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 27-MAY-2015, entry version 85. DE RecName: Full=Protein UmuD; DE EC=3.4.21.-; DE Contains: DE RecName: Full=Protein UmuD'; GN Name=umuD; OrderedLocusNames=b1183, JW1172; 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=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 RT mutagenesis 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., RA Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., RA Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., RA Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., RA Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., RA Yano M., Horiuchi T.; RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to 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., RA Mau B., 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 RT MG1655 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., RA Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [8] 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. Essential for CC induced (or SOS) mutagenesis. May modify the DNA replication CC machinery to allow bypass synthesis across a damaged template. 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 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 DisProt; DP00626; -. DR ProteinModelPortal; P0AG11; -. DR SMR; P0AG11; 32-139. DR DIP; DIP-29679N; -. DR IntAct; P0AG11; 13. DR STRING; 511145.b1183; -. DR MEROPS; S24.003; -. DR EnsemblBacteria; AAC74267; AAC74267; b1183. DR EnsemblBacteria; BAA36030; BAA36030; BAA36030. DR GeneID; 945746; -. DR KEGG; ecj:Y75_p1155; -. DR KEGG; eco:b1183; -. DR PATRIC; 32117612; VBIEscCol129921_1228. DR EchoBASE; EB1050; -. DR EcoGene; EG11057; umuD. DR eggNOG; COG1974; -. DR HOGENOM; HOG000232166; -. DR InParanoid; P0AG11; -. DR KO; K03503; -. DR OMA; FMERVSA; -. DR OrthoDB; EOG6JHRHJ; -. 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 Genevestigator; P0AG11; -. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IDA:EcoCyc. DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki. DR GO; GO:0071897; P:DNA biosynthetic process; IDA:GOC. 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; IMP:EcoCyc. DR Gene3D; 2.10.109.10; -; 1. DR InterPro; IPR028360; Peptidase_S24/S26_b-rbn. DR InterPro; IPR006197; Peptidase_S24_LexA. DR InterPro; IPR019759; Peptidase_S24_S26. 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; Complete proteome; DNA damage; KW DNA repair; Hydrolase; Protease; Reference proteome; Serine protease; KW SOS mutagenesis; SOS response. FT CHAIN 1 139 Protein UmuD. FT /FTId=PRO_0000041988. FT CHAIN 25 139 Protein UmuD'. FT /FTId=PRO_0000027305. FT ACT_SITE 60 60 For autocatalytic cleavage activity. FT ACT_SITE 97 97 For autocatalytic cleavage activity. FT SITE 24 25 Cleavage; by autolysis. FT MUTAGEN 27 27 P->D: In umuD1; non-cleavable. FT {ECO:0000269|PubMed:1320188}. FT MUTAGEN 65 65 G->R: In umuD44; non-cleavable. FT {ECO:0000269|PubMed:1320188}. FT MUTAGEN 92 92 G->D: In umuD77; non-cleavable. FT {ECO:0000269|PubMed:1320188}. FT HELIX 40 44 {ECO:0000244|PDB:1UMU}. FT HELIX 48 50 {ECO:0000244|PDB:1UMU}. FT STRAND 51 55 {ECO:0000244|PDB:1UMU}. FT STRAND 58 60 {ECO:0000244|PDB:1I4V}. FT HELIX 62 64 {ECO:0000244|PDB:1UMU}. FT STRAND 71 75 {ECO:0000244|PDB:1UMU}. FT STRAND 82 84 {ECO:0000244|PDB:1I4V}. FT STRAND 85 90 {ECO:0000244|PDB:1UMU}. FT STRAND 93 100 {ECO:0000244|PDB:1UMU}. FT STRAND 102 104 {ECO:0000244|PDB:1UMU}. FT STRAND 106 108 {ECO:0000244|PDB:1UMU}. FT STRAND 120 124 {ECO:0000244|PDB:1I4V}. FT STRAND 125 135 {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 //