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Protein

ATP-dependent DNA helicase DinG

Gene

dinG

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

Functioni

DNA-dependent ATPase and 5'-3' DNA helicase (PubMed:12748189, PubMed:17416902). Can also unwind DNA-RNA hybrid duplexes. Is active on D-loops and R-loops, and on forked structures (PubMed:17416902). May be involved in recombinational DNA repair and the resumption of replication after DNA damage (PubMed:17416902). The redox cluster is involved in DNA-mediated charge-transport signaling between DNA repair proteins from distinct pathways. 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).3 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.UniRule annotation2 Publications

Cofactori

[4Fe-4S] clusterUniRule annotation1 PublicationNote: Binds 1 [4Fe-4S] cluster. The iron-sulfur cluster is essential for protein stability and helicase activity.1 Publication

Enzyme regulationi

ATPase activity is 15-fold stimulated by single-stranded DNA (ssDNA). ATP-dependent DNA helicase activity requires divalent cations (Mg2+, Ca2+ or Mn2+) but is not detected in the presence of Zn2+ (PubMed:12748189). 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).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi120Iron-sulfur (4Fe-4S)UniRule annotation1 Publication1
Metal bindingi194Iron-sulfur (4Fe-4S)UniRule annotation1 Publication1
Metal bindingi199Iron-sulfur (4Fe-4S)UniRule annotation1 Publication1
Metal bindingi205Iron-sulfur (4Fe-4S)UniRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi54 – 61ATPUniRule annotation8

GO - Molecular functioni

  • 4 iron, 4 sulfur cluster binding Source: EcoCyc
  • ATPase activity Source: EcoliWiki
  • ATP binding Source: UniProtKB-KW
  • ATP-dependent DNA/RNA helicase activity Source: EcoCyc
  • ATP-dependent DNA helicase activity Source: EcoCyc
  • DNA binding Source: UniProtKB-KW
  • DNA helicase activity Source: EcoliWiki
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • DNA duplex unwinding Source: EcoCyc
  • DNA recombination Source: UniProtKB-KW
  • DNA repair Source: UniProtKB-KW
  • SOS response Source: EcoCyc

Keywordsi

Molecular functionDNA-binding, Helicase, Hydrolase
Biological processDNA damage, DNA recombination, DNA repair
Ligand4Fe-4S, ATP-binding, Iron, Iron-sulfur, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11357-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent DNA helicase DinGUniRule annotationCurated (EC:3.6.4.12UniRule annotation2 Publications)
Gene namesi
Name:dinG1 PublicationUniRule annotation
Synonyms:rarB
Ordered Locus Names:b0799, JW0784
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11357 dinG

Pathology & Biotechi

Disruption phenotypei

Deletion of the gene results in a slight reduction of UV resistance.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi120C → S: Abolishes iron-sulfur-binding. 1 Publication1
Mutagenesisi194C → S: Abolishes iron-sulfur-binding. 1 Publication1
Mutagenesisi199C → S: Abolishes iron-sulfur-binding. 1 Publication1
Mutagenesisi205C → S: Abolishes iron-sulfur-binding. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001019961 – 716ATP-dependent DNA helicase DinGAdd BLAST716

Proteomic databases

PaxDbiP27296
PRIDEiP27296

Expressioni

Inductioni

DNA damage-inducible. Transcriptionally regulated by LexA.1 Publication

Interactioni

Subunit structurei

Monomer in solution.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ssbP0AGE02EBI-1114590,EBI-1118620

Protein-protein interaction databases

BioGridi4259964, 118 interactors
IntActiP27296, 22 interactors
MINTiP27296
STRINGi316385.ECDH10B_0867

Chemistry databases

BindingDBiP27296

Structurei

3D structure databases

ProteinModelPortaliP27296
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini17 – 294Helicase ATP-bindingUniRule annotationAdd BLAST278

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi248 – 251DEAH boxUniRule annotation4

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105DVT Bacteria
COG1199 LUCA
HOGENOMiHOG000242573
InParanoidiP27296
KOiK03722
OMAiLIICSHD
PhylomeDBiP27296

