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Database: UniProt
Entry: S3K6H4_9ENTR
LinkDB: S3K6H4_9ENTR
Original site: S3K6H4_9ENTR 
ID   S3K6H4_9ENTR            Unreviewed;       584 AA.
AC   S3K6H4;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   RecName: Full=DNA primase {ECO:0000256|HAMAP-Rule:MF_00974};
DE            EC=2.7.7.101 {ECO:0000256|HAMAP-Rule:MF_00974};
GN   Name=dnaG {ECO:0000256|HAMAP-Rule:MF_00974};
GN   ORFNames=HMPREF0201_00396 {ECO:0000313|EMBL:EPF20664.1};
OS   Cedecea davisae DSM 4568.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cedecea.
OX   NCBI_TaxID=566551 {ECO:0000313|EMBL:EPF20664.1, ECO:0000313|Proteomes:UP000014585};
RN   [1] {ECO:0000313|EMBL:EPF20664.1, ECO:0000313|Proteomes:UP000014585}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4568 {ECO:0000313|EMBL:EPF20664.1,
RC   ECO:0000313|Proteomes:UP000014585};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Palsikar V.B., Zhang X., Suruliraj S., Perna N.T., Plunkett G.,
RA   Warren W., Mitreva M., Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2013) 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}.
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:0000256|HAMAP-Rule:MF_00974};
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}.
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:EPF20664.1}.
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DR   EMBL; ATDT01000003; EPF20664.1; -; Genomic_DNA.
DR   AlphaFoldDB; S3K6H4; -.
DR   STRING; 566551.HMPREF0201_00396; -.
DR   PATRIC; fig|566551.4.peg.366; -.
DR   HOGENOM; CLU_013501_5_1_6; -.
DR   Proteomes; UP000014585; Unassembled WGS sequence.
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; 3.40.1360.10; -; 1.
DR   Gene3D; 3.90.980.10; DNA primase, catalytic core, N-terminal domain; 1.
DR   Gene3D; 1.20.50.20; DnaG, RNA polymerase domain, helical bundle; 1.
DR   Gene3D; 3.90.580.10; Zinc finger, CHC2-type domain; 1.
DR   HAMAP; MF_00974; DNA_primase_DnaG; 1.
DR   InterPro; IPR016136; DNA_helicase_N/primase_C.
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; IPR013264; DNAG_N.
DR   InterPro; IPR034151; TOPRIM_DnaG_bac.
DR   InterPro; IPR006171; TOPRIM_domain.
DR   InterPro; IPR002694; Znf_CHC2.
DR   NCBIfam; TIGR01391; dnaG; 1.
DR   PANTHER; PTHR30313; DNA PRIMASE; 1.
DR   PANTHER; PTHR30313:SF2; DNA PRIMASE; 1.
DR   Pfam; PF10410; DnaB_bind; 1.
DR   Pfam; PF08278; DnaG_DnaB_bind; 1.
DR   Pfam; PF08275; DNAG_N; 1.
DR   Pfam; PF13155; Toprim_2; 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   SUPFAM; SSF56731; DNA primase core; 1.
DR   SUPFAM; SSF117023; DNA primase DnaG, C-terminal domain; 1.
DR   SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR   PROSITE; PS50880; TOPRIM; 1.
PE   3: Inferred from homology;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|HAMAP-Rule:MF_00974};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|HAMAP-Rule:MF_00974};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00974};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00974};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|HAMAP-
KW   Rule:MF_00974}.
FT   DOMAIN          262..344
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   ZN_FING         43..67
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00974"
SQ   SEQUENCE   584 AA;  65249 MW;  316CF4538DBAD4C4 CRC64;
     MGPMAGRIPR VFINDLIART DIVDLIDARV KLKKQGKNYH ACCPFHNEKT PSFTVNGDKQ
     FYHCFGCGAH GNALDFLMNY DKLEFVESVE ELATMHNLEV PYEAGNGPSQ IERHQRQSLY
     QLMDGLNAFY QQSLKLPAAE PARQYLGKRG LSDEVIAHFA IGYAPPGWDN ALKRFGGNSE
     NRQALTDAGM LVTNDKGRSY DRFRERVMFP IRDKRGRVIG FGGRVLGDGM PKYLNSPETD
     IFHKGRQLYG LYEAQQSQPE PARLLVVEGY MDVVALAQYG ISYAVASLGT STTADHIQLL
     FRVTDNVVCC YDGDRAGRDA AWRALETALP YMTDGRQLRF MFLPDGEDPD TLVRKEGKEA
     FETRMEQAQP LSTFLFNSLM PQVDLSTPDG RARLSTLALP LISQVPGETL RIYLRQQLGN
     KLGILDDSQL EKLMPKQVDG VTPRPAPQLK RTTMRILIGL LVQNPELAPL VPPLSGLDAA
     KLPGLTLFSD LVNACLAQPG LTTGQLLEQY RGTNEAATLE KLSAWDDIAD REIAEKTFTD
     SLDHLFDSAL ELRFEELMAR SRTEGLTPAE REEVRVITES RAKK
//
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