ID   MUG_SHIDS               Reviewed;         168 AA.
AC   Q32BP9;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=G/U mismatch-specific DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_01956};
DE            EC=3.2.2.28 {ECO:0000255|HAMAP-Rule:MF_01956};
DE   AltName: Full=Double-strand-specific uracil glycosylase {ECO:0000255|HAMAP-Rule:MF_01956};
DE   AltName: Full=Mismatch-specific uracil DNA-glycosylase {ECO:0000255|HAMAP-Rule:MF_01956};
DE            Short=MUG {ECO:0000255|HAMAP-Rule:MF_01956};
GN   Name=mug {ECO:0000255|HAMAP-Rule:MF_01956}; OrderedLocusNames=SDY_3252;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
CC   -!- FUNCTION: Excises ethenocytosine and uracil, which can arise by
CC       alkylation or deamination of cytosine, respectively, from the
CC       corresponding mispairs with guanine in ds-DNA. It is capable of
CC       hydrolyzing the carbon-nitrogen bond between the sugar-phosphate
CC       backbone of the DNA and the mispaired base. The complementary strand
CC       guanine functions in substrate recognition. Required for DNA damage
CC       lesion repair in stationary-phase cells. {ECO:0000255|HAMAP-
CC       Rule:MF_01956}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Specifically hydrolyzes mismatched double-stranded DNA and
CC         polynucleotides, releasing free uracil.; EC=3.2.2.28;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01956};
CC   -!- SUBUNIT: Binds DNA as a monomer. {ECO:0000255|HAMAP-Rule:MF_01956}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01956}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       TDG/mug family. {ECO:0000255|HAMAP-Rule:MF_01956}.
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DR   EMBL; CP000034; ABB63256.1; -; Genomic_DNA.
DR   RefSeq; WP_000228931.1; NC_007606.1.
DR   RefSeq; YP_404747.1; NC_007606.1.
DR   AlphaFoldDB; Q32BP9; -.
DR   SMR; Q32BP9; -.
DR   STRING; 300267.SDY_3252; -.
DR   EnsemblBacteria; ABB63256; ABB63256; SDY_3252.
DR   KEGG; sdy:SDY_3252; -.
DR   PATRIC; fig|300267.13.peg.3887; -.
DR   HOGENOM; CLU_042829_3_1_6; -.
DR   OMA; FWPVLHL; -.
DR   Proteomes; UP000002716; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008263; F:pyrimidine-specific mismatch base pair DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006285; P:base-excision repair, AP site formation; IEA:UniProtKB-UniRule.
DR   CDD; cd10028; UDG-F2_TDG_MUG; 1.
DR   Gene3D; 3.40.470.10; -; 1.
DR   HAMAP; MF_01956; MUG; 1.
DR   InterPro; IPR015637; MUG/TDG.
DR   InterPro; IPR023502; MUG_bact.
DR   InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR   InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR   PANTHER; PTHR12159; PTHR12159; 1.
DR   Pfam; PF03167; UDG; 1.
DR   SUPFAM; SSF52141; SSF52141; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA excision; DNA repair; DNA-binding; Hydrolase;
KW   Reference proteome.
FT   CHAIN           1..168
FT                   /note="G/U mismatch-specific DNA glycosylase"
FT                   /id="PRO_0000238686"
SQ   SEQUENCE   168 AA;  18659 MW;  9CA9BBDA9A2E3F13 CRC64;
     MVEDILAPGL RVVFCGINPG LSSAGTGFPF AHPANRFWKV IYQAGFTDRQ LKPQEAQHLL
     DYRCGVTKLV DRPTVQANEI SNQELHAGGR KLIEKIEDYQ PQALAILGKQ AYEQGFSQRG
     AQWGKQTLSI GSTQIWVLPN PSGLSRVSLE KLVEAYRELD QALVVRGR