ID   UNG_ECOLI               Reviewed;         229 AA.
AC   P12295;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 192.
DE   RecName: Full=Uracil-DNA glycosylase;
DE            Short=UDG;
DE            EC=3.2.2.27;
GN   Name=ung; OrderedLocusNames=b2580, JW2564;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-32.
RX   PubMed=2836397; DOI=10.1016/s0021-9258(18)68566-7;
RA   Varshney U., Hutcheon T., de Sande J.H.;
RT   "Sequence analysis, expression, and conservation of Escherichia coli uracil
RT   DNA glycosylase and its gene (ung).";
RL   J. Biol. Chem. 263:7776-7784(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RA   Nashimoto H.;
RT   "Non-ribosomal proteins affecting the assembly of ribosomes in Escherichia
RT   coli.";
RL   (In) Nierhaus K.H. (eds.);
RL   The translational apparatus, pp.185-195, Plenum Press, New York (1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RA   Nashimoto H., Saito N.;
RL   Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [7]
RP   STRUCTURE BY NMR.
RX   PubMed=9261156; DOI=10.1074/jbc.272.34.21408;
RA   Lundquist A.J., Beger R.D., Bennett S.E., Bolton P.H., Mosbaugh D.W.;
RT   "Site-directed mutagenesis and characterization of uracil-DNA glycosylase
RT   inhibitor protein. Role of specific carboxylic amino acids in complex
RT   formation with Escherichia coli uracil-DNA glycosylase.";
RL   J. Biol. Chem. 272:21408-21419(1997).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
RX   PubMed=9776748; DOI=10.1093/nar/26.21.4880;
RA   Ravishankar R., Sagar M.B., Roy S., Purnapatre K., Handa P., Varshney U.,
RA   Vijayan M.;
RT   "X-ray analysis of a complex of Escherichia coli uracil DNA glycosylase
RT   (EcUDG) with a proteinaceous inhibitor. The structure elucidation of a
RT   prokaryotic UDG.";
RL   Nucleic Acids Res. 26:4880-4887(1998).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
RX   PubMed=10080896; DOI=10.1006/jmbi.1999.2605;
RA   Putnam C.D., Shroyer M.J.N., Lundquist A.J., Mol C.D., Arvai A.S.,
RA   Mosbaugh D.W., Tainer J.A.;
RT   "Protein mimicry of DNA from crystal structures of the uracil-DNA
RT   glycosylase inhibitor protein and its complex with Escherichia coli uracil-
RT   DNA glycosylase.";
RL   J. Mol. Biol. 287:331-346(1999).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX   PubMed=10090282;
RX   DOI=10.1002/(sici)1097-0134(19990401)35:1<13::aid-prot2>3.3.co;2-u;
RA   Xiao G., Tordova M., Jagadeesh J., Drohat A.C., Stivers J.T.,
RA   Gilliland G.L.;
RT   "Crystal structure of Escherichia coli uracil DNA glycosylase and its
RT   complexes with uracil and glycerol: structure and glycosylase mechanism
RT   revisited.";
RL   Proteins 35:13-24(1999).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   PubMed=11027138; DOI=10.1021/bi001532v;
RA   Werner R.M., Jiang Y.L., Gordley R.G., Jagadeesh G.J., Ladner J.E.,
RA   Xiao G., Tordova M., Gilliland G.L., Stivers J.T.;
RT   "Stressing-out DNA? The contribution of serine-phosphodiester interactions
RT   in catalysis by uracil DNA glycosylase.";
RL   Biochemistry 39:12585-12594(2000).
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.
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   -!- SUBUNIT: Monomer.
CC   -!- INTERACTION:
CC       P12295; P08957: hsdM; NbExp=3; IntAct=EBI-559403, EBI-878571;
CC       P12295; P0A763: ndk; NbExp=3; IntAct=EBI-559403, EBI-370139;
CC       P12295; P14739: UGI; Xeno; NbExp=4; IntAct=EBI-559403, EBI-1025973;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       UNG family. {ECO:0000305}.
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DR   EMBL; J03725; AAA24743.1; -; Genomic_DNA.
DR   EMBL; D13169; BAA02448.1; -; Genomic_DNA.
DR   EMBL; D64044; BAA10923.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75633.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16466.1; -; Genomic_DNA.
DR   PIR; A28175; DGECU.
DR   RefSeq; NP_417075.1; NC_000913.3.
DR   RefSeq; WP_001262716.1; NZ_STEB01000011.1.
DR   PDB; 1EUG; X-ray; 1.60 A; A=1-229.
DR   PDB; 1EUI; X-ray; 3.20 A; A/B=2-229.
DR   PDB; 1FLZ; X-ray; 2.30 A; A=2-229.
