UVRD2_MYCTU
ID UVRD2_MYCTU Reviewed; 700 AA.
AC P9WMP9; 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 50.
DE RecName: Full=ATP-dependent DNA helicase UvrD2;
DE EC=3.6.4.12;
GN Name=uvrD2; OrderedLocusNames=Rv3198c; ORFNames=MTV014.42c;
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 DNA-DEPENDENT ATPASE.
RX PubMed=19766723; DOI=10.1016/j.pep.2009.09.006;
RA Kazarian K., Cassani C., Rizzi M.;
RT "Expression, purification and characterization of UvrD2 helicase from
RT Mycobacterium tuberculosis.";
RL Protein Expr. Purif. 69:215-218(2010).
RN [3]
RP FUNCTION AS A HELICASE, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, AND MUTAGENESIS OF GLN-266 AND GLU-508.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21725019; DOI=10.1128/jb.00302-11;
RA Williams A., Guthlein C., Beresford N., Bottger E.C., Springer B.,
RA Davis E.O.;
RT "UvrD2 is essential in Mycobacterium tuberculosis, but its helicase
RT activity is not required.";
RL J. Bacteriol. 193:4487-4494(2011).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [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).
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. {ECO:0000269|PubMed:19766723,
CC ECO:0000269|PubMed:21725019}.
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:21725019};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=68.0 uM for ATP {ECO:0000269|PubMed:21725019};
CC KM=0.049 uM for ssDNA {ECO:0000269|PubMed:21725019};
CC Note=kcat is 0.035 sec(-1) with ATP.;
CC -!- DISRUPTION PHENOTYPE: Essential for growth; the 100 C-terminal residues
CC are not required for growth. {ECO:0000269|PubMed:21725019}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP46012.1; -; Genomic_DNA.
DR PIR; D70951; D70951.
DR RefSeq; NP_217714.1; NC_000962.3.
DR RefSeq; WP_003416822.1; NZ_NVQJ01000003.1.
DR AlphaFoldDB; P9WMP9; -.
DR SMR; P9WMP9; -.
DR STRING; 83332.Rv3198c; -.
DR PaxDb; P9WMP9; -.
DR DNASU; 888902; -.
DR GeneID; 45427188; -.
DR GeneID; 888902; -.
DR KEGG; mtu:Rv3198c; -.
DR PATRIC; fig|83332.111.peg.3569; -.
DR TubercuList; Rv3198c; -.
DR eggNOG; COG0210; Bacteria.
DR OMA; YRHFVVD; -.
DR PhylomeDB; P9WMP9; -.
DR BRENDA; 3.6.4.12; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0033202; C:DNA helicase complex; IBA:GO_Central.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IDA:MTBBASE.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; DNA damage; DNA repair; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..700
FT /note="ATP-dependent DNA helicase UvrD2"
FT /id="PRO_0000102079"
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 REGION 601..700
FT /note="Not required for growth"
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"
FT MUTAGEN 266
FT /note="Q->R: Loss of growth, no ATPase activity. No DNA
FT unwinding. Does not translocate along DNA."
FT /evidence="ECO:0000269|PubMed:21725019"
FT MUTAGEN 508
FT /note="E->A: Not essential for growth, no helicase
FT activity. Wild-type ATPase activity, translocates along
FT DNA. No DNA unwinding."
FT /evidence="ECO:0000269|PubMed:21725019"
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
