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Database: UniProt
Entry: P27296
LinkDB: P27296
Original site: P27296 
ID   DING_ECOLI              Reviewed;         716 AA.
AC   P27296;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 3.
DT   16-OCT-2019, entry version 150.
DE   RecName: Full=ATP-dependent DNA helicase DinG {ECO:0000255|HAMAP-Rule:MF_02205, ECO:0000305};
DE            EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_02205, ECO:0000269|PubMed:12748189, ECO:0000269|PubMed:17416902};
GN   Name=dinG {ECO:0000255|HAMAP-Rule:MF_02205,
GN   ECO:0000303|PubMed:1629168}; Synonyms=rarB;
GN   OrderedLocusNames=b0799, JW0784;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8037924; DOI=10.1266/jjg.69.1;
RA   Ohmori H.;
RT   "Structural analysis of the rhlE gene of Escherichia coli.";
RL   Jpn. J. Genet. 69:1-12(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX   PubMed=1629168; DOI=10.1128/jb.174.15.5110-5116.1992;
RA   Lewis L.K., Mount D.W.;
RT   "Interaction of LexA repressor with the asymmetric dinG operator and
RT   complete nucleotide sequence of the gene.";
RL   J. Bacteriol. 174:5110-5116(1992).
RN   [3]
RP   SEQUENCE REVISION.
RX   PubMed=8385320; DOI=10.1093/nar/21.6.1497;
RA   Koonin E.V.;
RT   "Escherichia coli dinG gene encodes a putative DNA helicase related to
RT   a group of eukaryotic helicases including Rad3 protein.";
RL   Nucleic Acids Res. 21:1497-1497(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBUNIT, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=12748189; DOI=10.1074/jbc.m301188200;
RA   Voloshin O.N., Vanevski F., Khil P.P., Camerini-Otero R.D.;
RT   "Characterization of the DNA damage-inducible helicase DinG from
RT   Escherichia coli.";
RL   J. Biol. Chem. 278:28284-28293(2003).
RN   [8]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=17416902; DOI=10.1074/jbc.m700376200;
RA   Voloshin O.N., Camerini-Otero R.D.;
RT   "The DinG protein from Escherichia coli is a structure-specific
RT   helicase.";
RL   J. Biol. Chem. 282:18437-18447(2007).
RN   [9]
RP   COFACTOR, IRON-SULFUR-BINDING, ACTIVITY REGULATION, AND MUTAGENESIS OF
RP   CYS-120; CYS-194; CYS-199 AND CYS-205.
RX   PubMed=19074432; DOI=10.1074/jbc.m807943200;
RA   Ren B., Duan X., Ding H.;
RT   "Redox control of the DNA damage-inducible protein DinG helicase
RT   activity via its iron-sulfur cluster.";
RL   J. Biol. Chem. 284:4829-4835(2009).
RN   [10]
RP   FUNCTION.
RX   PubMed=24738733; DOI=10.1021/ja501973c;
RA   Grodick M.A., Segal H.M., Zwang T.J., Barton J.K.;
RT   "DNA-mediated signaling by proteins with 4Fe-4S clusters is necessary
RT   for genomic integrity.";
RL   J. Am. Chem. Soc. 136:6470-6478(2014).
CC   -!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase
CC       (PubMed:12748189, PubMed:17416902). Can also unwind DNA-RNA hybrid
CC       duplexes. Is active on D-loops and R-loops, and on forked
CC       structures (PubMed:17416902). May be involved in recombinational
CC       DNA repair and the resumption of replication after DNA damage
CC       (PubMed:17416902). The redox cluster is involved in DNA-mediated
CC       charge-transport signaling between DNA repair proteins from
CC       distinct pathways. DinG cooperates at long-range with endonuclease
CC       III, a base excision repair enzyme, using DNA charge transport to
CC       redistribute to regions of DNA damage (PubMed:24738733).
CC       {ECO:0000269|PubMed:12748189, ECO:0000269|PubMed:17416902,
CC       ECO:0000269|PubMed:24738733}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02205,
CC         ECO:0000269|PubMed:12748189, ECO:0000269|PubMed:17416902};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02205,
CC         ECO:0000269|PubMed:19074432};
CC       Note=Binds 1 [4Fe-4S] cluster. The iron-sulfur cluster is
CC       essential for protein stability and helicase activity.
