ID UMUD_ECOLI Reviewed; 139 AA. AC P0AG11; P04153; DT 01-NOV-1986, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1986, sequence version 1. DT 17-JUN-2020, entry version 116. DE RecName: Full=Protein UmuD; DE EC=3.4.21.-; DE AltName: Full=DNA polymerase V; DE Short=Pol V; DE Contains: DE RecName: Full=Protein UmuD'; GN Name=umuD; OrderedLocusNames=b1183, JW1172; 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=2989817; DOI=10.1073/pnas.82.13.4336; RA Kitagawa Y., Akaboshi E., Shinagawa H., Horii T., Ogawa H., Kato T.; RT "Structural analysis of the umu operon required for inducible mutagenesis RT in Escherichia coli."; RL Proc. Natl. Acad. Sci. U.S.A. 82:4336-4340(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2989816; DOI=10.1073/pnas.82.13.4331; RA Perry K.L., Elledge S.J., Mitchell B.B., Marsh L., Walker G.C.; RT "umuDC and mucAB operons whose products are required for UV light- and RT chemical-induced mutagenesis: UmuD, MucA, and LexA proteins share RT homology."; RL Proc. Natl. Acad. Sci. U.S.A. 82:4331-4335(1985). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8905232; DOI=10.1093/dnares/3.3.137; RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., RA Horiuchi T.; RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 12.7-28.0 min region on the linkage map."; RL DNA Res. 3:137-155(1996). 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 MUTAGENESIS. RX PubMed=1320188; DOI=10.1007/bf00265442; RA Koch W.H., Ennis D.G., Levine A.S., Woodgate R.; RT "Escherichia coli umuDC mutants: DNA sequence alterations and UmuD RT cleavage."; RL Mol. Gen. Genet. 233:443-448(1992). RN [7] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [8] RP REGULATION BY LEXA, AND INDUCTION. RC STRAIN=K12 / RW118; RX PubMed=10760155; DOI=10.1046/j.1365-2958.2000.01826.x; RA Fernandez De Henestrosa A.R., Ogi T., Aoyagi S., Chafin D., Hayes J.J., RA Ohmori H., Woodgate R.; RT "Identification of additional genes belonging to the LexA regulon in RT Escherichia coli."; RL Mol. Microbiol. 35:1560-1572(2000). RN [9] RP FUNCTION IN TRANSLION REPAIR, AND STIMULATION BY RECA AND BETA RP SLIDING-CLAMP COMPLEX. RX PubMed=10801133; DOI=10.1038/35010020; RA Tang M., Pham P., Shen X., Taylor J.S., O'Donnell M., Woodgate R., RA Goodman M.F.; RT "Roles of E. coli DNA polymerases IV and V in lesion-targeted and RT untargeted SOS mutagenesis."; RL Nature 404:1014-1018(2000). RN [10] RP INDUCTION BY HYDROXYUREA. RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574; RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024; RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J., RA Walker G.C.; RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia RT coli."; RL Mol. Cell 36:845-860(2009). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF UMUD'. RX PubMed=8614470; DOI=10.1038/380727a0; RA Peat T.S., Frank E., McDonald J.P., Levine A.S., Woodgate R., RA Hendrickson W.A.; RT "Structure of the UmuD' protein and its regulation in response to DNA RT damage."; RL Nature 380:727-730(1996). CC -!- FUNCTION: Involved in UV protection and mutation. Poorly processive, CC error-prone DNA polymerase involved in translesion repair CC (PubMed:10801133). Essential for induced (or SOS) mutagenesis. Able to CC replicate DNA across DNA lesions (thymine photodimers and abasic sites, CC called translesion synthesis) in the presence of activated RecA; CC efficiency is maximal in the presence of the beta sliding-clamp and CC clamp-loading complex of DNA polymerase III plus single-stranded CC binding protein (SSB) (PubMed:10801133). RecA and to a lesser extent CC the beta clamp-complex may target Pol V to replication complexes CC stalled at DNA template lesions (PubMed:10801133). CC {ECO:0000269|PubMed:10801133}. CC -!- INTERACTION: CC P0AG11; P0AG11: umuD; NbExp=6; IntAct=EBI-1122622, EBI-1122622; CC PRO_0000027305; P04152: umuC; NbExp=7; IntAct=EBI-25426537, EBI-1119849; CC -!- INDUCTION: Repressed by LexA, induced by DNA damage (PubMed:10760155). CC Induced 1.5-fold by hydroxyurea (PubMed:20005847). CC {ECO:0000269|PubMed:10760155, ECO:0000269|PubMed:20005847}. CC -!