P27296 · DING_ECOLI

Function

function

DNA-dependent ATPase and 5'-3' DNA helicase (PubMed:12748189, PubMed:17416902, PubMed:25059658, PubMed:37537265).
Can also unwind DNA:RNA hybrid duplexes (PubMed:17416902).
Is active on D-loops, R-loops, and on forked structures (PubMed:17416902, PubMed:37537265).
Unwinds G-quadruplex DNA in a 5'-3' direction; unwinding efficiency differs on different substrates (PubMed:25059658, PubMed:37537265).
Does not appear to unwind replication forks or Holliday junctions (PubMed:25059658).
Translocates on single-stranded (ss)DNA with a 5'-3' polarity (PubMed:25059658).
In vitro at high concentrations also unwinds in a 3'-5' direction (PubMed:25059658).
May be involved in recombinational DNA repair and the resumption of replication after DNA damage (PubMed:17416902).
The [4Fe-4S] cluster is redox active at cellular potentials and is involved in DNA-mediated charge-transport signaling between DNA repair proteins from distinct pathways (PubMed:24738733).
DinG cooperates at long-range with endonuclease III, a base excision repair enzyme, using DNA charge transport to redistribute to regions of DNA damage (PubMed:24738733).
Binds 10-11 nucleotides of ssDNA in a positively-charged groove across the helicase domains (PubMed:30520735).

Catalytic activity

Cofactor

Protein has several cofactor binding sites:
[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 1 [4Fe-4S] cluster (PubMed:19074432, PubMed:30520735, PubMed:25059658).
The iron-sulfur cluster is essential for protein stability and helicase activity.
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: ATP-dependent DNA helicase activity requires divalent cations (Mg2+, Ca2+ or Mn2+) but is not detected in the presence of Zn2+ (PubMed:12748189).

Activity regulation

ATPase activity is 15-fold stimulated by single-stranded DNA (ssDNA). Reduction of the [4Fe-4S] cluster reversibly switches off helicase activity. Remains fully active after exposure to 100-fold excess of hydrogen peroxide, but the [4Fe-4S] cluster can be efficiently modified by nitric oxide (NO), forming the DinG-bound dinitrosyl iron complex with the concomitant inactivation of helicase activity (PubMed:19074432).
Helicase activity on G-quadruplex DNA is inhibited by porphyrin derivatives meso-tetra (N-methyl-4-pyridyl) porphine tetra tosylate (T4) and N-methyl mesoporphyrin IX (NMM) (PubMed:25059658).
Helicase activity on forked duplexes is not inhibited by T4 or NMM (PubMed:25059658).
G-quadruplex ligands such as Pyridostatin, PhenDC3, BRACO-19 and Netropsin can alter recognition and unwinding of G-quadruplex DNAs; the effect is both ligand- and G-quadruplex DNA-specific (PubMed:37537265).

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site26ATP (UniProtKB | ChEBI)
Binding site31ATP (UniProtKB | ChEBI)
Binding site60ATP (UniProtKB | ChEBI)
Binding site61ATP (UniProtKB | ChEBI)
Binding site120[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site194[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site199[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site205[4Fe-4S] cluster (UniProtKB | ChEBI)
Binding site599ATP (UniProtKB | ChEBI)
Binding site656ATP (UniProtKB | ChEBI)
Binding site659ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Function5'-3' DNA helicase activity
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionDNA binding
Molecular FunctionDNA helicase activity
Molecular FunctionDNA/RNA helicase activity
Molecular Functionisomerase activity
Molecular Functionmetal ion binding
Biological ProcessDNA duplex unwinding
Biological ProcessDNA repair
Biological ProcessG-quadruplex DNA unwinding
Biological ProcessSOS response

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent DNA helicase DinG
  • EC number
  • Alternative names
    • DNA 5'-3' helicase DinG

Gene names

    • Name
      dinG
    • Synonyms
      rarB
    • Ordered locus names
      b0799, JW0784

Organism names

  • Taxonomic identifier
  • Strains
    • K12 / W3110 / ATCC 27325 / DSM 5911
    • K12 / MG1655 / ATCC 47076
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia

