ID   MUG_SALPB               Reviewed;         168 AA.
AC   A9N5Z1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=SPAB_04008;
OS   Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=1016998;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1250 / SPB7;
RG   The Salmonella enterica serovar Paratyphi B Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S.,
RA   Fulton R., Cordes M., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W.,
RA   Johnson M., Thiruvilangam P., Wilson R.;
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000886; ABX69337.1; -; Genomic_DNA.
DR   RefSeq; WP_000237772.1; NC_010102.1.
DR   AlphaFoldDB; A9N5Z1; -.
DR   SMR; A9N5Z1; -.
DR   KEGG; spq:SPAB_04008; -.
DR   PATRIC; fig|1016998.12.peg.3779; -.
DR   HOGENOM; CLU_042829_3_1_6; -.
DR   OMA; FWPVLHL; -.
DR   BioCyc; SENT1016998:SPAB_RS16280-MON; -.
DR   Proteomes; UP000008556; 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_1000088517"
SQ   SEQUENCE   168 AA;  18622 MW;  A94586096CB02BB7 CRC64;
     MVKDILAPGL RVVFCGINPG LSSANTGFPF AHPANRFWKV IHLAGFSDRQ LKPEEAEKLL
     DFRCGVTKLV DRPTVQATEV KLHELRSGGR NLIDKIEDYQ PAALAVLGKQ AFEQGFSQRG
     IAWGKQKIAI GATMVWVLPN PSGLNRIKTE KLVEAYRELD QALIMRGL