ID UVRD1_MYCLE Reviewed; 778 AA.
AC Q9CD72;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=ATP-dependent DNA helicase UvrD1;
DE EC=5.6.2.4;
DE AltName: Full=DNA 3'-5' helicase UvrD1 {ECO:0000305};
GN Name=uvrD; OrderedLocusNames=ML0153;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
CC -!- FUNCTION: DNA-dependent ATPase, acting on dsDNA with a 3'-ssDNA tail,
CC unwinding with 3'-to 5'-polarity. Also highly efficient on nicked DNA.
CC Involved in the post-incision events of nucleotide excision repair (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by
CC translocating in the 3'-5' direction.; EC=5.6.2.4;
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=5.6.2.4;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000305}.
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DR EMBL; AL583917; CAC29661.1; -; Genomic_DNA.
DR PIR; A86928; A86928.
DR RefSeq; NP_301239.1; NC_002677.1.
DR RefSeq; WP_010907564.1; NC_002677.1.
DR AlphaFoldDB; Q9CD72; -.
DR SMR; Q9CD72; -.
DR STRING; 272631.gene:17573968; -.
DR KEGG; mle:ML0153; -.
DR PATRIC; fig|272631.5.peg.237; -.
DR Leproma; ML0153; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_2_11; -.
DR OrthoDB; 9806690at2; -.
DR Proteomes; UP000000806; 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:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd17932; DEXQc_UvrD; 1.
DR CDD; cd18807; SF1_C_UvrD; 2.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR027417; P-loop_NTPase.
DR InterPro; IPR014016; UvrD-like_ATP-bd.
DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1.
DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1.
DR Pfam; PF21196; PcrA_UvrD_tudor; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 Isomerase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..778
FT /note="ATP-dependent DNA helicase UvrD1"
FT /id="PRO_0000102054"
FT DOMAIN 19..313
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT DOMAIN 314..610
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00617"
FT BINDING 43..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT BINDING 311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 778 AA; 85635 MW; 3964DF128E008EF6 CRC64;
MSVHTTDAKP DSEVDRLLDG LNPQQRQAVV HEGSPLLIVA GAGSGKTTVL ARRIAYLIAA
RSVGVSQILA ITFTNKAAAE MRERVARLVG DHTGPSMWVS TFHSTCVRIL RNQASLIGGL
NSNFSIYDVD DSRSLLQMIG QDMGLDIKRY SPRLMANAIS NLKNELIDAE SAVANLSSDT
DDLARTVATV YGEYQRRLRT ANALDFDDLI GETVGILQAF PQIAEHYRRR FRHVLVDEYQ
DTNHAQYVLV RELVGHGARN SPDDMPPGEL CVVGDADQSI YAFRGSTISN IEDFERDYPD
TTTILLEQNY RSTQNILSAA NSVIARNFGR RDKRLWTDAG KGELIVGYVS DNEHDEAKFI
ADEIDALVGG GEITYDDVAV LYRANNLSRS LEEVFIPTGI PYKVVGGFCF YESKEIRDLI
AYLRVLDNPG DAVSMRRILN TPRRGIGDRA EACVSVYAEN TGTSFADALQ AVAEGKVPML
NTRSVKAIAG FVALLDDLRC RVDDDLGELV ESVLERSGYL RELESSTDPQ ELARLDNLNE
LVSFAHEFST EQANAAALAK SLHTPEDEDV PDTGALAAFL EKVSLMSDTD QIPENNSGVV
TLMTLHAAKG LEFPVVFVTG WEDGMLPHMR TLGDPTELSE ERRLAYVGIT RARQRLYLSR
AITRSSWGQP ILNPESRFLR EIPPELIDWR RSILTDSYST PASGASRFGR VRPSSIRSGA
SKRALLVLAP GDRVTHDKYG LGRVEEVSGV GESAISLIDF GSSGRIKLMH NHAPVTKL
//
