ID UNG_ECOUT Reviewed; 229 AA.
AC Q1R8F2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 01-MAY-2013, entry version 48.
DE RecName: Full=Uracil-DNA glycosylase;
DE Short=UDG;
DE EC=3.2.2.27;
GN Name=ung; OrderedLocusNames=UTI89_C2902;
OS Escherichia coli (strain UTI89 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=364106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTI89 / UPEC;
RX PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R.,
RA Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R.,
RA Hultgren S.J., Gordon J.I.;
RT "Identification of genes subject to positive selection in
RT uropathogenic strains of Escherichia coli: a comparative genomics
RT approach.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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; CP000243; ABE08362.1; -; Genomic_DNA.
DR RefSeq; YP_541893.1; NC_007946.1.
DR ProteinModelPortal; Q1R8F2; -.
DR SMR; Q1R8F2; 1-229.
DR STRING; 364106.UTI89_C2902; -.
DR EnsemblBacteria; ABE08362; ABE08362; UTI89_C2902.
DR GeneID; 3992210; -.
DR KEGG; eci:UTI89_C2902; -.
DR PATRIC; 18455342; VBIEscCol42261_2901.
DR eggNOG; COG0692; -.
DR HOGENOM; HOG000229528; -.
DR KO; K03648; -.
DR OMA; AGKEIYP; -.
DR ProtClustDB; PRK05254; -.
DR BioCyc; ECOL364106:GHPQ-2943-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_1000009887.
FT ACT_SITE 64 64 Proton acceptor (By similarity).
SQ SEQUENCE 229 AA; 25681 MW; E94F193824FE6137 CRC64;
MANELTWHDV LAEEKQQPYF LNTLQTVASE RQSGVTIYPP QKDVFNAFRF TELGDVKVVI
LGQDPYHGPG QAHGLAFSVR PGIATPPSLL NMYKELENTI PGFTRPNHGY LESWARQGVL
LLNTVLTVRA GQAHSHASLG WETFTDKVIS LINQHREGVV FLLWGSHAQK KGAIIDKQRH
HVLKAPHPSP LSAHRGFFGC NHFVLANQWL EQRGETPIDW MPVLPAESE
//
