ID   UMUD_SHIFL              Reviewed;         139 AA.
AC   P0AG13; P04153;
DT   01-NOV-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1986, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Protein UmuD;
DE            EC=3.4.21.-;
DE   Contains:
DE     RecName: Full=Protein UmuD';
GN   Name=umuD; OrderedLocusNames=SF1172, S1260;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN42787.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16678.1; -; Genomic_DNA.
DR   RefSeq; NP_707080.1; NC_004337.2.
DR   RefSeq; WP_000897378.1; NZ_WPGW01000047.1.
DR   AlphaFoldDB; P0AG13; -.
DR   BMRB; P0AG13; -.
DR   SMR; P0AG13; -.
DR   STRING; 198214.SF1172; -.
DR   MEROPS; S24.003; -.
DR   EnsemblBacteria; AAN42787; AAN42787; SF1172.
DR   EnsemblBacteria; AAP16678; AAP16678; S1260.
DR   GeneID; 1024107; -.
DR   GeneID; 66674997; -.
DR   KEGG; sfl:SF1172; -.
DR   KEGG; sfx:S1260; -.
DR   PATRIC; fig|198214.7.peg.1386; -.
DR   HOGENOM; CLU_066192_0_0_6; -.
DR   OMA; VQIWGVA; -.
DR   OrthoDB; 1933795at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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_0000045247"
FT   CHAIN           25..139
FT                   /note="Protein UmuD'"
FT                   /id="PRO_0000045249"
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