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 27-MAR-2024, entry version 201. DE RecName: Full=DNA helicase II; DE EC=5.6.2.4 {ECO:0000269|PubMed:8419285}; DE AltName: Full=DNA 3'-5' helicase II {ECO:0000305}; GN Name=uvrD; Synonyms=mutU, pdeB, rad, recL; GN OrderedLocusNames=b3813, JW3786; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; 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, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP 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=Couples ATP hydrolysis with the unwinding of duplex DNA by CC translocating in the 3'-5' direction.; EC=5.6.2.4; CC Evidence={ECO:0000269|PubMed:8419285}; 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=5.6.2.4; CC Evidence={ECO:0000269|PubMed:8419285}; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 511145-b3813; -. DR EnsemblBacteria; AAC76816; AAC76816; b3813. DR GeneID; 75204806; -. 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; DYPDATT; -. DR OrthoDB; 9806690at2; -. DR PhylomeDB; P03018; -. DR BioCyc; EcoCyc:EG11064-MONOMER; -. DR BioCyc; MetaCyc:EG11064-MONOMER; -. 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:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0042803; F:protein homodimerization 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 CDD; cd17932; DEXQc_UvrD; 1. DR CDD; cd18807; SF1_C_UvrD; 1. DR Gene3D; 1.10.10.160; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR01075; uvrD; 1. DR PANTHER; PTHR11070:SF2; ATP-DEPENDENT DNA HELICASE SRS2; 1. DR PANTHER; PTHR11070; UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER; 1. DR Pfam; PF21196; PcrA_UvrD_tudor; 1. DR Pfam; PF00580; UvrD-helicase; 1. DR Pfam; PF13361; UvrD_C; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; Isomerase; 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:7EGS" FT TURN 679..681 FT /evidence="ECO:0007829|PDB:7EGS" FT STRAND 682..690 FT /evidence="ECO:0007829|PDB:7EGS" FT HELIX 693..695 FT /evidence="ECO:0007829|PDB:7EGS" FT STRAND 697..702 FT /evidence="ECO:0007829|PDB:7EGS" FT TURN 703..705 FT /evidence="ECO:0007829|PDB:7EGS" FT STRAND 706..711 FT /evidence="ECO:0007829|PDB:7EGS" FT HELIX 712..714 FT /evidence="ECO:0007829|PDB:7EGS" FT STRAND 717..719 FT /evidence="ECO:0007829|PDB:7EGS" 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 //