dnaG [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

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Official Symbol: dnaG
Primary source: ECOCYC:EG10239
Locus tag: b3066
See related: ASAP:ABE-0010065
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage: Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as: dnaP; ECK3056; parB; sdgA
Summary: DNA primase catalyzes the synthesis of RNA primers on single-stranded template DNA . [More information is available at EcoCyc: EG10239].
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Genomic context

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Sequence:: NC_000913.3 (3211107..3212852)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Metabolic cofactors NADH and FAD act as non-canonical initiating substrates for a primase and affect replication primer processing in vitro.
Title: Metabolic cofactors NADH and FAD act as non-canonical initiating substrates for a primase and affect replication primer processing in vitro.
we propose that DnaC controls the ability of DnaB to interact with primase by modifying the conformation of the N-terminal domain of DnaB
Title: DnaC, the indispensable companion of DnaB helicase, controls the accessibility of DnaB helicase by primase.
Cooperative base pair melting by helicase and polymerase positioned one nucleotide from each other.
Title: Cooperative base pair melting by helicase and polymerase positioned one nucleotide from each other.
This study identifies the C-terminal helicase-binding domain of DnaG primase (DnaG-C) and the highly conserved C-terminal region of single-stranded DNA-binding protein as interaction sites.
Title: The helicase-binding domain of Escherichia coli DnaG primase interacts with the highly conserved C-terminal region of single-stranded DNA-binding protein.
ParB complexes P1 plasmids, ParA-ATP stimulates this interaction and ParA-ADP inhibits ParB pairing activity in a parS-independent manner.
Title: ParAB-mediated intermolecular association of plasmid P1 parS sites.
A single-molecule analysis of the replication kinetics with varying DnaG concentrations indicates that a cooperative binding of two or three DnaG monomers to DnaB halts synthesis by Pol III.
Title: Single-molecule studies of fork dynamics in Escherichia coli DNA replication.
The structure reveals an unanticipated binding site that engages nucleic acid in two distinct configurations, indicating that it serves as a nonspecific capture and tracking locus for template DNA.
Title: Identification of a DNA primase template tracking site redefines the geometry of primer synthesis.
N-terminus verified by Edman degradation on mature peptide
Title: Sequences of the Escherichia coli dnaG primase gene and regulation of its expression.
analysis of centromere pairing by a plasmid-encoded type I ParB protein
Title: Centromere pairing by a plasmid-encoded type I ParB protein.
essential for IncP-9 plasmid pM3 replication
Title: Ability of IncP-9 plasmid pM3 to replicate in Escherichia coli is dependent on both rep and par functions.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables DNA binding	IEA Inferred from Electronic Annotation more info
enables DNA primase activity	IBA Inferred from Biological aspect of Ancestor more info
enables DNA primase activity	IDA Inferred from Direct Assay more info	PubMed
enables DNA primase activity	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IEA Inferred from Electronic Annotation more info
enables nucleotidyltransferase activity	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables zinc ion binding	IDA Inferred from Direct Assay more info	PubMed
enables zinc ion binding	IEA Inferred from Electronic Annotation more info

Process	Evidence Code	Pubs
involved_in DNA replication	IEA Inferred from Electronic Annotation more info
involved_in DNA replication, synthesis of primer	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within DNA replication, synthesis of primer	IDA Inferred from Direct Assay more info	PubMed
involved_in DNA replication, synthesis of primer	IDA Inferred from Direct Assay more info	PubMed
involved_in DNA replication, synthesis of primer	IEA Inferred from Electronic Annotation more info
involved_in DNA replication, synthesis of primer	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in DNA replication, synthesis of primer	NAS Non-traceable Author Statement more info	PubMed
involved_in DNA unwinding involved in DNA replication	NAS Non-traceable Author Statement more info	PubMed
involved_in replication fork processing	NAS Non-traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
part_of DNA-directed RNA polymerase complex	IEA Inferred from Electronic Annotation more info
part_of DnaB-DnaG complex	IPI Inferred from Physical Interaction more info	PubMed
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
part_of primosome complex	IEA Inferred from Electronic Annotation more info
part_of primosome complex	NAS Non-traceable Author Statement more info	PubMed
part_of replisome	NAS Non-traceable Author Statement more info	PubMed

General protein information

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Preferred Names: DNA primase

NP_417538.1

EC 2.7.7.101

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

NC_000913.3 Reference assembly

Range

3211107..3212852

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

NP_417538.1 DNA primase [Escherichia coli str. K-12 substr. MG1655]

See identical proteins and their annotated locations for NP_417538.1

Status: PROVISIONAL

UniProtKB/TrEMBL

A0A5C9AFV3

Conserved Domains (1) summary

PRK05667
Location:2 → 581

dnaG; DNA primase; Validated