ID   UMUD_SALTY              Reviewed;         139 AA.
AC   P22493;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Protein UmuD;
DE            EC=3.4.21.-;
DE   Contains:
DE     RecName: Full=Protein UmuD';
GN   Name=umuD; OrderedLocusNames=STM1998;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=2144275; DOI=10.1128/jb.172.9.4964-4978.1990;
RA   Smith C.M., Koch W.H., Franklin S.B., Foster P.L., Cebula T.A.,
RA   Eisenstadt E.;
RT   "Sequence analysis and mapping of the Salmonella typhimurium LT2 umuDC
RT   operon.";
RL   J. Bacteriol. 172:4964-4978(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LT2;
RX   PubMed=2203737; DOI=10.1128/jb.172.9.4979-4987.1990;
RA   Thomas S.M., Crowne H.M., Pidsley S.C., Sedgwick S.G.;
RT   "Structural characterization of the Salmonella typhimurium LT2 umu
RT   operon.";
RL   J. Bacteriol. 172:4979-4987(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [4]
RP   PROTEOLYTIC PROCESSING.
RX   PubMed=1910151; DOI=10.1007/bf00264216;
RA   Woodgate R., Levine A.S., Koch W.H., Cebula T.A., Eisenstadt E.;
RT   "Induction and cleavage of Salmonella typhimurium UmuD protein.";
RL   Mol. Gen. Genet. 229:81-85(1991).
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.
CC   -!- SIMILARITY: Belongs to the peptidase S24 family. {ECO:0000305}.
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DR   EMBL; M57431; AAA27247.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20908.1; -; Genomic_DNA.
DR   PIR; A36713; A36713.
DR   RefSeq; NP_460949.1; NC_003197.2.
DR   RefSeq; WP_000394196.1; NC_003197.2.
DR   AlphaFoldDB; P22493; -.
DR   SMR; P22493; -.
DR   STRING; 99287.STM1998; -.
DR   MEROPS; S24.003; -.
DR   PaxDb; P22493; -.
DR   EnsemblBacteria; AAL20908; AAL20908; STM1998.
DR   GeneID; 1253519; -.
DR   KEGG; stm:STM1998; -.
DR   PATRIC; fig|99287.12.peg.2116; -.
DR   HOGENOM; CLU_066192_0_0_6; -.
DR   OMA; CVDRSLK; -.
DR   PhylomeDB; P22493; -.
DR   BioCyc; SENT99287:STM1998-MON; -.
DR   Proteomes; UP000001014; 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   1: Evidence at protein level;
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_0000041989"
FT   CHAIN           25..139
FT                   /note="Protein UmuD'"
FT                   /id="PRO_0000027307"
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"
SQ   SEQUENCE   139 AA;  15289 MW;  05FF3A508D84DAC5 CRC64;
     MEFFRPTELR EIIPLPFFSY LVPCGFPSPA ADYIEQRIDL NELLVSHPSS TYFVKASGDS
     MIEAGISDGD LLVVDSSRNA DHGDIVIAAI EGEFTVKRLQ LRPTVQLIPM NGAYRPIPVG
     SEDTLDIFGV VTFIIKAVS