ID   DING_MYCTU              Reviewed;         664 AA.
AC   P9WMR5; L0T6J2; P64314; Q10640;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 42.
DE   RecName: Full=Probable ATP-dependent helicase DinG homolog;
DE            EC=3.6.4.12;
GN   Name=dinG; OrderedLocusNames=Rv1329c; ORFNames=MTCY130.14c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Probable helicase involved in DNA repair and perhaps also
CC       replication. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the helicase family. DinG subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AL123456; CCP44087.1; -; Genomic_DNA.
DR   PIR; E70770; E70770.
DR   RefSeq; NP_215845.1; NC_000962.3.
DR   RefSeq; WP_003898827.1; NZ_NVQJ01000031.1.
DR   AlphaFoldDB; P9WMR5; -.
DR   SMR; P9WMR5; -.
DR   STRING; 83332.Rv1329c; -.
DR   PaxDb; P9WMR5; -.
DR   DNASU; 886889; -.
DR   GeneID; 45425307; -.
DR   GeneID; 886889; -.
DR   KEGG; mtu:Rv1329c; -.
DR   TubercuList; Rv1329c; -.
DR   eggNOG; COG1199; Bacteria.
DR   OMA; VVTNHAM; -.
DR   PhylomeDB; P9WMR5; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IBA:GO_Central.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR045028; DinG/Rad3-like.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR11472; PTHR11472; 2.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00491; HELICc2; 1.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW   Helicase; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..664
FT                   /note="Probable ATP-dependent helicase DinG homolog"
FT                   /id="PRO_0000102003"
FT   DOMAIN          14..290
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           246..249
FT                   /note="DEAH box"
FT   BINDING         49..56
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ   SEQUENCE   664 AA;  70168 MW;  875A13606091CDB1 CRC64;
     MSESVSMSVP ELLAIAVAAL GGTRRRGQQE MAAAVAHAFE TGEHLVVQAG TGTGKSLAYL
     VPAIIRALCD DAPVVVSTAT IALQRQLVDR DLPQLVDSLT NALPRRPKFA LLKGRRNYLC
     LNKIHNSVTA SDHDDERPQE ELFDPVAVTA LGRDVQRLTA WASTTVSGDR DDLKPGVGDR
     SWSQVSVSAR ECLGVARCPF GSECFSERAR GAAGLADVVV TNHALLAIDA VAESAVLPEH
     RLLVVDEAHE LADRVTSVAA AELTSATLGM AARRITRLVD PKVTQRLQAA SATFSSAIHD
     ARPGRIDCLD DEMATYLSAL RDAASAARSA IDTGSDTTTA SVRAEAGAVL TEISDTASRI
     LASFAPAIPD RSDVVWLEHE DNHESARAVL RVAPLSVAEL LATQVFARAT TVLTSATLTI
     GGSFDAMATA WGLTADTPWR GLDVGSPFQH AKSGILYVAA HLPPPGRDGS GSAEQLTEIA
     ELITAAGGRT LGLFSSMRAA RAATEAMRER LSTPVLCQGD DSTSTLVEKF TADAATSLFG
     TLSLWQGVDV PGPSLSLVLI DRIPFPRPDD PLLSARQRAV AARGGNGFMT VAASHAALLL
     AQGSGRLLRR VTDRGVVAVL DSRMATARYG EFLRASLPPF WQTTNATQVR AALRRLARAD
     AKAH