ID   UNG_HELPG               Reviewed;         233 AA.
AC   B5Z8Z4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 65.
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}; OrderedLocusNames=HPG27_1295;
OS   Helicobacter pylori (strain G27).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=563041;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G27;
RX   PubMed=18952803; DOI=10.1128/jb.01416-08;
RA   Baltrus D.A., Amieva M.R., Covacci A., Lowe T.M., Merrell D.S.,
RA   Ottemann K.M., Stein M., Salama N.R., Guillemin K.;
RT   "The complete genome sequence of Helicobacter pylori strain G27.";
RL   J. Bacteriol. 191:447-448(2009).
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; CP001173; ACI28043.1; -; Genomic_DNA.
DR   RefSeq; WP_000764889.1; NC_011333.1.
DR   AlphaFoldDB; B5Z8Z4; -.
DR   SMR; B5Z8Z4; -.
DR   EnsemblBacteria; ACI28043; ACI28043; HPG27_1295.
DR   KEGG; hpg:HPG27_1295; -.
DR   HOGENOM; CLU_032162_3_2_7; -.
DR   OMA; PDNGYLM; -.
DR   OrthoDB; 1260295at2; -.
DR   Proteomes; UP000001735; 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..233
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_1000096585"
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00148"
SQ   SEQUENCE   233 AA;  26254 MW;  C01EB400B22D268A CRC64;
     MKLFDYAPLS LAWREFLQSE FKKPYFLEIE KRYLEALKSP KTIFPKSSNL FYALNLTPPS
     AVKIILLGQD PYHSTYLENE QELPVAMGLS FSVEKNAPIP PSLKNIFKEL HANLGVPVPC
     CGDLSAWAKR GMLLLNAILS VEKNQAASHQ YIGWEAFSDQ ILMRLFKTTA PLIVVLLGKV
     AQKKIALIPK NKHIIITAPH PSPLSRGFLG SGVFSSVQKA YREVYRKDFD FSL