ID   UNG2_BACFN              Reviewed;         220 AA.
AC   Q5L9D9;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Uracil-DNA glycosylase 2 {ECO:0000255|HAMAP-Rule:MF_00148};
DE            Short=UDG 2 {ECO:0000255|HAMAP-Rule:MF_00148};
DE            EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_00148};
GN   Name=ung2 {ECO:0000255|HAMAP-Rule:MF_00148}; OrderedLocusNames=BF3608;
OS   Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS   / NCTC 9343 / Onslow).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=272559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 / Onslow;
RX   PubMed=15746427; DOI=10.1126/science.1107008;
RA   Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA   Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA   Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA   Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA   Barrell B.G., Parkhill J.;
RT   "Extensive DNA inversions in the B. fragilis genome control variable gene
RT   expression.";
RL   Science 307:1463-1465(2005).
CC   -!- FUNCTION: Excises uracil residues from the DNA which can arise as a
CC       result of misincorporation of dUMP residues by DNA polymerase or due to
CC       deamination of cytosine. {ECO:0000255|HAMAP-Rule:MF_00148}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes single-stranded DNA or mismatched double-stranded
CC         DNA and polynucleotides, releasing free uracil.; EC=3.2.2.27;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00148};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00148}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       UNG family. {ECO:0000255|HAMAP-Rule:MF_00148}.
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DR   EMBL; CR626927; CAH09289.1; -; Genomic_DNA.
DR   RefSeq; WP_005798174.1; NC_003228.3.
DR   AlphaFoldDB; Q5L9D9; -.
DR   SMR; Q5L9D9; -.
DR   STRING; 272559.BF9343_3508; -.
DR   EnsemblBacteria; CAH09289; CAH09289; BF9343_3508.
DR   GeneID; 66331552; -.
DR   KEGG; bfs:BF9343_3508; -.
DR   eggNOG; COG0692; Bacteria.
DR   HOGENOM; CLU_032162_3_0_10; -.
DR   OMA; PDNGYLM; -.
DR   OrthoDB; 1260295at2; -.
DR   Proteomes; UP000006731; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-UniRule.
DR   CDD; cd10027; UDG-F1-like; 1.
DR   Gene3D; 3.40.470.10; -; 1.
DR   HAMAP; MF_00148; UDG; 1.
DR   InterPro; IPR002043; UDG_fam1.
DR   InterPro; IPR018085; Ura-DNA_Glyclase_AS.
DR   InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR   InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR   PANTHER; PTHR11264; PTHR11264; 1.
DR   Pfam; PF03167; UDG; 1.
DR   SMART; SM00986; UDG; 1.
DR   SUPFAM; SSF52141; SSF52141; 1.
DR   TIGRFAMs; TIGR00628; ung; 1.
DR   PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA repair; Hydrolase; Reference proteome.
FT   CHAIN           1..220
FT                   /note="Uracil-DNA glycosylase 2"
FT                   /id="PRO_0000176060"
FT   ACT_SITE        65
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00148"
SQ   SEQUENCE   220 AA;  24998 MW;  63BFB3CFD93566B6 CRC64;
     MNVQIEESWK THLEPEFEKD YFRTLTEFVR SEYSQYQIFP PGKLIFNAFN LCPFDKVKVV
     IIGQDPYHGP GQAHGLCFSV NDGVAFPPSL VNIFKEIKED IGTPAPSTGN LTRWAEQGVL
     LLNATLTVRA HQAGSHQRRG WEEFTDAAIR VLAEERENLV FILWGSYAQK KGAFIDRNKH
     LVLSSAHPSP LSAYNGFFGN KHFSKTNEYL KAHGKTEINW