CC       {ECO:0000269|PubMed:19074432};
CC   -!- ACTIVITY REGULATION: ATPase activity is 15-fold stimulated by
CC       single-stranded DNA (ssDNA). ATP-dependent DNA helicase activity
CC       requires divalent cations (Mg(2+), Ca(2+) or Mn(2+)) but is not
CC       detected in the presence of Zn(2+) (PubMed:12748189). Reduction of
CC       the [4Fe-4S] cluster reversibly switches off helicase activity.
CC       Remains fully active after exposure to 100-fold excess of hydrogen
CC       peroxide, but the [4Fe-4S] cluster can be efficiently modified by
CC       nitric oxide (NO), forming the DinG-bound dinitrosyl iron complex
CC       with the concomitant inactivation of helicase activity
CC       (PubMed:19074432). {ECO:0000269|PubMed:12748189,
CC       ECO:0000269|PubMed:19074432}.
CC   -!- SUBUNIT: Monomer in solution. {ECO:0000269|PubMed:12748189}.
CC   -!- INTERACTION:
CC       P0AGE0:ssb; NbExp=2; IntAct=EBI-1114590, EBI-1118620;
CC   -!- INDUCTION: DNA damage-inducible. Transcriptionally regulated by
CC       LexA. {ECO:0000269|PubMed:1629168}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene results in a slight
CC       reduction of UV resistance. {ECO:0000269|PubMed:12748189}.
CC   -!- SIMILARITY: Belongs to the helicase family. DinG subfamily. Type 1
CC       sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_02205, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA23685.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
DR   EMBL; L02123; AAA53655.1; -; Genomic_DNA.
DR   EMBL; M81935; AAA23685.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC73886.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35465.1; -; Genomic_DNA.
DR   PIR; G64816; G64816.
DR   RefSeq; NP_415320.1; NC_000913.3.
DR   RefSeq; WP_001340191.1; NZ_STEB01000019.1.
DR   PDB; 6FWR; X-ray; 2.50 A; A=1-716.
DR   PDB; 6FWS; X-ray; 2.50 A; A/B=1-716.
DR   PDBsum; 6FWR; -.
DR   PDBsum; 6FWS; -.
DR   SMR; P27296; -.
DR   BioGrid; 4259964; 118.
DR   IntAct; P27296; 22.
DR   MINT; P27296; -.
DR   STRING; 511145.b0799; -.
DR   BindingDB; P27296; -.
DR   PaxDb; P27296; -.
DR   PRIDE; P27296; -.
DR   EnsemblBacteria; AAC73886; AAC73886; b0799.
DR   EnsemblBacteria; BAA35465; BAA35465; BAA35465.
DR   GeneID; 945431; -.
DR   KEGG; ecj:JW0784; -.
DR   KEGG; eco:b0799; -.
DR   PATRIC; fig|511145.12.peg.826; -.
DR   EchoBASE; EB1332; -.
DR   EcoGene; EG11357; dinG.
DR   eggNOG; ENOG4105DVT; Bacteria.
DR   eggNOG; COG1199; LUCA.
DR   HOGENOM; HOG000242573; -.
DR   InParanoid; P27296; -.
DR   KO; K03722; -.
DR   PhylomeDB; P27296; -.
DR   BioCyc; EcoCyc:EG11357-MONOMER; -.
DR   BioCyc; ECOL316407:JW0784-MONOMER; -.
DR   PRO; PR:P27296; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:EcoCyc.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATPase activity; IDA:EcoliWiki.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003678; F:DNA helicase activity; IDA:EcoCyc.
DR   GO; GO:0033677; F:DNA/RNA helicase activity; IDA:EcoCyc.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0032508; P:DNA duplex unwinding; IDA:EcoCyc.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0009432; P:SOS response; IEP:EcoCyc.
DR   HAMAP; MF_02205; DinG_proteobact; 1.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR   InterPro; IPR010614; DEAD_2.
DR   InterPro; IPR039000; DinG_proteobact.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR006554; Helicase-like_DEXD_c2.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF06733; DEAD_2; 1.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00488; DEXDc2; 1.
