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Database: UniProt
Entry: DNAG_BACSU
LinkDB: DNAG_BACSU
Original site: DNAG_BACSU 
ID   DNAG_BACSU              Reviewed;         603 AA.
AC   P05096;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   08-MAY-2019, entry version 148.
DE   RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_00974};
DE            EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_00974};
GN   Name=dnaG {ECO:0000255|HAMAP-Rule:MF_00974}; Synonyms=dnaE;
GN   OrderedLocusNames=BSU25210;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3919021;
RA   Wang L.-F., Price C.W., Doi R.H.;
RT   "Bacillus subtilis dnaE encodes a protein homologous to DNA primase of
RT   Escherichia coli.";
RL   J. Biol. Chem. 260:3368-3372(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3086839; DOI=10.1093/nar/14.10.4293;
RA   Wang L.F., Doi R.H.;
RT   "Nucleotide sequence and organization of Bacillus subtilis RNA
RT   polymerase major sigma (sigma 43) operon.";
RL   Nucleic Acids Res. 14:4293-4307(1986).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of
RT   the Bacillus subtilis genome containing the skin element and many
RT   sporulation genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [5]
RP   SEQUENCE REVISION TO 274-275.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
RA   Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus
RT   subtilis 168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
CC   -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA
CC       molecules used as primers for DNA polymerase during DNA
CC       replication. {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-
CC       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-
CC       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.
CC       {ECO:0000255|HAMAP-Rule:MF_00974}.
DR   EMBL; M10040; AAA22406.1; -; Genomic_DNA.
DR   EMBL; X03897; CAA27537.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12488.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14451.2; -; Genomic_DNA.
DR   PIR; A22282; A22282.
DR   RefSeq; NP_390400.2; NC_000964.3.
DR   RefSeq; WP_003230066.1; NZ_JNCM01000036.1.
DR   PDB; 5GUJ; X-ray; 2.50 A; A=112-435.
DR   PDBsum; 5GUJ; -.
DR   SMR; P05096; -.
DR   DIP; DIP-46405N; -.
DR   IntAct; P05096; 12.
DR   STRING; 224308.BSU25210; -.
DR   PaxDb; P05096; -.
DR   PRIDE; P05096; -.
DR   EnsemblBacteria; CAB14451; CAB14451; BSU25210.
DR   GeneID; 937899; -.
DR   KEGG; bsu:BSU25210; -.
DR   PATRIC; fig|224308.179.peg.2741; -.
DR   eggNOG; ENOG4105C9G; Bacteria.
DR   eggNOG; COG0358; LUCA.
DR   HOGENOM; HOG000014483; -.
DR   InParanoid; P05096; -.
DR   KO; K02316; -.
DR   OMA; RIMFPIY; -.
DR   PhylomeDB; P05096; -.
DR   BioCyc; BSUB:BSU25210-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IBA:GO_Central.
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; 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; 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; 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; Complete proteome; DNA replication; DNA-binding;
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Primosome; Reference proteome; Transcription;
KW   Transferase; Zinc; Zinc-finger.
FT   CHAIN         1    603       DNA primase.
FT                                /FTId=PRO_0000180479.
FT   DOMAIN      262    343       Toprim. {ECO:0000255|HAMAP-
FT                                Rule:MF_00974}.
FT   ZN_FING      40     64       CHC2-type. {ECO:0000255|HAMAP-
FT                                Rule:MF_00974}.
FT   METAL       268    268       Magnesium 1; catalytic.
FT                                {ECO:0000255|HAMAP-Rule:MF_00974}.
FT   METAL       312    312       Magnesium 1; catalytic.
FT                                {ECO:0000255|HAMAP-Rule:MF_00974}.
FT   METAL       312    312       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00974}.
FT   METAL       314    314       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00974}.
FT   CONFLICT    274    275       IS -> YT (in Ref. 1; AAA22406, 2;
FT                                CAA27537 and 3; BAA12488). {ECO:0000305}.
FT   HELIX       113    134       {ECO:0000244|PDB:5GUJ}.
