DING_ECOL6
ID DING_ECOL6 Reviewed; 716 AA.
AC Q8FJN1;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=ATP-dependent DNA helicase DinG {ECO:0000255|HAMAP-Rule:MF_02205};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_02205};
GN Name=dinG {ECO:0000255|HAMAP-Rule:MF_02205}; OrderedLocusNames=c0883;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase.
CC {ECO:0000255|HAMAP-Rule:MF_02205}.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02205};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_02205};
CC -!- SIMILARITY: Belongs to the helicase family. DinG subfamily. Type 1 sub-
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_02205}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014075; AAN79356.1; -; Genomic_DNA.
DR RefSeq; WP_001218658.1; NC_004431.1.
DR AlphaFoldDB; Q8FJN1; -.
DR SMR; Q8FJN1; -.
DR STRING; 199310.c0883; -.
DR EnsemblBacteria; AAN79356; AAN79356; c0883.
DR KEGG; ecc:c0883; -.
DR eggNOG; COG1199; Bacteria.
DR HOGENOM; CLU_012117_4_1_6; -.
DR OMA; PRRAQNY; -.
DR BioCyc; ECOL199310:C0883-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.300; -; 2.
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; IPR045028; DinG/Rad3-like.
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 PANTHER; PTHR11472; PTHR11472; 1.
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.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; ATP-binding; DNA-binding; Helicase; Hydrolase; Iron; Iron-sulfur;
KW Metal-binding; Nucleotide-binding.
FT CHAIN 1..716
FT /note="ATP-dependent DNA helicase DinG"
FT /id="PRO_0000101998"
FT DOMAIN 17..294
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02205"
FT DOMAIN 517..698
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02205"
FT MOTIF 248..251
FT /note="DEAH box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02205"
FT BINDING 54..61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02205, ECO:0000305"
FT BINDING 120
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02205"
FT BINDING 194
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02205"
FT BINDING 199
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02205"
FT BINDING 205
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02205"
SQ SEQUENCE 716 AA; 81441 MW; 5855E85E868C49D4 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 MAAFFREQVE SKKHLGMLVL
FASGRAMQRF LDYVTDLRLM LLVQGDQPRY RLVELHRKRV ANGERSVLVG LQSFAEGLDL
KGDLLSQVHI HKIAFPPIDS PVVITEGEWL KSLNRYPFEV QSLPSASFNL IQQVGRLIRS
HGCWGEVVIY DKRLLTKNYG KRLLDALPVF PIEQPEVPEG IVKKKEKTKS PRRRRR
