ID DNAG_MYCTU Reviewed; 639 AA.
AC P9WNW1; L0TC89; P63962; P95239;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
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}; OrderedLocusNames=Rv2343c;
GN ORFNames=MTCY98.12c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011445;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4]
RP SUBUNIT.
RC STRAIN=H37Rv;
RX PubMed=32634279; DOI=10.1111/mmi.14571;
RA Zaveri A., Wang R., Botella L., Sharma R., Zhu L., Wallach J.B., Song N.,
RA Jansen R.S., Rhee K.Y., Ehrt S., Schnappinger D.;
RT "Depletion of the DarG antitoxin in Mycobacterium tuberculosis triggers the
RT DNA-damage response and leads to cell death.";
RL Mol. Microbiol. 114:641-652(2020).
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 (By similarity). Co-
CC immunoprecipitates with DarG in the presence and absence of darT
CC (PubMed:32634279). {ECO:0000255|HAMAP-Rule:MF_00974,
CC ECO:0000269|PubMed:32634279}.
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 -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC {ECO:0000269|PubMed:19099550}.
CC -!- SIMILARITY: Belongs to the DnaG primase family. {ECO:0000255|HAMAP-
CC Rule:MF_00974}.
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DR EMBL; AL123456; CCP45131.1; -; Genomic_DNA.
DR PIR; H70661; H70661.
DR RefSeq; NP_216859.1; NC_000962.3.
DR RefSeq; WP_003412049.1; NZ_NVQJ01000012.1.
DR PDB; 5W33; X-ray; 2.85 A; A=112-432.
DR PDB; 5W34; X-ray; 2.95 A; A/B=112-432.
DR PDB; 5W35; X-ray; 3.31 A; A/B=112-432.
DR PDB; 5W36; X-ray; 2.46 A; A/B=112-432.
DR PDBsum; 5W33; -.
DR PDBsum; 5W34; -.
DR PDBsum; 5W35; -.
DR PDBsum; 5W36; -.
DR AlphaFoldDB; P9WNW1; -.
DR SMR; P9WNW1; -.
DR STRING; 83332.Rv2343c; -.
DR PaxDb; 83332-Rv2343c; -.
DR DNASU; 885996; -.
DR GeneID; 885996; -.
DR KEGG; mtu:Rv2343c; -.
DR TubercuList; Rv2343c; -.
DR eggNOG; COG0358; Bacteria.
DR InParanoid; P9WNW1; -.
DR OrthoDB; 9803773at2; -.
DR PhylomeDB; P9WNW1; -.
DR BRENDA; 2.7.7.101; 3445.
DR Proteomes; UP000001584; 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:0005886; C:plasma membrane; HDA:MTBBASE.
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; 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; 3.40.1360.10; -; 1.
DR Gene3D; 3.90.980.10; DNA primase, catalytic core, N-terminal domain; 1.
DR Gene3D; 3.90.580.10; Zinc finger, CHC2-type domain; 1.
DR HAMAP; MF_00974; DNA_primase_DnaG; 1.
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; PF13662; Toprim_4; 1.
DR Pfam; PF01807; zf-CHC2; 1.
DR PIRSF; PIRSF002811; DnaG; 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; SSF57783; Zinc beta-ribbon; 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..639
FT /note="DNA primase"
FT /id="PRO_0000180506"
FT DOMAIN 262..348
FT /note="Toprim"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT ZN_FING 41..65
FT /note="CHC2-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT REGION 460..479
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 319
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 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT BINDING 321
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00974"
FT HELIX 114..131
FT /evidence="ECO:0007829|PDB:5W36"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:5W33"
FT HELIX 138..145
FT /evidence="ECO:0007829|PDB:5W36"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:5W36"
FT HELIX 151..156
FT /evidence="ECO:0007829|PDB:5W36"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:5W36"
FT STRAND 164..167
FT /evidence="ECO:0007829|PDB:5W36"
FT HELIX 168..175
FT /evidence="ECO:0007829|PDB:5W36"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:5W36"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:5W36"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:5W36"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:5W36"
FT STRAND 215..222
FT /evidence="ECO:0007829|PDB:5W36"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:5W36"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:5W36"
FT HELIX 251..261
FT /evidence="ECO:0007829|PDB:5W36"
FT STRAND 263..266
FT /evidence="ECO:0007829|PDB:5W36"
FT HELIX 270..278
FT /evidence="ECO:0007829|PDB:5W36"
FT STRAND 284..290
FT /evidence="ECO:0007829|PDB:5W36"
FT HELIX 294..304
FT /evidence="ECO:0007829|PDB:5W36"
FT TURN 305..309
FT /evidence="ECO:0007829|PDB:5W36"
FT STRAND 313..321
FT /evidence="ECO:0007829|PDB:5W36"
FT HELIX 322..330
FT /evidence="ECO:0007829|PDB:5W36"
FT STRAND 333..335
FT /evidence="ECO:0007829|PDB:5W36"
FT TURN 337..341
FT /evidence="ECO:0007829|PDB:5W36"
FT STRAND 342..346
FT /evidence="ECO:0007829|PDB:5W36"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:5W36"
FT HELIX 353..370
FT /evidence="ECO:0007829|PDB:5W36"
FT HELIX 375..384
FT /evidence="ECO:0007829|PDB:5W36"
FT HELIX 392..407
FT /evidence="ECO:0007829|PDB:5W36"
FT HELIX 412..426
FT /evidence="ECO:0007829|PDB:5W36"
SQ SEQUENCE 639 AA; 69593 MW; E5A4887F2357C833 CRC64;
MSGRISDRDI AAIREGARIE DVVGDYVQLR RAGADSLKGL CPFHNEKSPS FHVRPNHGHF
HCFGCGEGGD VYAFIQKIEH VSFVEAVELL ADRIGHTISY TGAATSVQRD RGSRSRLLAA
NAAAAAFYAQ ALQSDEAAPA RQYLTERSFD AAAARKFGCG FAPSGWDSLT KHLQRKGFEF
EELEAAGLSR QGRHGPMDRF HRRLLWPIRT SAGEVVGFGA RRLFDDDAME AKYVNTPETL
LYKKSSVMFG IDLAKRDIAK GHQAVVVEGY TDVMAMHLAG VTTAVASCGT AFGGEHLAML
RRLMMDDSFF RGELIYVFDG DEAGRAAALK AFDGEQKLAG QSFVAVAPDG MDPCDLRLKC
GDAALRDLVA RRTPLFEFAI RAAIAEMDLD SAEGRVAALR RCVPMVGQIK DPTLRDEYAR
QLAGWVGWAD VAQVIGRVRG EAKRTKHPRL GRLGSTTIAR AAQRPTAGPP TELAVRPDPR
DPTLWPQREA LKSALQYPAL AGPVFDALTV EGFTHPEYAA VRAAIDTAGG TSAGLSGAQW
LDMVRQQTTS TVTSALISEL GVEAIQVDDD KLPRYIAGVL ARLQEVWLGR QIAEVKSKLQ
RMSPIEQGDE YHALFGDLVA MEAYRRSLLE QASGDDLTA
//
