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 03-AUG-2022, entry version 158.
DE RecName: Full=DNA primase {ECO:0000255|HAMAP-Rule:MF_00974};
DE EC=2.7.7.101 {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; DOI=10.1016/s0021-9258(19)83630-x;
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.;
CC EC=2.7.7.101; Evidence={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}.
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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 AlphaFoldDB; P05096; -.
DR SASBDB; P05096; -.
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; BSU_25210.
DR GeneID; 937899; -.
DR KEGG; bsu:BSU25210; -.
DR PATRIC; fig|224308.179.peg.2741; -.
DR eggNOG; COG0358; Bacteria.
DR InParanoid; P05096; -.
DR OMA; LMWPIRD; -.
DR PhylomeDB; P05096; -.
DR BioCyc; BSUB:BSU25210-MON; -.
DR BRENDA; 2.7.7.101; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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: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; 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 BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="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:0007829|PDB:5GUJ"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:5GUJ"
FT TURN 147..149
FT /evidence="ECO:0007829|PDB:5GUJ"
FT HELIX 152..158
FT /evidence="ECO:0007829|PDB:5GUJ"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:5GUJ"
FT HELIX 169..176
FT /evidence="ECO:0007829|PDB:5GUJ"
FT HELIX 181..186
FT /evidence="ECO:0007829|PDB:5GUJ"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:5GUJ"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:5GUJ"
FT STRAND 205..212
FT /evidence="ECO:0007829|PDB:5GUJ"
FT STRAND 218..228
FT /evidence="ECO:0007829|PDB:5GUJ"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:5GUJ"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:5GUJ"
FT HELIX 251..261
FT /evidence="ECO:0007829|PDB:5GUJ"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:5GUJ"
FT HELIX 270..278
FT /evidence="ECO:0007829|PDB:5GUJ"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:5GUJ"
FT HELIX 294..303
FT /evidence="ECO:0007829|PDB:5GUJ"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:5GUJ"
FT HELIX 315..330
FT /evidence="ECO:0007829|PDB:5GUJ"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:5GUJ"
FT HELIX 346..353
FT /evidence="ECO:0007829|PDB:5GUJ"
FT HELIX 355..361
FT /evidence="ECO:0007829|PDB:5GUJ"
FT TURN 362..365
FT /evidence="ECO:0007829|PDB:5GUJ"
FT HELIX 369..376
FT /evidence="ECO:0007829|PDB:5GUJ"
FT TURN 377..380
FT /evidence="ECO:0007829|PDB:5GUJ"
FT HELIX 386..400
FT /evidence="ECO:0007829|PDB:5GUJ"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:5GUJ"
FT HELIX 406..420
FT /evidence="ECO:0007829|PDB:5GUJ"
FT HELIX 424..434
FT /evidence="ECO:0007829|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
