ID   UNG_ECOBW               Reviewed;         229 AA.
AC   C4ZYK3;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   01-MAY-2013, entry version 27.
DE   RecName: Full=Uracil-DNA glycosylase;
DE            Short=UDG;
DE            EC=3.2.2.27;
GN   Name=ung; OrderedLocusNames=BWG_2344;
OS   Escherichia coli (strain K12 / MC4100 / BW2952).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=595496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MC4100 / BW2952;
RX   PubMed=19376874; DOI=10.1128/JB.00118-09;
RA   Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L.,
RA   Reeves P.R., Wang L.;
RT   "Genomic sequencing reveals regulatory mutations and recombinational
RT   events in the widely used MC4100 lineage of Escherichia coli K-12.";
RL   J. Bacteriol. 191:4025-4029(2009).
CC   -!- FUNCTION: Excises uracil residues from the DNA which can arise as
CC       a result of misincorporation of dUMP residues by DNA polymerase or
CC       due to deamination of cytosine (By similarity).
CC   -!- CATALYTIC ACTIVITY: Hydrolyzes single-stranded DNA or mismatched
CC       double-stranded DNA and polynucleotides, releasing free uracil.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase family.
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DR   EMBL; CP001396; ACR65765.1; -; Genomic_DNA.
DR   RefSeq; YP_002927541.1; NC_012759.1.
DR   ProteinModelPortal; C4ZYK3; -.
DR   SMR; C4ZYK3; 3-225.
DR   STRING; 595496.BWG_2344; -.
DR   PRIDE; C4ZYK3; -.
DR   EnsemblBacteria; ACR65765; ACR65765; BWG_2344.
DR   GeneID; 7955850; -.
DR   KEGG; ebw:BWG_2344; -.
DR   PATRIC; 18274094; VBIEscCol60876_2564.
DR   eggNOG; COG0692; -.
DR   HOGENOM; HOG000229528; -.
DR   KO; K03648; -.
DR   OMA; AGKEIYP; -.
DR   ProtClustDB; PRK05254; -.
DR   BioCyc; ECOL595496:GI18-4226-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:HAMAP.
DR   GO; GO:0006284; P:base-excision repair; IEA:HAMAP.
DR   Gene3D; 3.40.470.10; -; 1.
DR   HAMAP; MF_00148; UDG; 1; -.
DR   InterPro; IPR018085; Ura-DNA_Glyclase_AS.
DR   InterPro; IPR002043; Ura_DNA_glycsylse.
DR   InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR   PANTHER; PTHR11264; PTHR11264; 1.
DR   Pfam; PF03167; UDG; 1.
DR   SMART; SM00986; UDG; 1.
DR   SUPFAM; SSF52141; UDNA_glycsylseSF; 1.
DR   TIGRFAMs; TIGR00628; ung; 1.
DR   PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; DNA damage; DNA repair; Glycosidase;
KW   Hydrolase.
FT   CHAIN         1    229       Uracil-DNA glycosylase.
FT                                /FTId=PRO_1000203374.
FT   ACT_SITE     64     64       Proton acceptor (By similarity).
SQ   SEQUENCE   229 AA;  25693 MW;  CD44F1E214FE74ED CRC64;
     MANELTWHDV LAEEKQQPYF LNTLQTVASE RQSGVTIYPP QKDVFNAFRF TELGDVKVVI
     LGQDPYHGPG QAHGLAFSVR PGIAIPPSLL NMYKELENTI PGFTRPNHGY LESWARQGVL
     LLNTVLTVRA GQAHSHASLG WETFTDKVIS LINQHREGVV FLLWGSHAQK KGAIIDKQRH
     HVLKAPHPSP LSAHRGFFGC NHFVLANQWL EQRGETPIDW MPVLPAESE
//