UVRD1_MYCTO
ID UVRD1_MYCTO Reviewed; 771 AA.
AC P9WMQ0; L0T870; P0A5A3; P71561;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=ATP-dependent DNA helicase UvrD1;
DE EC=3.6.4.12;
GN Name=uvrD1; Synonyms=ivrd, pcrA; OrderedLocusNames=MT0976;
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, acting on dsDNA with a 3'-ssDNA tail,
CC unwinding with 3'-to 5'-polarity. A minimal tail of 18 nt is required
CC for activity. Also highly efficient on nicked DNA. Involved in the
CC post-incision events of nucleotide excision repair, as well as in
CC nitrosative and oxidative stress response and possibly in persistence
CC in the host. Inhibits RecA-mediated DNA strand exchange; this does not
CC require ATPase activity. When combined with UvrA greatly inhibits RecA-
CC mediated DNA strand exchange (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 -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000516; AAK45224.1; -; Genomic_DNA.
DR PIR; C70716; C70716.
DR RefSeq; WP_003404859.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WMQ0; -.
DR SMR; P9WMQ0; -.
DR EnsemblBacteria; AAK45224; AAK45224; MT0976.
DR KEGG; mtc:MT0976; -.
DR PATRIC; fig|83331.31.peg.1047; -.
DR HOGENOM; CLU_004585_5_2_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
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 GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR005751; ATP-dep_DNA_helicase_PcrA.
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; PTHR11070; 1.
DR Pfam; PF00580; UvrD-helicase; 1.
DR Pfam; PF13361; UvrD_C; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01073; pcrA; 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..771
FT /note="ATP-dependent DNA helicase UvrD1"
FT /id="PRO_0000427265"
FT DOMAIN 21..311
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT DOMAIN 312..603
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00617"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 45..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT BINDING 309
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 771 AA; 85050 MW; DBAA84E151F4E2C9 CRC64;
MSVHATDAKP PGPSPADQLL DGLNPQQRQA VVHEGSPLLI VAGAGSGKTA VLTRRIAYLM
AARGVGVGQI LAITFTNKAA AEMRERVVGL VGEKARYMWV STFHSTCVRI LRNQAALIEG
LNSNFSIYDA DDSRRLLQMV GRDLGLDIKR YSPRLLANAI SNLKNELIDP HQALAGLTED
SDDLARAVAS VYDEYQRRLR AANALDFDDL IGETVAVLQA FPQIAQYYRR RFRHVLVDEY
QDTNHAQYVL VRELVGRDSN DGIPPGELCV VGDADQSIYA FRGATIRNIE DFERDYPDTR
TILLEQNYRS TQNILSAANS VIARNAGRRE KRLWTDAGAG ELIVGYVADN EHDEARFVAE
EIDALAEGSE ITYNDVAVFY RTNNSSRSLE EVLIRAGIPY KVVGGVRFYE RKEIRDIVAY
LRVLDNPGDA VSLRRILNTP RRGIGDRAEA CVAVYAENTG VGFGDALVAA AQGKVPMLNT
RAEKAIAGFV EMFDELRGRL DDDLGELVEA VLERTGYRRE LEASTDPQEL ARLDNLNELV
SVAHEFSTDR ENAAALGPDD EDVPDTGVLA DFLERVSLVA DADEIPEHGA GVVTLMTLHT
AKGLEFPVVF VTGWEDGMFP HMRALDNPTE LSEERRLAYV GITRARQRLY VSRAIVRSSW
GQPMLNPESR FLREIPQELI DWRRTAPKPS FSAPVSGAGR FGSARPSPTR SGASRRPLLV
LQVGDRVTHD KYGLGRVEEV SGVGESAMSL IDFGSSGRVK LMHNHAPVTK L
