ID   MUG_ECOLI               Reviewed;         168 AA.
AC   P0A9H1; P43342; Q2M9D7;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   27-MAR-2024, entry version 131.
DE   RecName: Full=G/U mismatch-specific DNA glycosylase;
DE            EC=3.2.2.28;
DE   AltName: Full=Double-strand-specific uracil glycosylase;
DE   AltName: Full=Mismatch-specific uracil DNA-glycosylase;
DE            Short=MUG;
GN   Name=mug; Synonyms=ygjF; OrderedLocusNames=b3068, JW3040;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
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   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-168.
RC   STRAIN=K12;
RX   PubMed=6269063; DOI=10.1093/nar/9.12.2889;
RA   Burton Z.F., Burgess R.R., Lin J., Moore D., Holder S., Gross C.A.;
RT   "The nucleotide sequence of the cloned rpoD gene for the RNA polymerase
RT   sigma subunit from E coli K12.";
RL   Nucleic Acids Res. 9:2889-2903(1981).
RN   [4]
RP   IDENTIFICATION.
RX   PubMed=7567469; DOI=10.1093/nar/23.17.3554;
RA   Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.;
RT   "Detection of new genes in a bacterial genome using Markov models for three
RT   gene classes.";
RL   Nucleic Acids Res. 23:3554-3562(1995).
RN   [5]
RP   FUNCTION.
RX   PubMed=8878487; DOI=10.1038/383735a0;
RA   Gallinari P., Jiricny J.;
RT   "A new class of uracil-DNA glycosylases related to human thymine-DNA
RT   glycosylase.";
RL   Nature 383:735-738(1996).
RN   [6]
RP   INDUCTION.
RX   PubMed=11555290; DOI=10.1046/j.1365-2958.2001.02559.x;
RA   Mokkapati S.K., Fernandez de Henestrosa A.R., Bhagwat A.S.;
RT   "Escherichia coli DNA glycosylase Mug: a growth-regulated enzyme required
RT   for mutation avoidance in stationary-phase cells.";
RL   Mol. Microbiol. 41:1101-1111(2001).
RN   [7]
RP   FUNCTION.
RX   PubMed=12668677; DOI=10.1074/jbc.m210860200;
RA   O'Neill R.J., Vorob'eva O.V., Shahbakhti H., Zmuda E., Bhagwat A.S.,
RA   Baldwin G.S.;
RT   "Mismatch uracil glycosylase from Escherichia coli: a general mismatch or a
RT   specific DNA glycosylase?";
RL   J. Biol. Chem. 278:20526-20532(2003).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH DNA.
RX   PubMed=9489705; DOI=10.1016/s0092-8674(00)80904-6;
RA   Barrett T.E., Savva R., Panayotou G., Brown T., Barlow T., Jiricny J.,
RA   Pearl L.H.;
RT   "Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch
RT   recognition by complementary-strand interactions.";
RL   Cell 92:117-129(1998).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH DNA.
RX   PubMed=9699633; DOI=10.1038/1394;
RA   Barrett T.E., Savva R., Barlow T., Brown T., Jiricny J., Pearl L.H.;
RT   "Structure of a DNA base-excision product resembling a cisplatin inter-
RT   strand adduct.";
RL   Nat. Struct. Biol. 5:697-701(1998).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) IN COMPLEX WITH DNA.
RX   PubMed=10581234; DOI=10.1093/emboj/18.23.6599;
RA   Barrett T.E., Schaerer O.D., Savva R., Brown T., Jiricny J., Verdine G.L.,
RA   Pearl L.H.;
RT   "Crystal structure of a thwarted mismatch glycosylase DNA repair complex.";
RL   EMBO J. 18:6599-6609(1999).
CC   -!- FUNCTION: Excises ethenocytosine and uracil, which can arise by
CC       alkylation or deamination of cytosine, respectively, from the
CC       corresponding mispairs with guanine in ds-DNA. It is capable of
CC       hydrolyzing the carbon-nitrogen bond between the sugar-phosphate
CC       backbone of the DNA and the mispaired base. The complementary strand
CC       guanine functions in substrate recognition. Required for DNA damage
CC       lesion repair in stationary-phase cells. {ECO:0000269|PubMed:12668677,
CC       ECO:0000269|PubMed:8878487}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Specifically hydrolyzes mismatched double-stranded DNA and
CC         polynucleotides, releasing free uracil.; EC=3.2.2.28;
CC   -!- ACTIVITY REGULATION: Subject to strong product inhibition. N-glycosyl
CC       hydrolysis proceeds 100-fold faster than product release.
CC   -!- SUBUNIT: Binds DNA as a monomer. {ECO:0000269|PubMed:10581234,
CC       ECO:0000269|PubMed:9489705, ECO:0000269|PubMed:9699633}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Induced in stationary phase. {ECO:0000269|PubMed:11555290}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       TDG/mug family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U28379; AAA89148.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76104.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77119.1; -; Genomic_DNA.
DR   EMBL; J01687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; B65095; B65095.
DR   RefSeq; NP_417540.1; NC_000913.3.
DR   RefSeq; WP_000228937.1; NZ_STEB01000001.1.
