ID   UNG_CAMJJ               Reviewed;         231 AA.
AC   A1VXG9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00148};
DE            Short=UDG {ECO:0000255|HAMAP-Rule:MF_00148};
DE            EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_00148};
GN   Name=ung {ECO:0000255|HAMAP-Rule:MF_00148};
GN   OrderedLocusNames=CJJ81176_0121;
OS   Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=354242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=81-176;
RA   Fouts D.E., Nelson K.E., Sebastian Y.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000538; EAQ71923.1; -; Genomic_DNA.
DR   RefSeq; WP_002854281.1; NC_008787.1.
DR   AlphaFoldDB; A1VXG9; -.
DR   SMR; A1VXG9; -.
DR   STRING; 354242.CJJ81176_0121; -.
DR   EnsemblBacteria; EAQ71923; EAQ71923; CJJ81176_0121.
DR   KEGG; cjj:CJJ81176_0121; -.
DR   eggNOG; COG0692; Bacteria.
DR   HOGENOM; CLU_032162_1_1_7; -.
DR   OMA; PDNGYLM; -.
DR   Proteomes; UP000000646; 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.
FT   CHAIN           1..231
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_1000009876"
FT   ACT_SITE        74
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00148"
SQ   SEQUENCE   231 AA;  26314 MW;  EE514FCA18BEC2E3 CRC64;
     MEEITINIDK IKINDDWKEF LRDEFQKKYF LEIKKQYLNA INQNIIIYPP ANLIFNAFNL
     CPLKEIKIII LGQDPYHQPN QAMGLSFSVP KNVKIPPSLN NIFKELQNDL NITPAKSGDL
     SSWAKQGVLL LNSILSVEAN KAASHSSWGW QEFSDAIIHK LSNEKSGLVF MLWGNYAKSK
     EILIDNTKHL ILKAAHPSPL ARTGFLGCKH FSKANEFLKK VGKIPIDWKI V