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 29-MAY-2013, entry version 132.
DE RecName: Full=DNA helicase II;
DE EC=3.6.4.12;
GN Name=uvrD; Synonyms=mutU, pdeB, rad, recL;
GN OrderedLocusNames=b3813, JW3786;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
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;
RA Yamamoto Y., Ogawa T., Shinagawa H., Nakayama T., Matsuo H., Ogawa H.;
RT "Determination of the initiation sites of transcription and
RT translation of 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
RT from 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.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(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
RT MG1655 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
RT the 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;
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 VARIANT UVRD252.
RX PubMed=8419285;
RA Washburn B.K., Kushner S.R.;
RT "Characterization of DNA helicase II from a uvrD252 mutant of
RT Escherichia coli.";
RL J. Bacteriol. 175:341-350(1993).
CC -!- FUNCTION: Has both ATPase and helicase activities. Unwinds DNA
CC duplexes with 3' to 5' polarity with respect to the bound strand
CC and initiates unwinding most effectively when a single-stranded
CC region is present. Involved in the post-incision events of
CC nucleotide excision repair and methyl-directed mismatch repair.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- INTERACTION:
CC P0A9P0:lpdA; NbExp=2; IntAct=EBI-559573, EBI-542856;
CC P23367:mutL; NbExp=7; IntAct=EBI-559573, EBI-554913;
CC -!- SIMILARITY: Belongs to the helicase family. UvrD subfamily.
CC -!- SIMILARITY: Contains 1 uvrD-like helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 uvrD-like helicase C-terminal domain.
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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_000913.2.
DR RefSeq; YP_491628.1; NC_007779.1.
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 PDBsum; 2IS1; -.
DR PDBsum; 2IS2; -.
DR PDBsum; 2IS4; -.
DR PDBsum; 2IS6; -.
DR PDBsum; 3LFU; -.
DR ProteinModelPortal; P03018; -.
DR SMR; P03018; 1-656.
DR DIP; DIP-11103N; -.
DR IntAct; P03018; 35.
DR MINT; MINT-1223204; -.
DR STRING; 511145.b3813; -.
DR PaxDb; P03018; -.
DR PRIDE; P03018; -.
DR EnsemblBacteria; AAC76816; AAC76816; b3813.
DR EnsemblBacteria; BAE77487; BAE77487; BAE77487.
DR GeneID; 12934346; -.
DR GeneID; 948347; -.
DR KEGG; ecj:Y75_p3364; -.
DR KEGG; eco:b3813; -.
DR PATRIC; 32123127; VBIEscCol129921_3929.
DR EchoBASE; EB1057; -.
DR EcoGene; EG11064; uvrD.
DR eggNOG; COG0210; -.
DR HOGENOM; HOG000033016; -.
DR KO; K03657; -.
DR OMA; ASPHSIL; -.
DR ProtClustDB; PRK11773; -.
DR BioCyc; EcoCyc:EG11064-MONOMER; -.
DR BioCyc; ECOL316407:JW3786-MONOMER; -.
DR BioCyc; MetaCyc:EG11064-MONOMER; -.
DR EvolutionaryTrace; P03018; -.
DR Genevestigator; P03018; -.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006268; P:DNA unwinding involved in replication; IEA:InterPro.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.160; -; 1.
DR InterPro; IPR013986; DExx_box_DNA_helicase_dom.
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; Complete proteome;
KW Direct protein sequencing; DNA damage; DNA repair; DNA replication;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding;
KW Reference proteome; SOS response.
FT CHAIN 1 720 DNA helicase II.
FT /FTId=PRO_0000102072.
FT DOMAIN 8 286 UvrD-like helicase ATP-binding.
FT DOMAIN 287 564 UvrD-like helicase C-terminal.
FT NP_BIND 32 37 ATP (By similarity).
FT BINDING 284 284 ATP (By similarity).
FT VARIANT 30 30 G -> D (in uvrD252, which is UV
FT sensitive).
FT CONFLICT 224 224 D -> N (in Ref. 1; CAA25321).
FT CONFLICT 291 293 SAA -> NAR (in Ref. 1; CAA25321).
FT CONFLICT 330 330 A -> T (in Ref. 1; CAA25321).
FT CONFLICT 540 540 L -> V (in Ref. 1; CAA25321).
FT HELIX 4 7
FT STRAND 8 10
FT HELIX 12 18
FT STRAND 25 29
FT STRAND 31 33
FT HELIX 35 48
FT HELIX 54 56
FT STRAND 57 63
FT HELIX 64 78
FT STRAND 86 89
FT HELIX 90 100
FT HELIX 103 105
FT STRAND 112 114
FT HELIX 116 129
FT TURN 134 136
FT HELIX 139 151
FT TURN 156 158
FT HELIX 166 184
FT STRAND 186 188
FT HELIX 189 202
FT HELIX 204 213
FT STRAND 216 221
FT HELIX 222 224
FT HELIX 227 237
FT TURN 238 240
FT STRAND 242 247
FT HELIX 249 251
FT HELIX 255 257
FT HELIX 263 270
FT STRAND 275 279
FT STRAND 283 285
FT HELIX 287 297
FT STRAND 300 302
FT STRAND 318 325
FT HELIX 326 342
FT HELIX 347 349
FT STRAND 350 356
FT HELIX 357 359
FT HELIX 360 369
FT STRAND 374 379
FT HELIX 382 384
FT HELIX 386 399
FT HELIX 404 410
FT HELIX 420 432
FT HELIX 437 446
FT HELIX 452 471
FT TURN 472 474
FT HELIX 477 487
FT HELIX 490 495
FT HELIX 500 519
FT HELIX 530 540
FT HELIX 542 544
FT STRAND 554 558
FT HELIX 560 562
FT STRAND 567 572
FT TURN 579 581
FT HELIX 583 586
FT STRAND 587 590
FT HELIX 592 603
FT STRAND 606 620
FT STRAND 623 626
FT HELIX 631 635
FT HELIX 638 640
FT STRAND 641 643
FT STRAND 646 649
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
//
