hda inibitor of reinitiation of DNA replication [Escherichia coli str. K-12 substr. MG1655] - Gene

Summary

Go to the top of the page Help

Official Symbol: hda
Official Full Name: inibitor of reinitiation of DNA replication
Primary source: ECOCYC:G7313
Locus tag: b2496
See related: ASAP:ABE-0008217
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: ECK2492; idaB; yfgE
Summary: hda is a DnaA paralog. [More information is available at EcoGene: EG14201]. IdaB is a member of the AAA chaperone-like family of ATPases that is required for the inhibition of the initiation of DNA synthesis via antagonism of DnaA activity by the DNA polymerase III beta subunit (sliding clamp) . [More information is available at EcoCyc: G7313].
NEW: Try the new Gene table
Try the new Transcript table

Genomic context

Go to the top of the page Help

Sequence:: NC_000913.3 (2618075..2618776, complement)

NC_000913.3 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

Go to the top of the page Help

Go to reference sequence details

Genomic Sequence:: NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

Go to the top of the page Help

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

structural and mutational analyses of the Hda-beta clamp complex indicate that the interaction of the beta clamp with Hda controls the ability of Hda to interact with DnaA.
Title: Dynamic assembly of Hda and the sliding clamp in the regulation of replication licensing.
results establish a model in which interaction between DnaA Asn-44 and Hda stabilizes the association between the AAA+ domains of DnaA and Hda to facilitate DnaA-ATP hydrolysis during RIDA(regulatory inactivation of DnaA)
Title: The DnaA N-terminal domain interacts with Hda to facilitate replicase clamp-mediated inactivation of DnaA.
Taken together, these findings suggest that although one or more Hda functions are essential for cell viability, regulatory inactivation of DnaA may be dispensable.
Title: Evidence for roles of the Escherichia coli Hda protein beyond regulatory inactivation of DnaA.
functional DnaA-Hda interactions require a second interaction site within DnaA domain IV in addition to the AAA+ domain
Title: DnaA protein DNA-binding domain binds to Hda protein to promote inter-AAA+ domain interaction involved in regulatory inactivation of DnaA.
Here, the authors demonstrate that direct and functional interaction of ADP-Hda with DnaA requires the Hda residues Ser-152, Phe-118 and Asn-122 as well as Hda Arg-153 and DnaA Arg-334.
Title: Novel essential residues of Hda for interaction with DnaA in the regulatory inactivation of DnaA: unique roles for Hda AAA Box VI and VII motifs.
Hda monomerization by ADP binding promotes replicase clamp-mediated DnaA-ATP hydrolysis
Title: Hda monomerization by ADP binding promotes replicase clamp-mediated DnaA-ATP hydrolysis.
Mutations that reduce initiation frequency from oriC suppress the growth defect of Hda-deficient cells.
Title: Loss of Hda activity stimulates replication initiation from I-box, but not R4 mutant origins in Escherichia coli.
The presence of genes encoding a previously unpublished adhesin termed Hda was found in several EAEC strains isolated from Denmark, suggesting that this adhesin represents an important variant in the Afa/Dr/AAF family.
Title: New adhesin of enteroaggregative Escherichia coli related to the Afa/Dr/AAF family.
data suggest the model: DnaA-ATP is hydrolyzed at a binding interface between the AAA(+) domains of DnaA and Hda; the DnaA N-terminal domain supports this interaction; the interaction of DnaA-ATP with the Hda-clamp complex occurs in a catalytic mode
Title: Protein associations in DnaA-ATP hydrolysis mediated by the Hda-replicase clamp complex.
Overexpression of the Hda DnaA-related protein in Escherichia coli inhibits multiplication, affects membrane permeability, and induces the SOS response.
Title: Overexpression of the Hda DnaA-related protein in Escherichia coli inhibits multiplication, affects membrane permeability, and induces the SOS response.

Submit: New GeneRIF Correction See all GeneRIFs (12)

Interactions

Go to the top of the page Help

Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

Go to the top of the page Help

Gene Ontology Provided by EcoCyc

Function	Evidence Code	Pubs
enables ADP binding	IDA Inferred from Direct Assay more info	PubMed
enables identical protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables nucleotide binding	IEA Inferred from Electronic Annotation more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in DNA replication	IBA Inferred from Biological aspect of Ancestor more info
involved_in DNA replication	IEA Inferred from Electronic Annotation more info
involved_in DNA replication initiation	IBA Inferred from Biological aspect of Ancestor more info
involved_in negative regulation of DNA replication	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of DNA-templated DNA replication initiation	IBA Inferred from Biological aspect of Ancestor more info
involved_in negative regulation of DNA-templated DNA replication initiation	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within negative regulation of DNA-templated DNA replication initiation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of DNA-templated DNA replication initiation	NAS Non-traceable Author Statement more info	PubMed
involved_in regulation of DNA-templated DNA replication initiation	NAS Non-traceable Author Statement more info	PubMed

Component	Evidence Code	Pubs
part_of Hda-beta clamp complex	IPI Inferred from Physical Interaction more info	PubMed
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in membrane	IDA Inferred from Direct Assay more info	PubMed
located_in plasma membrane	IEA Inferred from Electronic Annotation more info
part_of replication inhibiting complex	IPI Inferred from Physical Interaction more info	PubMed