ID   UVRD2_MYCTO             Reviewed;         700 AA.
AC   P9WMP8; L0TBT8; O53344; P64320;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 46.
DE   RecName: Full=ATP-dependent DNA helicase UvrD2;
DE            EC=3.6.4.12;
GN   Name=uvrD2; OrderedLocusNames=MT3291;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: DNA-dependent ATPase, stimulated equally by ss- and dsDNA.
CC       Has both ATPase and helicase activities, and translocates along ssDNA
CC       displacing bound streptavidin. Its essentiality for growth does not
CC       depend on its helicase activity (By similarity). {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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK47634.1; -; Genomic_DNA.
DR   PIR; D70951; D70951.
DR   RefSeq; WP_003416822.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WMP8; -.
DR   SMR; P9WMP8; -.
DR   PRIDE; P9WMP8; -.
DR   EnsemblBacteria; AAK47634; AAK47634; MT3291.
DR   GeneID; 45427188; -.
DR   KEGG; mtc:MT3291; -.
DR   PATRIC; fig|83331.31.peg.3544; -.
DR   HOGENOM; CLU_004585_5_6_11; -.
DR   Proteomes; UP000001020; Chromosome.
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; IEA:UniProtKB-EC.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.160; -; 1.
DR   Gene3D; 1.10.150.80; -; 1.
DR   Gene3D; 3.40.50.300; -; 3.
DR   InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR   InterPro; IPR014017; DNA_helicase_UvrD-like_C.
DR   InterPro; IPR000212; DNA_helicase_UvrD/REP.
DR   InterPro; IPR010997; HRDC-like_sf.
DR   InterPro; IPR002121; HRDC_dom.
DR   InterPro; IPR044876; HRDC_dom_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014016; UvrD-like_ATP-bd.
DR   PANTHER; PTHR11070; PTHR11070; 1.
DR   Pfam; PF00570; HRDC; 1.
DR   Pfam; PF00580; UvrD-helicase; 1.
DR   Pfam; PF13361; UvrD_C; 2.
DR   SMART; SM00341; HRDC; 1.
DR   SUPFAM; SSF47819; SSF47819; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50967; HRDC; 1.
DR   PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR   PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW   Nucleotide-binding.
FT   CHAIN           1..700
FT                   /note="ATP-dependent DNA helicase UvrD2"
FT                   /id="PRO_0000427266"
FT   DOMAIN          10..301
FT                   /note="UvrD-like helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT   DOMAIN          302..553
FT                   /note="UvrD-like helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00617"
FT   DOMAIN          626..700
FT                   /note="HRDC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00328"
FT   REGION          565..595
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         34..39
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT   BINDING         299
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   700 AA;  75604 MW;  60A1B7520855C81C CRC64;
     MSIASDPLIA GLDDQQREAV LAPRGPVCVL AGAGTGKTRT ITHRIASLVA SGHVAAGQVL
     AVTFTQRAAG EMRSRLRALD AAARTGSGVG AVQALTFHAA AYRQLRYFWS RVIADTGWQL
     LDSKFAVVAR AASRTRLHAS TDDVRDLAGE IEWAKASLIG PEEYVTAVAA ARRDPPLDAA
     QIAAVYSEYE ALKARGDGVT LLDFDDLLLH TAAAIENDAA VAEEFQDRYR CFVVDEYQDV
     TPLQQRVLSA WLGDRDDLTV VGDANQTIYS FTGASPRFLL DFSRRFPDAA VVRLERDYRS
     TPQVVSLANR VIAAARGRVA GSKLRLSGQR EPGPVPSFHE HSDEPAEAAT VAASIARLIA
     SGTPPSEVAI LYRVNAQSEV YEEALTQAGI AYQVRGGEGF FNRQEIKQAL LALQRVSERD
     TDAALSDVVR AVLAPLGLTA QPPVGTRARE RWEALTALAE LVDDELAQRP ALQLPGLLAE
     LRRRAEARHP PVVQGVTLAS LHAAKGLEWD AVFLVGLADG TLPISHALAH GPNSEPVEEE
     RRLLYVGITR ARVHLALSWA LSRSPGGRQS RKPSRFLNGI APQTRADPVP GTSRRNRGAA
     ARCRICNNEL NTSAAVMLRR CETCAADVDE ELLLQLKSWR LSTAKEQNVP AYVVFTDNTL
     IAIAELLPTD DAALIAIPGI GARKLEQYGS DVLQLVRGRT