UVRD_ECOLI
ID UVRD_ECOLI Reviewed; 720 AA.
AC P03018; P76758; Q2M8B9; Q47709;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=DNA helicase II;
DE EC=3.6.4.12;
GN Name=uvrD; Synonyms=mutU, pdeB, rad, recL; OrderedLocusNames=b3813, JW3786;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6379604; DOI=10.1093/nar/12.14.5789;
RA Finch P.W., Emmerson P.T.;
RT "The nucleotide sequence of the uvrD gene of E. coli.";
RL Nucleic Acids Res. 12:5789-5799(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2943729; DOI=10.1093/oxfordjournals.jbchem.a135631;
RA Yamamoto Y., Ogawa T., Shinagawa H., Nakayama T., Matsuo H., Ogawa H.;
RT "Determination of the initiation sites of transcription and translation of
RT the uvrD gene of Escherichia coli.";
RL J. Biochem. 99:1579-1590(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-258.
RX PubMed=6324092; DOI=10.1093/nar/11.24.8625;
RA Easton A.M., Kushner S.R.;
RT "Transcription of the uvrD gene of Escherichia coli is controlled by the
RT lexA repressor and by attenuation.";
RL Nucleic Acids Res. 11:8625-8640(1983).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-17.
RC STRAIN=K12;
RX PubMed=2254268; DOI=10.1128/jb.172.12.6973-6980.1990;
RA Colloms S.D., Sykora P., Szatmari G., Sherratt D.J.;
RT "Recombination at ColE1 cer requires the Escherichia coli xerC gene
RT product, a member of the lambda integrase family of site-specific
RT recombinases.";
RL J. Bacteriol. 172:6973-6980(1990).
RN [8]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF GLY-30.
RX PubMed=8419285; DOI=10.1128/jb.175.2.341-350.1993;
RA Washburn B.K., Kushner S.R.;
RT "Characterization of DNA helicase II from a uvrD252 mutant of Escherichia
RT coli.";
RL J. Bacteriol. 175:341-350(1993).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / AB1157;
RX PubMed=25484163; DOI=10.1111/mmi.12899;
RA Cooper D.L., Boyle D.C., Lovett S.T.;
RT "Genetic analysis of Escherichia coli RadA: functional motifs and genetic
RT interactions.";
RL Mol. Microbiol. 95:769-779(2015).
CC -!- FUNCTION: A helicase with DNA-dependent ATPase activity
CC (PubMed:8419285). Unwinds DNA duplexes with 3' to 5' polarity with
CC respect to the bound strand. Initiates unwinding more efficiently from
CC a nicked substrate than ds duplex DNA (PubMed:8419285). Involved in the
CC post-incision events of nucleotide excision repair and methyl-directed
CC mismatch repair, and probably also in repair of alkylated DNA
CC (Probable). {ECO:0000269|PubMed:8419285, ECO:0000305|PubMed:25484163}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.05 mM for ATP {ECO:0000269|PubMed:8419285};
CC -!- INTERACTION:
CC P03018; P0A9P0: lpdA; NbExp=3; IntAct=EBI-559573, EBI-542856;
CC P03018; P25665: metE; NbExp=2; IntAct=EBI-559573, EBI-551247;
CC P03018; P23367: mutL; NbExp=7; IntAct=EBI-559573, EBI-554913;
CC P03018; P0A8V2: rpoB; NbExp=3; IntAct=EBI-559573, EBI-544996;
CC P03018; P0A8T7: rpoC; NbExp=3; IntAct=EBI-559573, EBI-543604;
CC -!- DISRUPTION PHENOTYPE: Strongly sensitive to UV, ciprofloxacin (CFX),
CC and azidothymidine (AZT) in single deletion mutants, radA-uvrD double
CC deletions are more sensitive yet. Adding recF mutations almost
CC completely suppresses AZT and partially suppresses UV and CFX
CC sensitivity, suggesting RadA processes a class of intermediates that
CC accumulate in uvrD mutants (PubMed:25484163).
CC {ECO:0000269|PubMed:25484163}.
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC {ECO:0000305}.
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DR EMBL; X00738; CAA25321.1; -; Genomic_DNA.
DR EMBL; D00069; BAA00048.1; -; Genomic_DNA.
DR EMBL; X04037; CAA27671.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67609.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76816.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77487.1; -; Genomic_DNA.
DR EMBL; X00225; CAA25043.1; -; Genomic_DNA.
DR EMBL; M38257; AAA24765.1; -; Genomic_DNA.
DR PIR; F65185; HJECD2.
DR RefSeq; NP_418258.1; NC_000913.3.
DR RefSeq; WP_000383406.1; NZ_SSZK01000025.1.
DR PDB; 2IS1; X-ray; 2.90 A; A/B=1-680.
DR PDB; 2IS2; X-ray; 3.00 A; A/B=1-680.
