ID   UNG_CHLTR               Reviewed;         229 AA.
AC   O84613;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Uracil-DNA glycosylase;
DE            Short=UDG;
DE            EC=3.2.2.27;
GN   Name=ung; OrderedLocusNames=CT_607;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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; AE001273; AAC68210.1; -; Genomic_DNA.
DR   PIR; C71493; C71493.
DR   RefSeq; NP_220124.1; NC_000117.1.
DR   RefSeq; WP_009871975.1; NC_000117.1.
DR   AlphaFoldDB; O84613; -.
DR   SMR; O84613; -.
DR   STRING; 813.O172_03320; -.
DR   EnsemblBacteria; AAC68210; AAC68210; CT_607.
DR   GeneID; 884388; -.
DR   KEGG; ctr:CT_607; -.
DR   PATRIC; fig|272561.5.peg.664; -.
DR   HOGENOM; CLU_032162_3_0_0; -.
DR   InParanoid; O84613; -.
DR   OMA; PDNGYLM; -.
DR   Proteomes; UP000000431; 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..229
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000176084"
FT   ACT_SITE        70
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   229 AA;  26002 MW;  9AD49846F8DCDC3B CRC64;
     MHEAFTIEQL PPSWQEQLKD EWSQPYWSQL LAFLKSEYAQ ATIYPKKENV FAALQSTPFD
     QVRVVILGQD PYHGEGQAHG LSFSVPRGQA LPPSLRNIFQ ELHTDLGIRN ESGCLQAWAD
     QGVLLLNTVL TVRAGEAFSH AGRGWERFTD AIVTKLIQNR THVIFVLWGN AARQKCNLLF
     QTKHQHAVLA CPHPSPLAAH RGFFGCCHFS KINYLLKKQG KTMINWKIE