- SIMILARITY: Belongs to the peptidase S24 family. {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; M10107; AAA24728.1; -; Genomic_DNA. DR EMBL; M13387; AAA98073.1; -; Genomic_DNA. DR EMBL; U00096; AAC74267.1; -; Genomic_DNA. DR EMBL; AP009048; BAA36030.1; -; Genomic_DNA. DR PIR; A03551; ZWECD. DR RefSeq; NP_415701.1; NC_000913.3. DR RefSeq; WP_000897378.1; NZ_STEB01000023.1. DR PDB; 1AY9; X-ray; 3.00 A; A/B=32-139. DR PDB; 1I4V; NMR; -; A/B=26-139. DR PDB; 1UMU; X-ray; 2.50 A; A/B=25-137. DR PDBsum; 1AY9; -. DR PDBsum; 1I4V; -. DR PDBsum; 1UMU; -. DR SMR; P0AG11; -. DR BioGRID; 4261817; 117. DR BioGRID; 850113; 7. DR DIP; DIP-29679N; -. DR IntAct; P0AG11; 15. DR STRING; 511145.b1183; -. DR MEROPS; S24.003; -. DR PaxDb; P0AG11; -. DR PRIDE; P0AG11; -. DR EnsemblBacteria; AAC74267; AAC74267; b1183. DR EnsemblBacteria; BAA36030; BAA36030; BAA36030. DR GeneID; 945746; -. DR KEGG; ecj:JW1172; -. DR KEGG; eco:b1183; -. DR PATRIC; fig|1411691.4.peg.1104; -. DR EchoBASE; EB1050; -. DR eggNOG; ENOG4105KT5; Bacteria. DR eggNOG; COG1974; LUCA. DR HOGENOM; CLU_066192_0_0_6; -. DR InParanoid; P0AG11; -. DR KO; K03503; -. DR PhylomeDB; P0AG11; -. DR BioCyc; EcoCyc:EG11057-MONOMER; -. DR BioCyc; ECOL316407:JW1172-MONOMER; -. DR BioCyc; MetaCyc:EG11057-MONOMER; -. DR BRENDA; 3.4.21.B30; 2026. DR EvolutionaryTrace; P0AG11; -. DR PRO; PR:P0AG11; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0009355; C:DNA polymerase V complex; IDA:EcoCyc. DR GO; GO:0008094; F:DNA-dependent ATPase activity; IDA:EcoCyc. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:EcoCyc. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0003697; F:single-stranded DNA binding; IDA:EcoCyc. DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoCyc. DR GO; GO:0006281; P:DNA repair; IMP:EcoCyc. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR GO; GO:0009432; P:SOS response; IEP:EcoCyc. DR GO; GO:0019985; P:translesion synthesis; IDA:EcoCyc. DR CDD; cd06529; S24_LexA-like; 1. DR DisProt; DP00626; -. DR InterPro; IPR039418; LexA-like. DR InterPro; IPR036286; LexA/Signal_pep-like_sf. DR InterPro; IPR006197; Peptidase_S24_LexA. DR InterPro; IPR015927; Peptidase_S24_S26A/B/C. DR Pfam; PF00717; Peptidase_S24; 1. DR PRINTS; PR00726; LEXASERPTASE. DR SUPFAM; SSF51306; SSF51306; 1. PE 1: Evidence at protein level; KW 3D-structure; Autocatalytic cleavage; DNA damage; DNA repair; Hydrolase; KW Protease; Reference proteome; Serine protease; SOS mutagenesis; KW SOS response. FT CHAIN 1..139 FT /note="Protein UmuD" FT /id="PRO_0000041988" FT CHAIN 25..139 FT /note="Protein UmuD'" FT /id="PRO_0000027305" FT ACT_SITE 60 FT /note="For autocatalytic cleavage activity" FT ACT_SITE 97 FT /note="For autocatalytic cleavage activity" FT SITE 24..25 FT /note="Cleavage; by autolysis" FT MUTAGEN 27 FT /note="P->D: In umuD1; non-cleavable." FT /evidence="ECO:0000269|PubMed:1320188" FT MUTAGEN 65 FT /note="G->R: In umuD44; non-cleavable." FT /evidence="ECO:0000269|PubMed:1320188" FT MUTAGEN 92 FT /note="G->D: In umuD77; non-cleavable." FT /evidence="ECO:0000269|PubMed:1320188" FT HELIX 40..44 FT /evidence="ECO:0000244|PDB:1UMU" FT HELIX 48..50 FT /evidence="ECO:0000244|PDB:1UMU" FT STRAND 51..55 FT /evidence="ECO:0000244|PDB:1UMU" FT STRAND 58..60 FT /evidence="ECO:0000244|PDB:1I4V" FT HELIX 62..64 FT /evidence="ECO:0000244|PDB:1UMU" FT STRAND 71..75 FT /evidence="ECO:0000244|PDB:1UMU" FT STRAND 82..84 FT /evidence="ECO:0000244|PDB:1I4V" FT STRAND 85..90 FT /evidence="ECO:0000244|PDB:1UMU" FT STRAND 93..100 FT /evidence="ECO:0000244|PDB:1UMU" FT STRAND 102..104 FT /evidence="ECO:0000244|PDB:1UMU" FT STRAND 106..108 FT /evidence="ECO:0000244|PDB:1UMU" FT STRAND 120..124 FT /evidence="ECO:0000244|PDB:1I4V" FT STRAND 125..135 FT /evidence="ECO:0000244|PDB:1UMU" SQ SEQUENCE 139 AA; 15063 MW; 0681A3FFAC7ED583 CRC64; MLFIKPADLR EIVTFPLFSD LVQCGFPSPA ADYVEQRIDL NQLLIQHPSA TYFVKASGDS MIDGGISDGD LLIVDSAITA SHGDIVIAAV DGEFTVKKLQ LRPTVQLIPM NSAYSPITIS SEDTLDVFGV VIHVVKAMR //