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Database: UniProt
Entry: E5B6G2_ERWAM
LinkDB: E5B6G2_ERWAM
Original site: E5B6G2_ERWAM 
ID   E5B6G2_ERWAM            Unreviewed;       139 AA.
AC   E5B6G2;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Error-prone repair, SOS-response transcriptional repressor {ECO:0000313|EMBL:CBX80982.1};
DE            EC=3.4.21.- {ECO:0000313|EMBL:CBX80982.1};
GN   Name=umuD {ECO:0000313|EMBL:CBX80982.1};
GN   ORFNames=EAIL5_2162 {ECO:0000313|EMBL:CBX80982.1};
OS   Erwinia amylovora ATCC BAA-2158.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=889211 {ECO:0000313|EMBL:CBX80982.1};
RN   [1] {ECO:0000313|EMBL:CBX80982.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC BAA-2158 {ECO:0000313|EMBL:CBX80982.1};
RA   Powney R., Smits T.H., Sawbridge T., Frey B., Blom J., Frey J.E.,
RA   Plummer K.M., Beer S.V., Luck J., Duffy B., Rodoni B.;
RT   "Genome Sequence of an Erwinia amylovora Strain with Pathogenicity
RT   Restricted to Rubus Plants.";
RL   J. Bacteriol. 193:785-786(2011).
CC   -!- SIMILARITY: Belongs to the peptidase S24 family.
CC       {ECO:0000256|ARBA:ARBA00007484, ECO:0000256|RuleBase:RU003991}.
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DR   EMBL; FR719191; CBX80982.1; -; Genomic_DNA.
DR   AlphaFoldDB; E5B6G2; -.
DR   MEROPS; S24.003; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR   CDD; cd06529; S24_LexA-like; 1.
DR   Gene3D; 2.10.109.10; Umud Fragment, subunit A; 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   PANTHER; PTHR33516; LEXA REPRESSOR; 1.
DR   PANTHER; PTHR33516:SF13; PROPHAGE REPRESSOR COHE-RELATED; 1.
DR   Pfam; PF00717; Peptidase_S24; 1.
DR   PRINTS; PR00726; LEXASERPTASE.
DR   SUPFAM; SSF51306; LexA/Signal peptidase; 1.
PE   3: Inferred from homology;
KW   Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813,
KW   ECO:0000256|RuleBase:RU003991}; DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003991};
KW   Protease {ECO:0000256|ARBA:ARBA00022825};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   SOS mutagenesis {ECO:0000256|ARBA:ARBA00023199};
KW   SOS response {ECO:0000256|ARBA:ARBA00023236}.
FT   DOMAIN          16..131
FT                   /note="Peptidase S24/S26A/S26B/S26C"
FT                   /evidence="ECO:0000259|Pfam:PF00717"
SQ   SEQUENCE   139 AA;  15411 MW;  508A0296B3678049 CRC64;
     MPLIRPLDID CSLLLPLFSE RVPCGFPSPA QDYVEDRIDL NKLAIKHPSA TYFIKVSGDS
     MCEAGIGDGD LLIVDRSLNA VHGDIVVAAI AGEFTVKELR THPFLQLVPH NPHYSPISFR
     NEEELEIFGV VTFTLKAHK
//
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