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Protein

DNA primase

Gene

dnaG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.UniRule annotation2 Publications

Cofactori

Protein has several cofactor binding sites:
  • Zn2+UniRule annotation2 PublicationsNote: Binds 1 zinc ion per monomer.UniRule annotation2 Publications
  • Mg2+UniRule annotationNote: Binds two Mg2+ per subunit.UniRule annotation

Enzyme regulationi

Activity can be regulated by an intermolecular trans association between the zinc-binding domain and the catalytic core domain of two different primase molecules.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi265Magnesium 1; catalyticUniRule annotation1
Metal bindingi309Magnesium 1; catalyticUniRule annotation1
Metal bindingi309Magnesium 2UniRule annotation1
Metal bindingi311Magnesium 2UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri40 – 64CHC2-typeUniRule annotationAdd BLAST25

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • DNA primase activity Source: EcoliWiki
  • magnesium ion binding Source: UniProtKB-HAMAP
  • zinc ion binding Source: EcoliWiki

GO - Biological processi

  • DNA replication, synthesis of RNA primer Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication, Transcription

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG10239-MONOMER.
ECOL316407:JW3038-MONOMER.
MetaCyc:EG10239-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA primaseUniRule annotation (EC:2.7.7.-UniRule annotation)
Gene namesi
Name:dnaGUniRule annotation
Synonyms:dnaP, parB
Ordered Locus Names:b3066, JW3038
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10239. dnaG.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • primosome complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Primosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi165W → A: Abolishes DNA-binding and primer synthesis. 1 Publication1
Mutagenesisi199R → A: Abolishes primer synthesis but can still bind DNA. Abolishes DNA-binding; when associated with A-201. 1 Publication1
Mutagenesisi201R → A: Abolishes primer synthesis but can still bind DNA. Abolishes DNA-binding; when associated with A-199. 1 Publication1
Mutagenesisi576Q → A: Decreases interaction with DnaB and primase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001804901 – 581DNA primaseAdd BLAST581

Proteomic databases

PaxDbiP0ABS5.
PRIDEiP0ABS5.

Interactioni

Subunit structurei

Monomer. Interacts with DnaB. The primase-helicase complex is composed of up to three DnaG bound to one DnaB hexamer.UniRule annotation6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
dnaBP0ACB03EBI-549259,EBI-548978
ssbP0AGE02EBI-549259,EBI-1118620

Protein-protein interaction databases

BioGridi4262146. 193 interactors.
DIPiDIP-47954N.
IntActiP0ABS5. 17 interactors.
MINTiMINT-1222307.
STRINGi511145.b3066.

Structurei

Secondary structure

1581
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi116 – 131Combined sources16
Helixi134 – 136Combined sources3
Helixi137 – 145Combined sources9
Helixi150 – 156Combined sources7
Beta strandi159 – 161Combined sources3
Beta strandi163 – 165Combined sources3
Helixi167 – 172Combined sources6
Helixi176 – 184Combined sources9
Beta strandi187 – 190Combined sources4
Beta strandi196 – 199Combined sources4
Beta strandi202 – 209Combined sources8
Beta strandi211 – 213Combined sources3
Beta strandi215 – 225Combined sources11
Beta strandi229 – 232Combined sources4
Turni241 – 243Combined sources3
Helixi248 – 253Combined sources6
Beta strandi261 – 266Combined sources6
Helixi267 – 275Combined sources9
Beta strandi281 – 283Combined sources3
Beta strandi285 – 288Combined sources4
Helixi291 – 300Combined sources10
Beta strandi302 – 311Combined sources10
Helixi312 – 325Combined sources14
Helixi326 – 328Combined sources3
Beta strandi334 – 340Combined sources7
Helixi346 – 362Combined sources17
Helixi368 – 376Combined sources9
Helixi377 – 379Combined sources3
Helixi385 – 399Combined sources15
Helixi405 – 419Combined sources15
Helixi424 – 427Combined sources4
Helixi448 – 460Combined sources13
Helixi462 – 467Combined sources6
Turni472 – 474Combined sources3
Helixi476 – 478Combined sources3
Helixi482 – 493Combined sources12
Helixi500 – 505Combined sources6
Turni507 – 509Combined sources3
Helixi510 – 512Combined sources3
Helixi513 – 540Combined sources28
Turni541 – 543Combined sources3
Helixi544 – 558Combined sources15
Turni559 – 561Combined sources3
Helixi565 – 577Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DD9X-ray1.60A111-433[»]
1DDEX-ray1.70A111-433[»]
1EQNX-ray2.90A/B/C/D/E111-429[»]
1T3WX-ray2.80A/B434-581[»]
2HAJNMR-A434-581[»]
3B39X-ray2.35A/B111-429[»]
ProteinModelPortaliP0ABS5.
SMRiP0ABS5.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABS5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini259 – 341ToprimUniRule annotationAdd BLAST83