DR   PDB; 1MTL; X-ray; 2.80 A; A/B=1-168.
DR   PDB; 1MUG; X-ray; 1.80 A; A=1-168.
DR   PDB; 1MWI; X-ray; 2.35 A; A=1-168.
DR   PDB; 1MWJ; X-ray; 2.85 A; A=1-168.
DR   PDBsum; 1MTL; -.
DR   PDBsum; 1MUG; -.
DR   PDBsum; 1MWI; -.
DR   PDBsum; 1MWJ; -.
DR   AlphaFoldDB; P0A9H1; -.
DR   SMR; P0A9H1; -.
DR   BioGRID; 4262387; 157.
DR   IntAct; P0A9H1; 21.
DR   STRING; 511145.b3068; -.
DR   jPOST; P0A9H1; -.
DR   PaxDb; 511145-b3068; -.
DR   EnsemblBacteria; AAC76104; AAC76104; b3068.
DR   GeneID; 75205345; -.
DR   GeneID; 947560; -.
DR   KEGG; ecj:JW3040; -.
DR   KEGG; eco:b3068; -.
DR   PATRIC; fig|1411691.4.peg.3661; -.
DR   EchoBASE; EB2576; -.
DR   eggNOG; COG3663; Bacteria.
DR   HOGENOM; CLU_042829_3_1_6; -.
DR   InParanoid; P0A9H1; -.
DR   OMA; FWPVLHL; -.
DR   OrthoDB; 9799921at2; -.
DR   PhylomeDB; P0A9H1; -.
DR   BioCyc; EcoCyc:EG12717-MONOMER; -.
DR   BioCyc; MetaCyc:EG12717-MONOMER; -.
DR   BRENDA; 3.2.2.28; 2026.
DR   EvolutionaryTrace; P0A9H1; -.
DR   PRO; PR:P0A9H1; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0043739; F:G/U mismatch-specific uracil-DNA glycosylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008263; F:pyrimidine-specific mismatch base pair DNA N-glycosylase activity; IDA:EcoCyc.
DR   GO; GO:0004844; F:uracil DNA N-glycosylase activity; IBA:GO_Central.
DR   GO; GO:0006285; P:base-excision repair, AP site formation; IDA:EcoCyc.
DR   CDD; cd10028; UDG-F2_TDG_MUG; 1.
DR   Gene3D; 3.40.470.10; Uracil-DNA glycosylase-like domain; 1.
DR   HAMAP; MF_01956; MUG; 1.
DR   InterPro; IPR015637; MUG/TDG.
DR   InterPro; IPR023502; MUG_bact.
DR   InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR   InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR   PANTHER; PTHR12159; G/T AND G/U MISMATCH-SPECIFIC DNA GLYCOSYLASE; 1.
DR   PANTHER; PTHR12159:SF9; G_T MISMATCH-SPECIFIC THYMINE DNA GLYCOSYLASE; 1.
DR   Pfam; PF03167; UDG; 1.
DR   SUPFAM; SSF52141; Uracil-DNA glycosylase-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; DNA damage; DNA excision; DNA repair; DNA-binding;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..168
FT                   /note="G/U mismatch-specific DNA glycosylase"
FT                   /id="PRO_0000185774"
FT   STRAND          11..18
FT                   /evidence="ECO:0007829|PDB:1MUG"
FT   HELIX           21..26
FT                   /evidence="ECO:0007829|PDB:1MUG"
FT   HELIX           37..43
FT                   /evidence="ECO:0007829|PDB:1MUG"
FT   STRAND          46..49
FT                   /evidence="ECO:0007829|PDB:1MUG"
FT   HELIX           53..62
FT                   /evidence="ECO:0007829|PDB:1MUG"
FT   STRAND          64..69
FT                   /evidence="ECO:0007829|PDB:1MUG"
FT   STRAND          74..76
FT                   /evidence="ECO:0007829|PDB:1MWJ"
FT   HELIX           77..79
FT                   /evidence="ECO:0007829|PDB:1MUG"
FT   HELIX           82..99
FT                   /evidence="ECO:0007829|PDB:1MUG"
FT   STRAND          102..107
FT                   /evidence="ECO:0007829|PDB:1MUG"
FT   HELIX           109..116
FT                   /evidence="ECO:0007829|PDB:1MUG"
FT   STRAND          123..130
FT                   /evidence="ECO:0007829|PDB:1MUG"
FT   STRAND          133..138
FT                   /evidence="ECO:0007829|PDB:1MUG"
FT   HELIX           149..162
FT                   /evidence="ECO:0007829|PDB:1MUG"
SQ   SEQUENCE   168 AA;  18673 MW;  F1CD9B2E2030D6A7 CRC64;
     MVEDILAPGL RVVFCGINPG LSSAGTGFPF AHPANRFWKV IYQAGFTDRQ LKPQEAQHLL
     DYRCGVTKLV DRPTVQANEV SKQELHAGGR KLIEKIEDYQ PQALAILGKQ AYEQGFSQRG
     AQWGKQTLTI GSTQIWVLPN PSGLSRVSLE KLVEAYRELD QALVVRGR
//