FT   HELIX       138    146       {ECO:0000244|PDB:5GUJ}.
FT   TURN        147    149       {ECO:0000244|PDB:5GUJ}.
FT   HELIX       152    158       {ECO:0000244|PDB:5GUJ}.
FT   STRAND      161    163       {ECO:0000244|PDB:5GUJ}.
FT   HELIX       169    176       {ECO:0000244|PDB:5GUJ}.
FT   HELIX       181    186       {ECO:0000244|PDB:5GUJ}.
FT   STRAND      189    192       {ECO:0000244|PDB:5GUJ}.
FT   STRAND      199    203       {ECO:0000244|PDB:5GUJ}.
FT   STRAND      205    212       {ECO:0000244|PDB:5GUJ}.
FT   STRAND      218    228       {ECO:0000244|PDB:5GUJ}.
FT   STRAND      230    235       {ECO:0000244|PDB:5GUJ}.
FT   TURN        244    246       {ECO:0000244|PDB:5GUJ}.
FT   HELIX       251    261       {ECO:0000244|PDB:5GUJ}.
FT   STRAND      263    269       {ECO:0000244|PDB:5GUJ}.
FT   HELIX       270    278       {ECO:0000244|PDB:5GUJ}.
FT   STRAND      283    290       {ECO:0000244|PDB:5GUJ}.
FT   HELIX       294    303       {ECO:0000244|PDB:5GUJ}.
FT   STRAND      305    309       {ECO:0000244|PDB:5GUJ}.
FT   HELIX       315    330       {ECO:0000244|PDB:5GUJ}.
FT   STRAND      334    337       {ECO:0000244|PDB:5GUJ}.
FT   HELIX       346    353       {ECO:0000244|PDB:5GUJ}.
FT   HELIX       355    361       {ECO:0000244|PDB:5GUJ}.
FT   TURN        362    365       {ECO:0000244|PDB:5GUJ}.
FT   HELIX       369    376       {ECO:0000244|PDB:5GUJ}.
FT   TURN        377    380       {ECO:0000244|PDB:5GUJ}.
FT   HELIX       386    400       {ECO:0000244|PDB:5GUJ}.
FT   STRAND      403    405       {ECO:0000244|PDB:5GUJ}.
FT   HELIX       406    420       {ECO:0000244|PDB:5GUJ}.
FT   HELIX       424    434       {ECO:0000244|PDB:5GUJ}.
SQ   SEQUENCE   603 AA;  68736 MW;  525D8631845C14AA CRC64;
     MGNRIPDEIV DQVQKSADIV EVIGDYVQLK KQGRNYFGLC PFHGESTPSF SVSPDKQIFH
     CFGCGAGGNV FSFLRQMEGY SFAESVSHLA DKYQIDFPDD ITVHSGARPE SSGEQKMAEA
     HELLKKFYHH LLINTKEGQE ALDYLLSRGF TKELINEFQI GYALDSWDFI TKFLVKRGFS
     EAQMEKAGLL IRREDGSGYF DRFRNRVMFP IHDHHGAVVA FSGRALGSQQ PKYMNSPETP
     LFHKSKLLYN FYKARLHIRK QERAVLFEGF ADVISAVSSD VKESIATMGT SLTDDHVKIL
     RRNVEEIILC YDSDKAGYEA TLKASELLQK KGCKVRVAMI PDGLDPDDYI KKFGGEKFKN
     DIIDASVTVM AFKMQYFRKG KNLSDEGDRL AYIKDVLKEI STLSGSLEQE VYVKQLASEF
     SLSQESLTEQ LSVFSKQNKP ADNSGETKTR RAHLTTKARQ KRLRPAYENA ERLLLAHMLR
     DRSVIKKVID RVGFQFNIDE HRALAAYLYA FYEEGAELTP QHLMARVTDD HISQLLSDIL
     MLQVNQELSE AELSDYVKKV LNQRNWSMIK EKEAERAEAE RQKDFLRAAS LAQEIVTLNR
     SLK
//
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