UVRD2_MYCLE
ID UVRD2_MYCLE Reviewed; 714 AA.
AC P53528; Q9CCM9;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=ATP-dependent DNA helicase UvrD2;
DE EC=3.6.4.12;
GN Name=uvrD2; OrderedLocusNames=ML0637; ORFNames=B1937_F1_27;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
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, stimulated equally by ss- and dsDNA.
CC Has both ATPase and helicase activities (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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA17159.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAA17159.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAC30146.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U00016; AAA17159.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL583919; CAC30146.1; ALT_INIT; Genomic_DNA.
DR PIR; F86988; F86988.
DR PIR; S72591; S72591.
DR AlphaFoldDB; P53528; -.
DR SMR; P53528; -.
DR STRING; 272631.ML0637; -.
DR EnsemblBacteria; CAC30146; CAC30146; CAC30146.
DR KEGG; mle:ML0637; -.
DR Leproma; ML0637; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_6_11; -.
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: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; 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; Reference proteome.
FT CHAIN 1..714
FT /note="ATP-dependent DNA helicase UvrD2"
FT /id="PRO_0000102078"
FT DOMAIN 10..304
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT DOMAIN 305..560
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00617"
FT DOMAIN 633..713
FT /note="HRDC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00328"
FT REGION 572..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 587..602
FT /note="Polar residues"
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 302
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 714 AA; 77343 MW; C9D0E07089D9FBB1 CRC64;
MVMVVNPLTA GLDDEQREAV LAPRGPVCVL AGAGTGKTRT ITHRIAHLVG AGHVATGQVL
AVTFTQRAAA EMRSRLRALG AAVQAVSDFG VVRVLTFHAA AHRQLRYFWP RVIGDTGWQL
LDSKFATVAR AASSVRLHAG TDDVCDLAGE IEWAKASLIG PEEYVAAVAA IGRDTPLDAA
QIASVYAAYE ALKARGNGVP GVTLLDFDDL LLHTAAAIEN DAAVAEEFRD RYRCFVVDEY
QDVTPLQQRV LSAWLGDRDD LTVVGDANQT IYSFTGASPC FLLDFPRRFP DATVVRLERD
YRSTPQVVSL ANQVIAAAHG RVADSKFQLS GQREPGPAAS FHEYSDEPAE AAAVAASIAR
LIEFGTSPSE IAVLYRVNAQ SEAYEEALTE VGIAYQVRGG EGFFNRQEIK QALLALQRSA
ERSSQTEPNS PLSDVVRGVL EPLGLTAEKP VGSRARDRWE ALTALAELAD DEVAQHPRLD
LPGLLAELRL RADARHPPVV QGVTLASLHA VKGLEWDAVF LVGLADGTLP ISRALAHGAE
SEPVEEERRL LYVGITRARV YLALSWALSR TPGGRQSRKP SRFLNDIAPQ MGQNPASSRS
RRNRTATLRC RICKNDLTTP AAVMLQRCQI CAADVDEELL LQLKAWRLST AKEQNVPAYV
VLTDNTLIAI AELLPADEAA LIAVPGMSVR KIEQYGSDVL QLVRCRAVAV RTQT
