ID   DING_SALCH              Reviewed;         714 AA.
AC   Q57RD7;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=SCH_0818;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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}.
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DR   EMBL; AE017220; AAX64724.1; -; Genomic_DNA.
DR   RefSeq; WP_001539557.1; NC_006905.1.
DR   AlphaFoldDB; Q57RD7; -.
DR   SMR; Q57RD7; -.
DR   EnsemblBacteria; AAX64724; AAX64724; SCH_0818.
DR   KEGG; sec:SCH_0818; -.
DR   HOGENOM; CLU_012117_4_1_6; -.
DR   OMA; PRRAQNY; -.
DR   Proteomes; UP000000538; 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; 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; 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..714
FT                   /note="ATP-dependent DNA helicase DinG"
FT                   /id="PRO_0000101999"
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   714 AA;  80993 MW;  5B2CB7B7F9CC915D CRC64;
     MALTAALKAQ IAAWYKALQD QIPDFIPRAP QRQMIADVAR TLAGEEGRHL AIEAPTGVGK
     TLSYLIPGIA IAREEQKTLV VSTANVALQD QIFSKDLPLL RKIIPDLRFT AAFGRGRYVC
     PRNLAALASS EPTQQDLLAF LDDELTPNNQ EEQKRCARLK GDLDGYKWDG LRDHTDIAID
     DDLWRRLSTD KASCLNRNCH YYRECPFFVA RREIQEAEVV VANHALVMAA MESEAVLPEP
     KHLLLVLDEG HHLPDVARDA LEMSAEITAS WYRLQLDLFS KLVATSMEQF RPKTTPPLAN
     PERLNAHCEE VYELIASLNA ILNLYMPAAQ EAEHRFAMGE LPDEVMEICQ RLAKLTETLR
     GLAESFLNDL SEKTGSHDIV RLHRVILQMN WALGMFEAQS KLWRLASMAQ SSGAPVSKWA
     TREIREGQLH VWFHCVGIRV SDQLERLLWR SVPHIIVTSA TLRSLNSFSR LQEMSGLKEK
     AGDRFVALDS PFNHVEQGKL VIPQMRYEPT IDNEEQHIAE MAAYFREQLE SKKHHGMLVL
     FASGRAMQRF LEHVADVRLL LLVQGDQPRY RLVELHRKRV ESGERSVLVG LQSFAEGLDL
     KGELLTQVHI HKIAFPPIDS PVVITEGEWL KSLNRYPFEV QSLPSASFNL IQQVGRLIRS
     HACRGEVVIY DKRLLTKNYG QRLLNALPVF PIEQPAVPDV IVKPKAKPAR RRRR