DR   SMART; SM00491; HELICc2; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; ATP-binding; Complete proteome; DNA damage;
KW   DNA recombination; DNA repair; DNA-binding; Helicase; Hydrolase; Iron;
KW   Iron-sulfur; Metal-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    716       ATP-dependent DNA helicase DinG.
FT                                /FTId=PRO_0000101996.
FT   DOMAIN       17    294       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_02205}.
FT   NP_BIND      54     61       ATP. {ECO:0000255|HAMAP-Rule:MF_02205}.
FT   MOTIF       248    251       DEAH box. {ECO:0000255|HAMAP-
FT                                Rule:MF_02205}.
FT   METAL       120    120       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_02205,
FT                                ECO:0000305|PubMed:19074432}.
FT   METAL       194    194       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_02205,
FT                                ECO:0000305|PubMed:19074432}.
FT   METAL       199    199       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_02205,
FT                                ECO:0000305|PubMed:19074432}.
FT   METAL       205    205       Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP-
FT                                Rule:MF_02205,
FT                                ECO:0000305|PubMed:19074432}.
FT   MUTAGEN     120    120       C->S: Abolishes iron-sulfur-binding.
FT                                {ECO:0000269|PubMed:19074432}.
FT   MUTAGEN     194    194       C->S: Abolishes iron-sulfur-binding.
FT                                {ECO:0000269|PubMed:19074432}.
FT   MUTAGEN     199    199       C->S: Abolishes iron-sulfur-binding.
FT                                {ECO:0000269|PubMed:19074432}.
FT   MUTAGEN     205    205       C->S: Abolishes iron-sulfur-binding.
FT                                {ECO:0000269|PubMed:19074432}.
FT   CONFLICT    513    513       N -> H (in Ref. 2; AAA23685).
FT                                {ECO:0000305}.
FT   HELIX         5     19       {ECO:0000244|PDB:6FWR}.
FT   HELIX        29     42       {ECO:0000244|PDB:6FWR}.
FT   STRAND       50     53       {ECO:0000244|PDB:6FWR}.
FT   HELIX        60     75       {ECO:0000244|PDB:6FWR}.
FT   STRAND       78     85       {ECO:0000244|PDB:6FWR}.
FT   HELIX        86     94       {ECO:0000244|PDB:6FWR}.
FT   HELIX        96    103       {ECO:0000244|PDB:6FWR}.
FT   STRAND      109    111       {ECO:0000244|PDB:6FWR}.
FT   HELIX       115    117       {ECO:0000244|PDB:6FWR}.
FT   HELIX       121    129       {ECO:0000244|PDB:6FWR}.
FT   HELIX       137    142       {ECO:0000244|PDB:6FWR}.
FT   HELIX       150    164       {ECO:0000244|PDB:6FWR}.
FT   HELIX       172    174       {ECO:0000244|PDB:6FWR}.
FT   HELIX       181    187       {ECO:0000244|PDB:6FWR}.
FT   TURN        191    193       {ECO:0000244|PDB:6FWR}.
FT   HELIX       196    198       {ECO:0000244|PDB:6FWR}.
FT   HELIX       202    204       {ECO:0000244|PDB:6FWR}.
FT   HELIX       206    215       {ECO:0000244|PDB:6FWR}.
FT   STRAND      218    223       {ECO:0000244|PDB:6FWR}.
FT   HELIX       224    232       {ECO:0000244|PDB:6FWR}.
FT   STRAND      235    237       {ECO:0000244|PDB:6FWS}.
FT   HELIX       240    242       {ECO:0000244|PDB:6FWR}.
FT   STRAND      243    247       {ECO:0000244|PDB:6FWR}.
FT   HELIX       250    252       {ECO:0000244|PDB:6FWR}.
FT   HELIX       253    258       {ECO:0000244|PDB:6FWR}.
FT   HELIX       259    261       {ECO:0000244|PDB:6FWR}.
FT   STRAND      262    266       {ECO:0000244|PDB:6FWR}.
FT   HELIX       269    289       {ECO:0000244|PDB:6FWR}.
FT   HELIX       297    299       {ECO:0000244|PDB:6FWR}.
FT   HELIX       301    323       {ECO:0000244|PDB:6FWR}.
FT   STRAND      332    335       {ECO:0000244|PDB:6FWR}.
FT   HELIX       337    339       {ECO:0000244|PDB:6FWR}.
