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Protein

DNA primase

Gene

dnaG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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
  • zinc ion binding Source: EcoliWiki

GO - Biological processi

  • DNA replication, synthesis of RNA primer Source: EcoliWiki

Keywordsi

Molecular functionDNA-binding, Nucleotidyltransferase, Transferase
Biological processDNA replication, Transcription
LigandMagnesium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:EG10239-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

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

Show more details

Protein-protein interaction databases

BioGridi4262146, 230 interactors
ComplexPortaliCPX-1933 DnaB-DnaG complex
DIPiDIP-47954N
IntActiP0ABS5, 17 interactors
STRINGi316385.ECDH10B_3241

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

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
OMAiRIMFPIY
PhylomeDBiP0ABS5

Family and domain databases

CDDicd03364 TOPRIM_DnaG_primases, 1 hit
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
InterProiView protein in InterPro
IPR016136 DNA_helicase_N/primase_C
IPR013264 DNA_primase_core_N
IPR037068 DNA_primase_core_N_sf
IPR019475 DNA_primase_DnaB-bd
IPR006295 DNA_primase_DnaG
IPR013173 DNA_primase_DnaG_DnaB-bd_dom
IPR036977 DNA_primase_Znf_CHC2
IPR030846 DnaG_bac
IPR034151 TOPRIM_DnaG_bac
IPR006171 TOPRIM_domain
IPR002694 Znf_CHC2
PfamiView protein in Pfam
PF10410 DnaB_bind, 1 hit
PF08278 DnaG_DnaB_bind, 1 hit
PF08275 Toprim_N, 1 hit
PF01807 zf-CHC2, 1 hit
PIRSFiPIRSF002811 DnaG, 1 hit
SMARTiView protein in SMART
SM00766 DnaG_DnaB_bind, 1 hit
SM00493 TOPRIM, 1 hit
SM00400 ZnF_CHCC, 1 hit
TIGRFAMsiTIGR01391 dnaG, 1 hit
PROSITEiView protein in PROSITE
PS50880 TOPRIM, 1 hit

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
PATRICifig|1411691.4.peg.3664

Similar proteinsi

Entry informationi

Entry nameiDNAG_ECOLI
AccessioniPrimary (citable) accession number: P0ABS5
Secondary accession number(s): P02922
, P02923, Q2M9D9, Q47613
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 20, 2018
This is version 111 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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