Domaini

Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.UniRule annotation3 Publications

Sequence similaritiesi

Belongs to the DnaG primase family.UniRule annotation
Contains 1 Toprim domain.UniRule annotation

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri40 – 64CHC2-typeUniRule annotationAdd BLAST25

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiENOG4105C9G. Bacteria.
COG0358. LUCA.
HOGENOMiHOG000014483.
InParanoidiP0ABS5.
KOiK02316.
OMAiEHYRGTK.
PhylomeDBiP0ABS5.

Family and domain databases

Gene3Di1.10.860.10. 1 hit.
3.90.580.10. 1 hit.
3.90.980.10. 1 hit.
HAMAPiMF_00974. DNA_primase_DnaG. 1 hit.
InterProiIPR016136. DNA_helicase_N/primase_C.
IPR013264. DNA_primase_core_N.
IPR019475. DNA_primase_DnaB-bd.
IPR006295. DNA_primase_DnaG.
IPR013173. DNA_primase_DnaG_DnaB-bd_dom.
IPR030846. DnaG_bac.
IPR006171. Toprim_domain.
IPR002694. Znf_CHC2.
[Graphical view]
PfamiPF10410. DnaB_bind. 1 hit.
PF08278. DnaG_DnaB_bind. 1 hit.
PF08275. Toprim_N. 1 hit.
PF01807. zf-CHC2. 1 hit.
[Graphical view]
PIRSFiPIRSF002811. DnaG. 1 hit.
SMARTiSM00766. DnaG_DnaB_bind. 1 hit.
SM00493. TOPRIM. 1 hit.
SM00400. ZnF_CHCC. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01391. dnaG. 1 hit.
PROSITEiPS50880. TOPRIM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ABS5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGRIPRVFI NDLLARTDIV DLIDARVKLK KQGKNFHACC PFHNEKTPSF
60 70 80 90 100
TVNGEKQFYH CFGCGAHGNA IDFLMNYDKL EFVETVEELA AMHNLEVPFE
110 120 130 140 150
AGSGPSQIER HQRQTLYQLM DGLNTFYQQS LQQPVATSAR QYLEKRGLSH
160 170 180 190 200
EVIARFAIGF APPGWDNVLK RFGGNPENRQ SLIDAGMLVT NDQGRSYDRF
210 220 230 240 250
RERVMFPIRD KRGRVIGFGG RVLGNDTPKY LNSPETDIFH KGRQLYGLYE
260 270 280 290 300
AQQDNAEPNR LLVVEGYMDV VALAQYGINY AVASLGTSTT ADHIQLLFRA
310 320 330 340 350
TNNVICCYDG DRAGRDAAWR ALETALPYMT DGRQLRFMFL PDGEDPDTLV
360 370 380 390 400
RKEGKEAFEA RMEQAMPLSA FLFNSLMPQV DLSTPDGRAR LSTLALPLIS
410 420 430 440 450
QVPGETLRIY LRQELGNKLG ILDDSQLERL MPKAAESGVS RPVPQLKRTT
460 470 480 490 500
MRILIGLLVQ NPELATLVPP LENLDENKLP GLGLFRELVN TCLSQPGLTT
510 520 530 540 550
GQLLEHYRGT NNAATLEKLS MWDDIADKNI AEQTFTDSLN HMFDSLLELR
560 570 580
QEELIARERT HGLSNEERLE LWTLNQELAK K
Length:581
Mass (Da):65,565
Last modified:July 21, 1986 - v1
Checksum:i294CF020E7B45D94
GO