Accessions

  • Primary accession
    P27296

Proteomes

Phenotypes & Variants

Disruption phenotype

Knockout results in a slight reduction of UV resistance (PubMed:12748189).
Knockout mutants are sensitive to very high levels of chain-terminating nucleoside analog 3' azidothymidine (AZT) (PubMed:26544712).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis117Significant decrease in helicase activity, small decrease in ssDNA binding.
Mutagenesis120Abolishes iron-sulfur-binding.
Mutagenesis194Abolishes iron-sulfur-binding.
Mutagenesis199Abolishes iron-sulfur-binding.
Mutagenesis205Abolishes iron-sulfur-binding.
Mutagenesis211Significant decrease in helicase activity, small decrease in ssDNA binding.
Mutagenesis615Loss of helicase activity, loss of ssDNA binding.
Mutagenesis618Loss of helicase activity, loss of ssDNA binding.
Mutagenesis636Loss of helicase activity, loss of ssDNA binding.
Mutagenesis638Loss of helicase activity, loss of ssDNA binding.
Mutagenesis673Loss of helicase activity, loss of ssDNA binding.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001019961-716ATP-dependent DNA helicase DinG

Proteomic databases

Expression

Induction

DNA damage-inducible. Transcriptionally regulated by LexA.

Interaction

Subunit

Monomer in solution (PubMed:12748189, PubMed:30520735).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY P27296ssb P0AGE02EBI-1114590, EBI-1118620

Protein-protein interaction databases

Chemistry

Family & Domains

Features

Showing features for region, domain, motif.

TypeIDPosition(s)Description
Region1-114HD1 domain N-terminus
Domain17-294Helicase ATP-binding
Region115-216[4Fe-4S] domain
Region217-261HD1 domain middle
Motif248-251DEAH box
Region262-438Arch domain
Region439-491HD1 domain middle
Region492-716HD2 domain

Domain

Has 4 domains; the discontinous helicase 1 (HD1), helicase 2 (HD2), arch and Fe-S cluster domains (PubMed:30520735).
The arch domain sits above the other domains and contacts the Fe-S cluster domain above the ssDNA-binding surface (PubMed:30520735).
Addition of an ATP analog to a DinG-ssDNA crystal induces changes in the relative orientation of the domains; HD1 remains tightly bound while HD2 slides along the DNA, upon ATP hydrolysis HD1 slides while HD2 remains tightly bound, thus the enzyme translocates in a 5'-3' direction along the ssDNA (Probable) (PubMed:30520735).

Sequence similarities

Belongs to the helicase family. DinG subfamily. Type 1 sub-subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    716
  • Mass (Da)
    81,440
  • Last updated
    1994-06-01 v3
  • Checksum
    63E6767E8EAA67D2
MALTAALKAQIAAWYKALQEQIPDFIPRAPQRQMIADVAKTLAGEEGRHLAIEAPTGVGKTLSYLIPGIAIAREEQKTLVVSTANVALQDQIYSKDLPLLKKIIPDLKFTAAFGRGRYVCPRNLTALASTEPTQQDLLAFLDDELTPNNQEEQKRCAKLKGDLDTYKWDGLRDHTDIAIDDDLWRRLSTDKASCLNRNCYYYRECPFFVARREIQEAEVVVANHALVMAAMESEAVLPDPKNLLLVLDEGHHLPDVARDALEMSAEITAPWYRLQLDLFTKLVATCMEQFRPKTIPPLAIPERLNAHCEELYELIASLNNILNLYMPAGQEAEHRFAMGELPDEVLEICQRLAKLTEMLRGLAELFLNDLSEKTGSHDIVRLHRLILQMNRALGMFEAQSKLWRLASLAQSSGAPVTKWATREEREGQLHLWFHCVGIRVSDQLERLLWRSIPHIIVTSATLRSLNSFSRLQEMSGLKEKAGDRFVALDSPFNHCEQGKIVIPRMRVEPSIDNEEQHIAEMAAFFRKQVESKKHLGMLVLFASGRAMQRFLDYVTDLRLMLLVQGDQPRYRLVELHRKRVANGERSVLVGLQSFAEGLDLKGDLLSQVHIHKIAFPPIDSPVVITEGEWLKSLNRYPFEVQSLPSASFNLIQQVGRLIRSHGCWGEVVIYDKRLLTKNYGKRLLDALPVFPIEQPEVPEGIVKKKEKTKSPRRRRR

Sequence caution

The sequence AAA23685.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict513in Ref. 2; AAA23685

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
L02123
EMBL· GenBank· DDBJ
AAA53655.1
EMBL· GenBank· DDBJ
Genomic DNA
M81935
EMBL· GenBank· DDBJ
AAA23685.1
EMBL· GenBank· DDBJ
Genomic DNA Different initiation
U00096
EMBL· GenBank· DDBJ
AAC73886.1
EMBL· GenBank· DDBJ
Genomic DNA
AP009048
EMBL· GenBank· DDBJ
BAA35465.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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