO:0000313|Proteomes:UP000014038};
RN   [1] {ECO:0000313|EMBL:ENN91213.1, ECO:0000313|Proteomes:UP000014038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91-4 {ECO:0000313|EMBL:ENN91213.1,
RC   ECO:0000313|Proteomes:UP000014038};
RX   PubMed=23555299; DOI=10.1371/journal.pgen.1003393;
RA   Guy L., Nystedt B., Toft C., Zaremba-Niedzwiedzka K., Berglund E.C.,
RA   Granberg F., Naslund K., Eriksson A.S., Andersson S.G.;
RT   "A gene transfer agent and a dynamic repertoire of secretion systems
RT   hold the keys to the explosive radiation of the emerging pathogen
RT   Bartonella.";
RL   PLoS Genet. 9:E1003393-E1003393(2013).
CC   -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC       molecules used as primers for DNA polymerase during DNA
CC       replication. {ECO:0000256|HAMAP-Rule:MF_00974,
CC       ECO:0000256|PIRNR:PIRNR002811, 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; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC         ECO:0000256|PIRSR:PIRSR002811-1};
CC       Note=Binds 1 zinc ion per monomer. {ECO:0000256|HAMAP-
CC       Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC       ECO:0000256|PIRSR:PIRSR002811-1};
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.
CC       {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
CC       ECO:0000256|SAAS:SAAS00709351}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ENN91213.1}.
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DR   EMBL; AGWA01000007; ENN91213.1; -; Genomic_DNA.
DR   STRING; 1094491.BBbe_09080; -.
DR   EnsemblBacteria; ENN91213; ENN91213; BBbe_09080.
DR   PATRIC; fig|1094491.5.peg.982; -.
DR   Proteomes; UP000014038; Chromosome.
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; 3.90.580.10; -; 1.
DR   Gene3D; 3.90.980.10; -; 1.
DR   HAMAP; MF_00974; DNA_primase_DnaG; 1.
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; PF13662; Toprim_4; 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   Complete proteome {ECO:0000313|Proteomes:UP000014038};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993445};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|SAAS:SAAS00709369};
KW   DNA-directed RNA polymerase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709327};
KW   Magnesium {ECO:0000256|SAAS:SAAS00709345};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|PIRSR:PIRSR002811-1,
KW   ECO:0000256|SAAS:SAAS00709338};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709339};
KW   Primosome {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709304};
KW   Transcription {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00709341};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRNR:PIRNR002811, ECO:0000256|SAAS:SAAS00993442};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00974, ECO:0000256|PIRNR:PIRNR002811,
KW   ECO:0000256|PIRSR:PIRSR002811-1, ECO:0000256|SAAS:SAAS00709300};
KW   Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00974,
KW   ECO:0000256|PIRSR:PIRSR002811-1, ECO:0000256|SAAS:SAAS00709301}.
FT   DOMAIN      267    349       Toprim. {ECO:0000259|PROSITE:PS50880}.
FT   ZN_FING      43     67       CHC2-type. {ECO:0000256|HAMAP-Rule:
FT                                MF_00974, ECO:0000256|PIRSR:PIRSR002811-
FT                                1}.
SQ   SEQUENCE   645 AA;  74427 MW;  9A4FD5338FF314E0 CRC64;
     MRFPPDFLDE IRSRLPISTV ISQRVTFDPQ KSKPARGDFW FCCPFHGEKT PSFHCNDRKG
     CYYCFGCGVS GDIFTFLCKF DGLQFLEAVE RLADLAGMKL PLLDPQSHER EMQRASLYDV
     MGIAADFFQS SLHDKGGEQA RYYLNERGVT PELIKRFRIG FAPAGRTALK EMLSTHGISI
     KQMEDCGLLI SGEDVVVPYD RFRNRIIFPI EDLRGRVVAF GGRSLDKNMR AKYLNSPETV
     LFHKGNMLYN AASARKSNHS MREEKARSIL VVEGYMDVIA LTKAGFEKVV APLGTALTEE
     QIALLWQIEP DCVFCFDGDD AGLKAAFRVA DRVLPLLRVG VSVRFILLPQ GKDPDEIVRA
     GGVSLFDSFL QKSMPLIELL WWRATYGQRF ETPETRAALE RRLKQEIFTI KDEDVRRYYF
     QDIKKRLYDF FCPPFLKKKN VGGYDRNQKD EMFKRHSFSI LENSDMVRNL PHSIPLREAV
     ILLILAHYPD LCYENFEVLS ELELKNTELI NFHQSMLEIL GSQQIHDKTI MITLLEEKGQ
     KAILERMRNL VQSVGMRTTF TKAPIKDARA VLKQAIYLHL REHHLHKRLQ DIEEQLMKNP
     NNEVFDLLRE TKTELEQMRA TEALIEGFGC WFDEETDEIK PNEIK
//
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