ID   MUG_SALPC               Reviewed;         168 AA.
AC   C0PYY5;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 62.
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=SPC_3288;
OS   Salmonella paratyphi C (strain RKS4594).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=476213;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RKS4594;
RX   PubMed=19229335; DOI=10.1371/journal.pone.0004510;
RA   Liu W.-Q., Feng Y., Wang Y., Zou Q.-H., Chen F., Guo J.-T., Peng Y.-H.,
RA   Jin Y., Li Y.-G., Hu S.-N., Johnston R.N., Liu G.-R., Liu S.-L.;
RT   "Salmonella paratyphi C: genetic divergence from Salmonella choleraesuis
RT   and pathogenic convergence with Salmonella typhi.";
RL   PLoS ONE 4:E4510-E4510(2009).
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; CP000857; ACN47373.1; -; Genomic_DNA.
DR   RefSeq; WP_000237776.1; NC_012125.1.
DR   AlphaFoldDB; C0PYY5; -.
DR   SMR; C0PYY5; -.
DR   EnsemblBacteria; ACN47373; ACN47373; SPC_3288.
DR   KEGG; sei:SPC_3288; -.
DR   HOGENOM; CLU_042829_3_1_6; -.
DR   OMA; FWPVLHL; -.
DR   Proteomes; UP000001599; 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.
FT   CHAIN           1..168
FT                   /note="G/U mismatch-specific DNA glycosylase"
FT                   /id="PRO_1000188968"
SQ   SEQUENCE   168 AA;  18650 MW;  A946974A29B16FF5 CRC64;
     MVKDILAPGL RVVFCGINPG LSSANTGFPF AHPANRFWKV IHLAGFTDRQ LKPEEAEKLL
     DFRCGVTKLV DRPTVQATEV KLHELRSGGR NLIEKIEDYQ PAALAVLGKQ AFEQGFSQRG
     IAWGKQKIAI GATMVWVLPN PSGLNRIKTE KLVEAYRELD QALIMRGL