ID   UMUD_ECO57              Reviewed;         139 AA.
AC   P0AG12; P04153;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1986, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Protein UmuD;
DE            EC=3.4.21.-;
DE   Contains:
DE     RecName: Full=Protein UmuD';
GN   Name=umuD; OrderedLocusNames=Z1946, ECs1678;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Involved in UV protection and mutation. Essential for induced
CC       (or SOS) mutagenesis. May modify the DNA replication machinery to allow
CC       bypass synthesis across a damaged template (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase S24 family. {ECO:0000305}.
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DR   EMBL; AE005174; AAG56034.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35101.1; -; Genomic_DNA.
DR   PIR; F85696; F85696.
DR   PIR; F90838; F90838.
DR   RefSeq; NP_309705.1; NC_002695.1.
DR   RefSeq; WP_000897378.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; P0AG12; -.
DR   BMRB; P0AG12; -.
DR   SMR; P0AG12; -.
DR   STRING; 155864.EDL933_1877; -.
DR   MEROPS; S24.003; -.
DR   EnsemblBacteria; AAG56034; AAG56034; Z1946.
DR   EnsemblBacteria; BAB35101; BAB35101; ECs_1678.
DR   GeneID; 66674997; -.
DR   GeneID; 913194; -.
DR   KEGG; ece:Z1946; -.
DR   KEGG; ecs:ECs_1678; -.
DR   PATRIC; fig|386585.9.peg.1775; -.
DR   eggNOG; COG1974; Bacteria.
DR   HOGENOM; CLU_066192_0_0_6; -.
DR   OMA; VQIWGVA; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; IEA:UniProtKB-KW.
DR   CDD; cd06529; S24_LexA-like; 1.
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   3: Inferred from homology;
KW   Autocatalytic cleavage; DNA damage; DNA repair; Hydrolase; Protease;
KW   Reference proteome; Serine protease; SOS mutagenesis; SOS response.
FT   CHAIN           1..139
FT                   /note="Protein UmuD"
FT                   /id="PRO_0000045244"
FT   CHAIN           25..139
FT                   /note="Protein UmuD'"
FT                   /id="PRO_0000045246"
FT   ACT_SITE        60
FT                   /note="For autocatalytic cleavage activity"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        97
FT                   /note="For autocatalytic cleavage activity"
FT                   /evidence="ECO:0000250"
FT   SITE            24..25
FT                   /note="Cleavage; by autolysis"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   139 AA;  15063 MW;  0681A3FFAC7ED583 CRC64;
     MLFIKPADLR EIVTFPLFSD LVQCGFPSPA ADYVEQRIDL NQLLIQHPSA TYFVKASGDS
     MIDGGISDGD LLIVDSAITA SHGDIVIAAV DGEFTVKKLQ LRPTVQLIPM NSAYSPITIS
     SEDTLDVFGV VIHVVKAMR