ID   UNG_HELPY               Reviewed;         233 AA.
AC   P56397;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   25-MAY-2022, entry version 115.
DE   RecName: Full=Uracil-DNA glycosylase;
DE            Short=UDG;
DE            EC=3.2.2.27;
GN   Name=ung; OrderedLocusNames=HP_1347;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
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:0000250}.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       UNG family. {ECO:0000305}.
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DR   EMBL; AE000511; AAD08392.1; -; Genomic_DNA.
DR   PIR; C64688; C64688.
DR   RefSeq; NP_208139.1; NC_000915.1.
DR   RefSeq; WP_000764827.1; NC_018939.1.
DR   AlphaFoldDB; P56397; -.
DR   SMR; P56397; -.
DR   STRING; 85962.C694_06950; -.
DR   PaxDb; P56397; -.
DR   EnsemblBacteria; AAD08392; AAD08392; HP_1347.
DR   KEGG; hpy:HP_1347; -.
DR   PATRIC; fig|85962.47.peg.1442; -.
DR   eggNOG; COG0692; Bacteria.
DR   OMA; PDNGYLM; -.
DR   PhylomeDB; P56397; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IBA:GO_Central.
DR   GO; GO:0097510; P:base-excision repair, AP site formation via deaminated base removal; IBA:GO_Central.
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..233
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000176102"
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   233 AA;  26297 MW;  83BE8E39E6854B5E CRC64;
     MKLFDYAPLS LAWREFLQSE FKKPYFLEIE KRYLEALKIP KTIFPKSSNL FYALNLTPPC
     AVKIILLGQD PYHSTYLEND QELPVAMGLS FSVEKNAPIP PSLKNIFKEL HANLGVPVPC
     CGDLSAWAKR GMLLLNAILS VEKNQAASHQ YIGWEAFSDQ ILMRLFETTA PLIVVLLGKV
     AQKKIALIPK NKHIIITAPH PSPLSRGFLG SGVFTSVQKA YREVYRKDFD FSL