DR   PDB; 1LQG; X-ray; 2.90 A; A/B=2-229.
DR   PDB; 1LQJ; X-ray; 3.35 A; A/B/C/D=2-229.
DR   PDB; 1LQM; X-ray; 3.20 A; A/C/E/G=2-229.
DR   PDB; 1UUG; X-ray; 2.40 A; A/C=1-229.
DR   PDB; 2EUG; X-ray; 1.50 A; A=1-229.
DR   PDB; 2UUG; X-ray; 2.60 A; A/B=1-229.
DR   PDB; 3EUG; X-ray; 1.43 A; A=1-229.
DR   PDB; 3UF7; X-ray; 1.20 A; A=1-229.
DR   PDB; 4EUG; X-ray; 1.40 A; A=1-229.
DR   PDB; 5EUG; X-ray; 1.60 A; A=1-229.
DR   PDBsum; 1EUG; -.
DR   PDBsum; 1EUI; -.
DR   PDBsum; 1FLZ; -.
DR   PDBsum; 1LQG; -.
DR   PDBsum; 1LQJ; -.
DR   PDBsum; 1LQM; -.
DR   PDBsum; 1UUG; -.
DR   PDBsum; 2EUG; -.
DR   PDBsum; 2UUG; -.
DR   PDBsum; 3EUG; -.
DR   PDBsum; 3UF7; -.
DR   PDBsum; 4EUG; -.
DR   PDBsum; 5EUG; -.
DR   AlphaFoldDB; P12295; -.
DR   SMR; P12295; -.
DR   BioGRID; 4263474; 132.
DR   BioGRID; 851404; 2.
DR   DIP; DIP-11092N; -.
DR   IntAct; P12295; 10.
DR   STRING; 511145.b2580; -.
DR   jPOST; P12295; -.
DR   PaxDb; 511145-b2580; -.
DR   EnsemblBacteria; AAC75633; AAC75633; b2580.
DR   GeneID; 947067; -.
DR   KEGG; ecj:JW2564; -.
DR   KEGG; eco:b2580; -.
DR   PATRIC; fig|1411691.4.peg.4154; -.
DR   EchoBASE; EB1051; -.
DR   eggNOG; COG0692; Bacteria.
DR   HOGENOM; CLU_032162_3_1_6; -.
DR   InParanoid; P12295; -.
DR   OMA; PDNGYLM; -.
DR   OrthoDB; 9804372at2; -.
DR   PhylomeDB; P12295; -.
DR   BioCyc; EcoCyc:EG11058-MONOMER; -.
DR   BioCyc; MetaCyc:EG11058-MONOMER; -.
DR   BRENDA; 3.2.2.27; 2026.
DR   SABIO-RK; P12295; -.
DR   EvolutionaryTrace; P12295; -.
DR   PRO; PR:P12295; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IDA:EcoCyc.
DR   GO; GO:0097510; P:base-excision repair, AP site formation via deaminated base removal; IDA:EcoCyc.
DR   CDD; cd10027; UDG-F1-like; 1.
DR   Gene3D; 3.40.470.10; Uracil-DNA glycosylase-like domain; 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   NCBIfam; TIGR00628; ung; 1.
DR   PANTHER; PTHR11264; URACIL-DNA GLYCOSYLASE; 1.
DR   PANTHER; PTHR11264:SF0; URACIL-DNA GLYCOSYLASE; 1.
DR   Pfam; PF03167; UDG; 1.
DR   SMART; SM00986; UDG; 1.
DR   SMART; SM00987; UreE_C; 1.
DR   SUPFAM; SSF52141; Uracil-DNA glycosylase-like; 1.
DR   PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; DNA damage; DNA repair;
KW   Hydrolase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2836397"
FT   CHAIN           2..229
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000176091"
FT   ACT_SITE        64
FT                   /note="Proton acceptor"
FT   HELIX           7..11
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   HELIX           14..16
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   HELIX           18..33
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   STRAND          37..39
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   HELIX           41..43
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   HELIX           46..50
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   STRAND          58..64
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   TURN            69..71
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   STRAND          74..77
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   STRAND          81..83
FT                   /evidence="ECO:0007829|PDB:1LQJ"
FT   HELIX           87..99
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   HELIX           112..115
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   TURN            116..118
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   STRAND          119..125
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   TURN            133..138
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   HELIX           141..155
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   STRAND          160..165
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   HELIX           166..171
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   TURN            172..174
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   TURN            177..179
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   STRAND          180..185
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   TURN            190..199
FT                   /evidence="ECO:0007829|PDB:3UF7"
FT   HELIX           202..212
FT                   /evidence="ECO:0007829|PDB:3UF7"
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
//