UVRD1_MYCTU
ID UVRD1_MYCTU Reviewed; 771 AA.
AC P9WMQ1; 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 45.
DE RecName: Full=ATP-dependent DNA helicase UvrD1;
DE EC=3.6.4.12;
GN Name=uvrD1; Synonyms=ivrd, pcrA; OrderedLocusNames=Rv0949;
GN ORFNames=MTCY10D7.25c;
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 FUNCTION AS A HELICASE, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ACTIVITY
RP REGULATION, AND SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17158674; DOI=10.1128/jb.01421-06;
RA Curti E., Smerdon S.J., Davis E.O.;
RT "Characterization of the helicase activity and substrate specificity of
RT Mycobacterium tuberculosis UvrD.";
RL J. Bacteriol. 189:1542-1555(2007).
RN [3]
RP FUNCTION AS AN ATPASE, FUNCTION IN DNA UNWINDING, FUNCTION IN INHIBITION OF
RP DNA STRAND EXCHANGE, INTERACTION WITH RECA, AND MUTAGENESIS OF GLN-276.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20455546; DOI=10.1021/bi902021d;
RA Singh P., Patil K.N., Khanduja J.S., Kumar P.S., Williams A., Rossi F.,
RA Rizzi M., Davis E.O., Muniyappa K.;
RT "Mycobacterium tuberculosis UvrD1 and UvrA proteins suppress DNA strand
RT exchange promoted by cognate and noncognate RecA proteins.";
RL Biochemistry 49:4872-4883(2010).
RN [4]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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).
RN [5]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=22467787; DOI=10.1128/jb.06654-11;
RA Houghton J., Townsend C., Williams A.R., Rodgers A., Rand L., Walker K.B.,
RA Bottger E.C., Springer B., Davis E.O.;
RT "Important role for Mycobacterium tuberculosis UvrD1 in pathogenesis and
RT persistence apart from its function in nucleotide excision repair.";
RL J. Bacteriol. 194:2916-2923(2012).
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. {ECO:0000269|PubMed:17158674,
CC ECO:0000269|PubMed:20455546, ECO:0000269|PubMed:22467787}.
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;
CC Evidence={ECO:0000269|PubMed:17158674};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17158674};
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000269|PubMed:17158674};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:17158674};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:17158674};
CC Note=Mg(2+); Mn(2+), Cu(2+), Ni(2+) or Co(2+) also support ATPase
CC activity. {ECO:0000269|PubMed:17158674};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:17158674}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=60.2 uM for ATP {ECO:0000269|PubMed:17158674};
CC Note=kcat is 43 sec(-1) with ATP.;
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:17158674};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:17158674};
CC -!- SUBUNIT: Monomer. Interacts with RecA. {ECO:0000269|PubMed:17158674,
CC ECO:0000269|PubMed:20455546}.
CC -!- INDUCTION: Up-regulated during mouse infection.
CC {ECO:0000269|PubMed:22467787}.
CC -!- DISRUPTION PHENOTYPE: Forms small colonies, liquid growth is unchanged.
CC Increased sensitivity to UV light, mitomycin C, nitrosative and
CC oxidative stress; a double uvrA/uvrD1 mutant is even more sensitive.
CC Single uvrD1 mutant is strongly attenuated in late stages of mouse
CC infection, the double uvrA/uvrD1 mutant is strongly attenuated at all
CC stages of infection. {ECO:0000269|PubMed:22467787}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP43697.1; -; Genomic_DNA.
DR PIR; C70716; C70716.
DR RefSeq; WP_003404859.1; NZ_NVQJ01000001.1.
DR RefSeq; YP_177772.1; NC_000962.3.
DR AlphaFoldDB; P9WMQ1; -.
DR SASBDB; P9WMQ1; -.
DR SMR; P9WMQ1; -.
DR STRING; 83332.Rv0949; -.
DR iPTMnet; P9WMQ1; -.
DR PaxDb; P9WMQ1; -.
DR DNASU; 885442; -.
DR GeneID; 885442; -.
DR KEGG; mtu:Rv0949; -.
DR TubercuList; Rv0949; -.
DR eggNOG; COG0210; Bacteria.
DR OMA; YQDTNRT; -.
DR PhylomeDB; P9WMQ1; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0033202; C:DNA helicase complex; IDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IDA:MTBBASE.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:MTBBASE.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:MTBBASE.
DR GO; GO:0032564; F:dATP binding; IDA:MTBBASE.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
DR GO; GO:0006302; P:double-strand break repair; IMP:MTBBASE.
DR GO; GO:0060543; P:negative regulation of strand invasion; IDA:MTBBASE.
DR GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR GO; GO:0009650; P:UV protection; IMP:MTBBASE.
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 1: Evidence at protein level;
KW Acetylation; ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase;
KW Hydrolase; Nucleotide-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:21969609"
FT CHAIN 2..771
FT /note="ATP-dependent DNA helicase UvrD1"
FT /id="PRO_0000102055"
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"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:21969609"
FT MUTAGEN 276
FT /note="Q->R: Loss of ATPase and DNA unwinding, partially
FT inhibits DNA strand exchange."
FT /evidence="ECO:0000269|PubMed:20455546"
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
