UMUD_ECOLI
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 03-AUG-2022, entry version 126.
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 TRANSLATION 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}.
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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 AlphaFoldDB; P0AG11; -.
DR BMRB; P0AG11; -.
DR SMR; P0AG11; -.
DR BioGRID; 4261817; 117.
DR BioGRID; 850113; 7.
DR ComplexPortal; CPX-5544; DNA polymerase V mutasome complex.
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; 66674997; -.
DR GeneID; 945746; -.
DR KEGG; ecj:JW1172; -.
DR KEGG; eco:b1183; -.
DR PATRIC; fig|1411691.4.peg.1104; -.
DR EchoBASE; EB1050; -.
DR eggNOG; COG1974; Bacteria.
DR HOGENOM; CLU_066192_0_0_6; -.
DR InParanoid; P0AG11; -.
DR OMA; VQIWGVA; -.
DR PhylomeDB; P0AG11; -.
DR BioCyc; EcoCyc:EG11057-MON; -.
DR BioCyc; MetaCyc:EG11057-MON; -.
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:ATP-dependent activity, acting on DNA; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0009432; P:SOS response; IDA:ComplexPortal.
DR GO; GO:0019985; P:translesion synthesis; IDA:ComplexPortal.
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:0007829|PDB:1UMU"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1UMU"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:1UMU"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:1I4V"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1UMU"
FT STRAND 71..75
FT /evidence="ECO:0007829|PDB:1UMU"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:1I4V"
FT STRAND 85..90
FT /evidence="ECO:0007829|PDB:1UMU"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:1UMU"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1UMU"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1UMU"
FT STRAND 120..124
FT /evidence="ECO:0007829|PDB:1I4V"
FT STRAND 125..135
FT /evidence="ECO:0007829|PDB:1UMU"
SQ SEQUENCE 139 AA; 15063 MW; 0681A3FFAC7ED583 CRC64;
MLFIKPADLR EIVTFPLFSD LVQCGFPSPA ADYVEQRIDL NQLLIQHPSA TYFVKASGDS
MIDGGISDGD LLIVDSAITA SHGDIVIAAV DGEFTVKKLQ LRPTVQLIPM NSAYSPITIS
SEDTLDVFGV VIHVVKAMR
