Probable ATP-dependent helicase DinG - Escherichia coli (strain K12)

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P27296 (DING_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 104. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Probable ATP-dependent helicase DinG
EC=3.6.4.12

Alternative name(s):
DNA-damage-inducible protein G

Gene names

Name:	dinG
Synonyms:	rarB
Ordered Locus Names:	b0799, JW0784

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	716 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable helicase involved in DNA repair and perhaps also replication. Ref.3
Catalytic activity	ATP + H₂O = ADP + phosphate.
Cofactor	Binds 1 4Fe-4S cluster. Ref.7
Domain	4Fe-4S iron-sulfur-binding is required for protein stability and helicase activity. The cluster is modified by nitric oxide, forming the DinG-bound dinitrosyl iron complex with the inactivation of helicase activity (Ref.7).
Sequence similarities	Belongs to the helicase family. DinG subfamily. Contains 1 helicase ATP-binding domain.
Sequence caution	The sequence AAA23685.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair
Ligand	4Fe-4S ATP-binding DNA-binding Iron Iron-sulfur Metal-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW DNA repair Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent DNA helicase activity Inferred from direct assay PubMed 12748189. Source: EcoCyc DNA binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 716

716

Probable ATP-dependent helicase DinG

PRO_0000101996

Regions

Domain

17 – 294

278

Helicase ATP-binding

Nucleotide binding

54 – 61

ATP Probable

Motif

248 – 251

DEGH box

Sites

Metal binding

120

Iron-sulfur (4Fe-4S) By similarity

Metal binding

194

Iron-sulfur (4Fe-4S) By similarity

Metal binding

199

Iron-sulfur (4Fe-4S) By similarity

Metal binding

205

Iron-sulfur (4Fe-4S) By similarity

Experimental info

Mutagenesis

120

C → S: Abolishes iron-sulfur-binding. Ref.7

Mutagenesis

194

C → S: Abolishes iron-sulfur-binding. Ref.7

Mutagenesis

199

C → S: Abolishes iron-sulfur-binding. Ref.7

Mutagenesis

205

C → S: Abolishes iron-sulfur-binding. Ref.7

Sequence conflict

513

N → H in AAA23685. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P27296 [UniParc].

Last modified June 1, 1994. Version 3.
Checksum: 63E6767E8EAA67D2
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FASTA

716

81,440

        10         20         30         40         50         60 
MALTAALKAQ IAAWYKALQE QIPDFIPRAP QRQMIADVAK TLAGEEGRHL AIEAPTGVGK 

        70         80         90        100        110        120 
TLSYLIPGIA IAREEQKTLV VSTANVALQD QIYSKDLPLL KKIIPDLKFT AAFGRGRYVC 

       130        140        150        160        170        180 
PRNLTALAST EPTQQDLLAF LDDELTPNNQ EEQKRCAKLK GDLDTYKWDG LRDHTDIAID 

       190        200        210        220        230        240 
DDLWRRLSTD KASCLNRNCY YYRECPFFVA RREIQEAEVV VANHALVMAA MESEAVLPDP 

       250        260        270        280        290        300 
KNLLLVLDEG HHLPDVARDA LEMSAEITAP WYRLQLDLFT KLVATCMEQF RPKTIPPLAI 

       310        320        330        340        350        360 
PERLNAHCEE LYELIASLNN ILNLYMPAGQ EAEHRFAMGE LPDEVLEICQ RLAKLTEMLR 

       370        380        390        400        410        420 
GLAELFLNDL SEKTGSHDIV RLHRLILQMN RALGMFEAQS KLWRLASLAQ SSGAPVTKWA 

       430        440        450        460        470        480 
TREEREGQLH LWFHCVGIRV SDQLERLLWR SIPHIIVTSA TLRSLNSFSR LQEMSGLKEK 

       490        500        510        520        530        540 
AGDRFVALDS PFNHCEQGKI VIPRMRVEPS IDNEEQHIAE MAAFFRKQVE SKKHLGMLVL 

       550        560        570        580        590        600 
FASGRAMQRF LDYVTDLRLM LLVQGDQPRY RLVELHRKRV ANGERSVLVG LQSFAEGLDL 

       610        620        630        640        650        660 
KGDLLSQVHI HKIAFPPIDS PVVITEGEWL KSLNRYPFEV QSLPSASFNL IQQVGRLIRS 

       670        680        690        700        710 
HGCWGEVVIY DKRLLTKNYG KRLLDALPVF PIEQPEVPEG IVKKKEKTKS PRRRRR

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural analysis of the rhlE gene of Escherichia coli." Ohmori H. Jpn. J. Genet. 69:1-12(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"Interaction of LexA repressor with the asymmetric dinG operator and complete nucleotide sequence of the gene." Lewis L.K., Mount D.W. J. Bacteriol. 174:5110-5116(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Escherichia coli dinG gene encodes a putative DNA helicase related to a group of eukaryotic helicases including Rad3 protein." Koonin E.V. Nucleic Acids Res. 21:1497-1497(1993) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION, PROBABLE FUNCTION.
[4]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"Redox control of the DNA damage-inducible protein DinG helicase activity via its iron-sulfur cluster." Ren B., Duan X., Ding H. J. Biol. Chem. 284:4829-4835(2009) [PubMed] [Europe PMC] [Abstract] Cited for: COFACTOR, IRON-SULFUR-BINDING, MUTAGENESIS OF CYS-120; CYS-194; CYS-199 AND CYS-205.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	G64816.
RefSeq	NP_415320.1. NC_000913.2. YP_489072.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P27296.
SMR	P27296. Positions 24-94.
ModBase	Search...
Protein-protein interaction databases
IntAct	P27296. 21 interactions.
STRING	511145.b0799.
Proteomic databases
PRIDE	P27296.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73886; AAC73886; b0799. BAA35465; BAA35465; BAA35465.
GeneID	12930970. 945431.
KEGG	ecj:Y75_p0772. eco:b0799.
PATRIC	32116801. VBIEscCol129921_0826.
Organism-specific databases
EchoBASE	EB1332.
EcoGene	EG11357. dinG.
Phylogenomic databases
eggNOG	COG1199.
HOGENOM	HOG000242573.
KO	K03722.
OMA	HCAGIRV.
ProtClustDB	PRK11747.
Enzyme and pathway databases
BioCyc	EcoCyc:EG11357-MONOMER. ECOL316407:JW0784-MONOMER.
Gene expression databases
Genevestigator	P27296.
Family and domain databases
InterPro	IPR006555. ATP-dep_Helicase_C. IPR010614. DEAD_2. IPR011545. DNA/RNA_helicase_DEAD/DEAH_N. IPR014013. Helic_SF1/SF2_ATP-bd_DinG/Rad3. IPR014001. Helicase_ATP-bd. [Graphical view]
Pfam	PF00270. DEAD. 1 hit. PF06733. DEAD_2. 1 hit. PF13307. Helicase_C_2. 1 hit. [Graphical view]
SMART	SM00487. DEXDc. 1 hit. SM00491. HELICc2. 1 hit. [Graphical view]
PROSITE	PS51193. HELICASE_ATP_BIND_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DING_ECOLI

Accession

Primary (citable) accession number: P27296

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	June 1, 1994
Last modified:	May 1, 2013
This is version 104 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents