DING_SALPA
ID DING_SALPA Reviewed; 714 AA.
AC Q5PG19;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=SPA1932;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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; CP000026; AAV77842.1; -; Genomic_DNA.
DR RefSeq; WP_001218627.1; NC_006511.1.
DR AlphaFoldDB; Q5PG19; -.
DR SMR; Q5PG19; -.
DR EnsemblBacteria; AAV77842; AAV77842; SPA1932.
DR KEGG; spt:SPA1932; -.
DR HOGENOM; CLU_012117_4_1_6; -.
DR OMA; PRRAQNY; -.
DR Proteomes; UP000008185; 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_0000102000"
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; 80972 MW; BFEE89DB63216876 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 KLVATCMEQF RPKTTPPLAN
PERLNAHCEE VYELIASLNA ILNLYMPAAQ EAEHRFAMGE LPDEVMEICQ RLAKLTETLR
GLAESFLNDL SEKTGSHDIM RLHRVILQMN RALGMFEAQS KLWRLASMAQ SSGAPVSKWA
TREIREGQLH VWFHCVGIRV SEQLERLLWC 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
