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Database: UniProt
Entry: P9WMQ1
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Original site: P9WMQ1 
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   23-MAY-2018, entry version 26.
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.,
RA   Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA   Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA   Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA   Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA   Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA   Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the
RT   complete genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   FUNCTION AS A HELICASE, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR,
RP   ENZYME 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
RT   of Mycobacterium tuberculosis UvrD.";
RL   J. Bacteriol. 189:1542-1555(2007).
RN   [3]
RP   FUNCTION AS AN ATPASE, FUNCTION IN DNA UNWINDING, FUNCTION IN
RP   INHIBITION OF DNA STRAND EXCHANGE, INTERACTION WITH RECA, AND
RP   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.,
RA   Rossi F., Rizzi M., Davis E.O., Muniyappa K.;
RT   "Mycobacterium tuberculosis UvrD1 and UvrA proteins suppress DNA
RT   strand 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
RP   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.,
RA   Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
RA   Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
RA   Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
RA   Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high
RT   resolution 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.,
RA   Walker K.B., Bottger E.C., Springer B., Davis E.O.;
RT   "Important role for Mycobacterium tuberculosis UvrD1 in pathogenesis
RT   and persistence apart from its function in nucleotide excision
RT   repair.";
RL   J. Bacteriol. 194:2916-2923(2012).
CC   -!- FUNCTION: DNA-dependent ATPase, acting on dsDNA with a 3'-ssDNA
CC       tail, unwinding with 3'-to 5'-polarity. A minimal tail of 18 nt is
CC       required for activity. Also highly efficient on nicked DNA.
CC       Involved in the post-incision events of nucleotide excision
CC       repair, as well as in nitrosative and oxidative stress response
CC       and possibly in persistence in the host. Inhibits RecA-mediated
CC       DNA strand exchange; this does not require ATPase activity. When
CC       combined with UvrA greatly inhibits RecA-mediated DNA strand
CC       exchange. {ECO:0000269|PubMed:17158674,
CC       ECO:0000269|PubMed:20455546, ECO:0000269|PubMed:22467787}.
CC   -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
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   -!- ENZYME REGULATION: Inhibited by EDTA.
CC       {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.
CC       {ECO:0000269|PubMed:17158674, 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
CC       unchanged. Increased sensitivity to UV light, mitomycin C,
CC       nitrosative and oxidative stress; a double uvrA/uvrD1 mutant is
CC       even more sensitive. Single uvrD1 mutant is strongly attenuated in
CC       late stages of mouse infection, the double uvrA/uvrD1 mutant is
CC       strongly attenuated at all stages of infection.
CC       {ECO:0000269|PubMed:22467787}.
CC   -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC       {ECO:0000305}.
DR   EMBL; AL123456; CCP43697.1; -; Genomic_DNA.
DR   PIR; C70716; C70716.
DR   RefSeq; WP_003404859.1; NZ_KK339370.1.
DR   RefSeq; YP_177772.1; NC_000962.3.
DR   ProteinModelPortal; P9WMQ1; -.
DR   SMR; P9WMQ1; -.
DR   STRING; 83332.Rv0949; -.
DR   iPTMnet; P9WMQ1; -.
DR   PaxDb; P9WMQ1; -.
DR   PRIDE; P9WMQ1; -.
DR   EnsemblBacteria; CCP43697; CCP43697; Rv0949.
DR   GeneID; 885442; -.
DR   KEGG; mtu:Rv0949; -.
DR   TubercuList; Rv0949; -.
DR   eggNOG; ENOG4105C4R; Bacteria.
DR   eggNOG; COG0210; LUCA.
DR   KO; K03657; -.
DR   OMA; YQDTNRT; -.
DR   PhylomeDB; P9WMQ1; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005618; C:cell wall; IDA:MTBBASE.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0033202; C:DNA helicase complex; IDA:MTBBASE.
DR   GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0043140; F:ATP-dependent 3'-5' DNA helicase activity; IDA:MTBBASE.
DR   GO; GO:0016887; F:ATPase activity; IDA:MTBBASE.
DR   GO; GO:0032564; F:dATP binding; IDA:MTBBASE.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; IDA:MTBBASE.
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:0040007; P:growth; IMP:MTBBASE.
DR   GO; GO:0060543; P:negative regulation of strand invasion; IDA:MTBBASE.
DR   GO; GO:0009650; P:UV protection; IMP:MTBBASE.
DR   Gene3D; 1.10.10.160; -; 1.
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   InterPro; IPR034739; UvrD/AddA_N.
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; Complete proteome; DNA damage; DNA repair;
KW   DNA-binding; Helicase; Hydrolase; Nucleotide-binding;
KW   Reference proteome.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:21969609}.
FT   CHAIN         2    771       ATP-dependent DNA helicase UvrD1.
FT                                /FTId=PRO_0000102055.
FT   DOMAIN       21    311       UvrD-like helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00560}.
FT   DOMAIN      312    603       UvrD-like helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00617}.
FT   NP_BIND      45     50       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00560}.
FT   BINDING     309    309       ATP. {ECO:0000250}.
FT   MOD_RES       2      2       N-acetylserine.
FT                                {ECO:0000244|PubMed:21969609}.
FT   MUTAGEN     276    276       Q->R: Loss of ATPase and DNA unwinding,
FT                                partially inhibits DNA strand exchange.
FT                                {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
//
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