DR PDB; 2IS4; X-ray; 2.60 A; A/B=1-680.
DR PDB; 2IS6; X-ray; 2.20 A; A/B=1-680.
DR PDB; 3LFU; X-ray; 1.80 A; A=1-647.
DR PDB; 6YI2; NMR; -; A=645-720.
DR PDB; 7EGS; X-ray; 1.70 A; B=654-720.
DR PDBsum; 2IS1; -.
DR PDBsum; 2IS2; -.
DR PDBsum; 2IS4; -.
DR PDBsum; 2IS6; -.
DR PDBsum; 3LFU; -.
DR PDBsum; 6YI2; -.
DR PDBsum; 7EGS; -.
DR AlphaFoldDB; P03018; -.
DR SMR; P03018; -.
DR BioGRID; 4263340; 265.
DR BioGRID; 852644; 3.
DR ComplexPortal; CPX-5542; MutL-UvrD DNA helicase complex.
DR DIP; DIP-11103N; -.
DR IntAct; P03018; 39.
DR STRING; 511145.b3813; -.
DR jPOST; P03018; -.
DR PaxDb; P03018; -.
DR PRIDE; P03018; -.
DR EnsemblBacteria; AAC76816; AAC76816; b3813.
DR EnsemblBacteria; BAE77487; BAE77487; BAE77487.
DR GeneID; 66672280; -.
DR GeneID; 948347; -.
DR KEGG; ecj:JW3786; -.
DR KEGG; eco:b3813; -.
DR PATRIC; fig|511145.12.peg.3929; -.
DR EchoBASE; EB1057; -.
DR eggNOG; COG0210; Bacteria.
DR HOGENOM; CLU_004585_5_2_6; -.
DR InParanoid; P03018; -.
DR OMA; YQDTNRT; -.
DR PhylomeDB; P03018; -.
DR BioCyc; EcoCyc:EG11064-MON; -.
DR BioCyc; MetaCyc:EG11064-MON; -.
DR BRENDA; 3.6.4.12; 2026.
DR SABIO-RK; P03018; -.
DR EvolutionaryTrace; P03018; -.
DR PRO; PR:P03018; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0033202; C:DNA helicase complex; IDA:EcoCyc.
DR GO; GO:0017117; C:single-stranded DNA-dependent ATP-dependent DNA helicase complex; IPI:ComplexPortal.
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:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IDA:CACAO.
DR GO; GO:0015616; F:DNA translocase activity; IDA:EcoCyc.
DR GO; GO:0017116; F:single-stranded DNA helicase activity; IDA:EcoCyc.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:EcoCyc.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:InterPro.
DR GO; GO:0006298; P:mismatch repair; IMP:EcoCyc.
DR GO; GO:0070716; P:mismatch repair involved in maintenance of fidelity involved in DNA-dependent DNA replication; IDA:ComplexPortal.
DR GO; GO:0006289; P:nucleotide-excision repair; IDA:EcoCyc.
DR GO; GO:0000717; P:nucleotide-excision repair, DNA duplex unwinding; IDA:ComplexPortal.
DR GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR GO; GO:0031297; P:replication fork processing; IMP:EcoCyc.
DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
DR GO; GO:0070581; P:rolling circle DNA replication; IMP:EcoCyc.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.160; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom_sf.
DR InterPro; IPR005753; DNA_helicase_ATP-dep_UvrD.
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; TIGR01075; uvrD; 1.
DR PROSITE; PS51198; UVRD_HELICASE_ATP_BIND; 1.
DR PROSITE; PS51217; UVRD_HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; DNA damage;
KW DNA repair; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1..720
FT /note="DNA helicase II"
FT /id="PRO_0000102072"
FT DOMAIN 8..286
FT /note="UvrD-like helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT DOMAIN 287..564
FT /note="UvrD-like helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00617"
FT BINDING 32..37
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00560"
FT BINDING 284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MUTAGEN 30
FT /note="G->D: In uvrD252, UV sensitive, significant loss of
FT DNA-dependent ATPase, helicase activity requires higher ATP
FT and MgCl(2), nearly inactive on 96 bp dsDNA. KM for ATP
FT rises to 1.2 mM."