FT   HELIX       343    372       {ECO:0000244|PDB:6FWR}.
FT   HELIX       379    407       {ECO:0000244|PDB:6FWR}.
FT   STRAND      416    424       {ECO:0000244|PDB:6FWR}.
FT   STRAND      426    438       {ECO:0000244|PDB:6FWR}.
FT   HELIX       441    447       {ECO:0000244|PDB:6FWR}.
FT   TURN        448    451       {ECO:0000244|PDB:6FWR}.
FT   STRAND      455    460       {ECO:0000244|PDB:6FWR}.
FT   HELIX       469    475       {ECO:0000244|PDB:6FWR}.
FT   TURN        479    482       {ECO:0000244|PDB:6FWR}.
FT   STRAND      484    487       {ECO:0000244|PDB:6FWR}.
FT   HELIX       494    497       {ECO:0000244|PDB:6FWR}.
FT   STRAND      498    501       {ECO:0000244|PDB:6FWR}.
FT   TURN        511    513       {ECO:0000244|PDB:6FWR}.
FT   HELIX       514    530       {ECO:0000244|PDB:6FWR}.
FT   STRAND      535    540       {ECO:0000244|PDB:6FWR}.
FT   HELIX       544    553       {ECO:0000244|PDB:6FWR}.
FT   HELIX       555    560       {ECO:0000244|PDB:6FWR}.
FT   STRAND      561    564       {ECO:0000244|PDB:6FWR}.
FT   HELIX       569    581       {ECO:0000244|PDB:6FWR}.
FT   STRAND      586    591       {ECO:0000244|PDB:6FWR}.
FT   HELIX       592    597       {ECO:0000244|PDB:6FWR}.
FT   HELIX       602    604       {ECO:0000244|PDB:6FWR}.
FT   STRAND      606    610       {ECO:0000244|PDB:6FWR}.
FT   HELIX       621    632       {ECO:0000244|PDB:6FWR}.
FT   HELIX       637    640       {ECO:0000244|PDB:6FWR}.
FT   HELIX       642    654       {ECO:0000244|PDB:6FWR}.
FT   STRAND      665    669       {ECO:0000244|PDB:6FWR}.
FT   HELIX       673    676       {ECO:0000244|PDB:6FWR}.
FT   HELIX       678    685       {ECO:0000244|PDB:6FWR}.
SQ   SEQUENCE   716 AA;  81440 MW;  63E6767E8EAA67D2 CRC64;
     MALTAALKAQ IAAWYKALQE QIPDFIPRAP QRQMIADVAK TLAGEEGRHL AIEAPTGVGK
     TLSYLIPGIA IAREEQKTLV VSTANVALQD QIYSKDLPLL KKIIPDLKFT AAFGRGRYVC
     PRNLTALAST EPTQQDLLAF LDDELTPNNQ EEQKRCAKLK GDLDTYKWDG LRDHTDIAID
     DDLWRRLSTD KASCLNRNCY YYRECPFFVA RREIQEAEVV VANHALVMAA MESEAVLPDP
     KNLLLVLDEG HHLPDVARDA LEMSAEITAP WYRLQLDLFT KLVATCMEQF RPKTIPPLAI
     PERLNAHCEE LYELIASLNN ILNLYMPAGQ EAEHRFAMGE LPDEVLEICQ RLAKLTEMLR
     GLAELFLNDL SEKTGSHDIV RLHRLILQMN RALGMFEAQS KLWRLASLAQ SSGAPVTKWA
     TREEREGQLH LWFHCVGIRV SDQLERLLWR SIPHIIVTSA TLRSLNSFSR LQEMSGLKEK
     AGDRFVALDS PFNHCEQGKI VIPRMRVEPS IDNEEQHIAE MAAFFRKQVE SKKHLGMLVL
     FASGRAMQRF LDYVTDLRLM LLVQGDQPRY RLVELHRKRV ANGERSVLVG LQSFAEGLDL
     KGDLLSQVHI HKIAFPPIDS PVVITEGEWL KSLNRYPFEV QSLPSASFNL IQQVGRLIRS
     HGCWGEVVIY DKRLLTKNYG KRLLDALPVF PIEQPEVPEG IVKKKEKTKS PRRRRR
//
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