(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 149.
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 polymerase
RT   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 the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   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., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., 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., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., 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., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   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 replication.
CC       {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}.
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;
DR   PRODOM; P05096.
DR   SWISS-2DPAGE; P05096.
KW   3D-structure; DNA replication; DNA-binding; DNA-directed RNA polymerase;
KW   Magnesium; Metal-binding; Nucleotidyltransferase; Primosome;
KW   Reference proteome; Transcription; Transferase; Zinc; Zinc-finger.
FT   CHAIN           1..603
FT                   /note="DNA primase"
FT                   /id="PRO_0000180479"
FT   DOMAIN          262..343
FT                   /note="Toprim"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   ZN_FING         40..64
FT                   /note="CHC2-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   METAL           268
FT                   /note="Magnesium 1; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   METAL           312
FT                   /note="Magnesium 1; catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   METAL           312
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   METAL           314
FT                   /note="Magnesium 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT   CONFLICT        274..275
FT                   /note="IS -> YT (in Ref. 1; AAA22406, 2; CAA27537 and 3;
FT                   BAA12488)"
FT                   /evidence="ECO:0000305"
FT   HELIX           113..134
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   HELIX           138..146
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   TURN            147..149
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   HELIX           152..158
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   STRAND          161..163
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   HELIX           169..176
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   HELIX           181..186
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   STRAND          189..192
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   STRAND          199..203
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   STRAND          205..212
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   STRAND          218..228
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   STRAND          230..235
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   TURN            244..246
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   HELIX           251..261
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   STRAND          263..269
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   HELIX           270..278
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   STRAND          283..290
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   HELIX           294..303
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   STRAND          305..309
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   HELIX           315..330
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   STRAND          334..337
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   HELIX           346..353
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   HELIX           355..361
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   TURN            362..365
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   HELIX           369..376
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   TURN            377..380
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   HELIX           386..400
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   STRAND          403..405
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   HELIX           406..420
FT                   /evidence="ECO:0000244|PDB:5GUJ"
FT   HELIX           424..434
FT                   /evidence="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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