FT /evidence="ECO:0000269|PubMed:8419285"
FT CONFLICT 224
FT /note="D -> N (in Ref. 1; CAA25321)"
FT /evidence="ECO:0000305"
FT CONFLICT 291..293
FT /note="SAA -> NAR (in Ref. 1; CAA25321)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="A -> T (in Ref. 1; CAA25321)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="L -> V (in Ref. 1; CAA25321)"
FT /evidence="ECO:0000305"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:3LFU"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:2IS1"
FT HELIX 12..18
FT /evidence="ECO:0007829|PDB:3LFU"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:3LFU"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2IS2"
FT HELIX 35..48
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:3LFU"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 64..78
FT /evidence="ECO:0007829|PDB:3LFU"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 90..100
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:3LFU"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 116..129
FT /evidence="ECO:0007829|PDB:3LFU"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:3LFU"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:2IS6"
FT HELIX 166..184
FT /evidence="ECO:0007829|PDB:3LFU"
FT STRAND 186..188
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 189..202
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 204..213
FT /evidence="ECO:0007829|PDB:3LFU"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 222..224
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 227..237
FT /evidence="ECO:0007829|PDB:3LFU"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:3LFU"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 263..270
FT /evidence="ECO:0007829|PDB:3LFU"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:3LFU"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 287..297
FT /evidence="ECO:0007829|PDB:3LFU"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:2IS6"
FT STRAND 318..325
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 326..342
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 347..349
FT /evidence="ECO:0007829|PDB:3LFU"
FT STRAND 350..356
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 360..369
FT /evidence="ECO:0007829|PDB:3LFU"
FT STRAND 374..379
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 386..399
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 404..410
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 420..432
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 437..446
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 452..471
FT /evidence="ECO:0007829|PDB:3LFU"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 477..487
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 490..495
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 500..519
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 530..540
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 542..544
FT /evidence="ECO:0007829|PDB:2IS6"
FT STRAND 554..558
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 560..562
FT /evidence="ECO:0007829|PDB:3LFU"
FT STRAND 567..572
FT /evidence="ECO:0007829|PDB:3LFU"
FT TURN 579..581
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 583..586
FT /evidence="ECO:0007829|PDB:2IS6"
FT STRAND 587..590
FT /evidence="ECO:0007829|PDB:2IS6"
FT HELIX 592..603
FT /evidence="ECO:0007829|PDB:3LFU"
FT STRAND 606..620
FT /evidence="ECO:0007829|PDB:3LFU"
FT STRAND 623..626
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 631..635
FT /evidence="ECO:0007829|PDB:3LFU"
FT HELIX 638..640
FT /evidence="ECO:0007829|PDB:3LFU"
FT STRAND 641..643
FT /evidence="ECO:0007829|PDB:3LFU"
FT STRAND 646..649
FT /evidence="ECO:0007829|PDB:2IS4"
FT STRAND 651..654
FT /evidence="ECO:0007829|PDB:6YI2"
FT STRAND 675..678
FT /evidence="ECO:0007829|PDB:6YI2"
FT TURN 679..681
FT /evidence="ECO:0007829|PDB:6YI2"
FT STRAND 682..692
FT /evidence="ECO:0007829|PDB:6YI2"
FT HELIX 693..695
FT /evidence="ECO:0007829|PDB:6YI2"
FT STRAND 697..702
FT /evidence="ECO:0007829|PDB:6YI2"
FT STRAND 707..711
FT /evidence="ECO:0007829|PDB:6YI2"
FT HELIX 712..715
FT /evidence="ECO:0007829|PDB:6YI2"
SQ SEQUENCE 720 AA; 81990 MW; FA68E7267C77B49A CRC64;
MDVSYLLDSL NDKQREAVAA PRSNLLVLAG AGSGKTRVLV HRIAWLMSVE NCSPYSIMAV
TFTNKAAAEM RHRIGQLMGT SQGGMWVGTF HGLAHRLLRA HHMDANLPQD FQILDSEDQL
RLLKRLIKAM NLDEKQWPPR QAMWYINSQK DEGLRPHHIQ SYGNPVEQTW QKVYQAYQEA
CDRAGLVDFA ELLLRAHELW LNKPHILQHY RERFTNILVD EFQDTNNIQY AWIRLLAGDT
GKVMIVGDDD QSIYGWRGAQ VENIQRFLND FPGAETIRLE QNYRSTSNIL SAANALIENN
NGRLGKKLWT DGADGEPISL YCAFNELDEA RFVVNRIKTW QDNGGALAEC AILYRSNAQS
RVLEEALLQA SMPYRIYGGM RFFERQEIKD ALSYLRLIAN RNDDAAFERV VNTPTRGIGD
RTLDVVRQTS RDRQLTLWQA CRELLQEKAL AGRAASALQR FMELIDALAQ ETADMPLHVQ
TDRVIKDSGL RTMYEQEKGE KGQTRIENLE ELVTATRQFS YNEEDEDLMP LQAFLSHAAL
EAGEGQADTW QDAVQLMTLH SAKGLEFPQV FIVGMEEGMF PSQMSLDEGG RLEEERRLAY
VGVTRAMQKL TLTYAETRRL YGKEVYHRPS RFIGELPEEC VEEVRLRATV SRPVSHQRMG
TPMVENDSGY KLGQRVRHAK FGEGTIVNME GSGEHSRLQV AFQGQGIKWL VAAYARLESV