Sequence cautioni

The sequence CAA23531 differs from that shown. Reason: Frameshift at positions 106 and 169.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti24D → N in CAA23636 (PubMed:6222240).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01687 Genomic DNA. Translation: AAA24600.1.
V00274 Genomic DNA. Translation: CAA23531.1. Frameshift.
U28379 Genomic DNA. Translation: AAA89146.1.
U00096 Genomic DNA. Translation: AAC76102.1.
AP009048 Genomic DNA. Translation: BAE77117.1.
V00346 Genomic DNA. Translation: CAA23636.1.
PIRiA03423. RYEC2.
RefSeqiNP_417538.1. NC_000913.3.
WP_000918827.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76102; AAC76102; b3066.
BAE77117; BAE77117; BAE77117.
GeneIDi947570.
KEGGiecj:JW3038.
eco:b3066.
PATRICi32121546. VBIEscCol129921_3160.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J01687 Genomic DNA. Translation: AAA24600.1.
V00274 Genomic DNA. Translation: CAA23531.1. Frameshift.
U28379 Genomic DNA. Translation: AAA89146.1.
U00096 Genomic DNA. Translation: AAC76102.1.
AP009048 Genomic DNA. Translation: BAE77117.1.
V00346 Genomic DNA. Translation: CAA23636.1.
PIRiA03423. RYEC2.
RefSeqiNP_417538.1. NC_000913.3.
WP_000918827.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DD9X-ray1.60A111-433[»]
1DDEX-ray1.70A111-433[»]
1EQNX-ray2.90A/B/C/D/E111-429[»]
1T3WX-ray2.80A/B434-581[»]
2HAJNMR-A434-581[»]
3B39X-ray2.35A/B111-429[»]
ProteinModelPortaliP0ABS5.
SMRiP0ABS5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4262146. 193 interactors.
DIPiDIP-47954N.
IntActiP0ABS5. 17 interactors.
MINTiMINT-1222307.
STRINGi511145.b3066.

Proteomic databases

PaxDbiP0ABS5.
PRIDEiP0ABS5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76102; AAC76102; b3066.
BAE77117; BAE77117; BAE77117.
GeneIDi947570.
KEGGiecj:JW3038.
eco:b3066.
PATRICi32121546. VBIEscCol129921_3160.

Organism-specific databases

EchoBASEiEB0235.
EcoGeneiEG10239. dnaG.

Phylogenomic databases

eggNOGiENOG4105C9G. Bacteria.
COG0358. LUCA.
HOGENOMiHOG000014483.
InParanoidiP0ABS5.
KOiK02316.
OMAiEHYRGTK.
PhylomeDBiP0ABS5.

Enzyme and pathway databases

BioCyciEcoCyc:EG10239-MONOMER.
ECOL316407:JW3038-MONOMER.
MetaCyc:EG10239-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP0ABS5.
PROiP0ABS5.

Family and domain databases

Gene3Di1.10.860.10. 1 hit.
3.90.580.10. 1 hit.
3.90.980.10. 1 hit.
HAMAPiMF_00974. DNA_primase_DnaG. 1 hit.
InterProiIPR016136. DNA_helicase_N/primase_C.
IPR013264. DNA_primase_core_N.
IPR019475. DNA_primase_DnaB-bd.
IPR006295. DNA_primase_DnaG.
IPR013173. DNA_primase_DnaG_DnaB-bd_dom.
IPR030846. DnaG_bac.
IPR006171. Toprim_domain.
IPR002694. Znf_CHC2.
[Graphical view]
PfamiPF10410. DnaB_bind. 1 hit.
PF08278. DnaG_DnaB_bind. 1 hit.
PF08275. Toprim_N. 1 hit.
PF01807. zf-CHC2. 1 hit.
[Graphical view]
PIRSFiPIRSF002811. DnaG. 1 hit.
SMARTiSM00766. DnaG_DnaB_bind. 1 hit.
SM00493. TOPRIM. 1 hit.
SM00400. ZnF_CHCC. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01391. dnaG. 1 hit.
PROSITEiPS50880. TOPRIM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDNAG_ECOLI
AccessioniPrimary (citable) accession number: P0ABS5
Secondary accession number(s): P02922
, P02923, Q2M9D9, Q47613
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.