Family and domain databases

HAMAPiMF_02205 DinG_proteobact, 1 hit
InterProiView protein in InterPro
IPR006555 ATP-dep_Helicase_C
IPR011545 DEAD/DEAH_box_helicase_dom
IPR010614 DEAD_2
IPR039000 DinG_proteobact
IPR014013 Helic_SF1/SF2_ATP-bd_DinG/Rad3
IPR006554 Helicase-like_DEXD_c2
IPR014001 Helicase_ATP-bd
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF00270 DEAD, 1 hit
PF06733 DEAD_2, 1 hit
PF13307 Helicase_C_2, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00488 DEXDc2, 1 hit
SM00491 HELICc2, 1 hit
SUPFAMiSSF52540 SSF52540, 4 hits
PROSITEiView protein in PROSITE
PS51193 HELICASE_ATP_BIND_2, 1 hit

Sequencei

Sequence statusi: Complete.

P27296-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALTAALKAQ IAAWYKALQE QIPDFIPRAP QRQMIADVAK TLAGEEGRHL
60 70 80 90 100
AIEAPTGVGK TLSYLIPGIA IAREEQKTLV VSTANVALQD QIYSKDLPLL
110 120 130 140 150
KKIIPDLKFT AAFGRGRYVC PRNLTALAST EPTQQDLLAF LDDELTPNNQ
160 170 180 190 200
EEQKRCAKLK GDLDTYKWDG LRDHTDIAID DDLWRRLSTD KASCLNRNCY
210 220 230 240 250
YYRECPFFVA RREIQEAEVV VANHALVMAA MESEAVLPDP KNLLLVLDEG
260 270 280 290 300
HHLPDVARDA LEMSAEITAP WYRLQLDLFT KLVATCMEQF RPKTIPPLAI
310 320 330 340 350
PERLNAHCEE LYELIASLNN ILNLYMPAGQ EAEHRFAMGE LPDEVLEICQ
360 370 380 390 400
RLAKLTEMLR GLAELFLNDL SEKTGSHDIV RLHRLILQMN RALGMFEAQS
410 420 430 440 450
KLWRLASLAQ SSGAPVTKWA TREEREGQLH LWFHCVGIRV SDQLERLLWR
460 470 480 490 500
SIPHIIVTSA TLRSLNSFSR LQEMSGLKEK AGDRFVALDS PFNHCEQGKI
510 520 530 540 550
VIPRMRVEPS IDNEEQHIAE MAAFFRKQVE SKKHLGMLVL FASGRAMQRF
560 570 580 590 600
LDYVTDLRLM LLVQGDQPRY RLVELHRKRV ANGERSVLVG LQSFAEGLDL
610 620 630 640 650
KGDLLSQVHI HKIAFPPIDS PVVITEGEWL KSLNRYPFEV QSLPSASFNL
660 670 680 690 700
IQQVGRLIRS HGCWGEVVIY DKRLLTKNYG KRLLDALPVF PIEQPEVPEG
710
IVKKKEKTKS PRRRRR
Length:716
Mass (Da):81,440
Last modified:June 1, 1994 - v3
Checksum:i63E6767E8EAA67D2
GO

Sequence cautioni

The sequence AAA23685 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti513N → H in AAA23685 (PubMed:1629168).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02123 Genomic DNA Translation: AAA53655.1
M81935 Genomic DNA Translation: AAA23685.1 Different initiation.
U00096 Genomic DNA Translation: AAC73886.1
AP009048 Genomic DNA Translation: BAA35465.1
PIRiG64816
RefSeqiNP_415320.1, NC_000913.3
WP_001340191.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73886; AAC73886; b0799
BAA35465; BAA35465; BAA35465
GeneIDi945431
KEGGiecj:JW0784
eco:b0799
PATRICifig|511145.12.peg.826

Similar proteinsi

Entry informationi

Entry nameiDING_ECOLI
AccessioniPrimary (citable) accession number: P27296
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: June 1, 1994
Last modified: May 23, 2018
This is version 139 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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