MUG_ECOLI
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 03-AUG-2022, entry version 123.
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; Proteobacteria; 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}.
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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; P0A9H1; -.
DR PRIDE; P0A9H1; -.
DR EnsemblBacteria; AAC76104; AAC76104; b3068.
DR EnsemblBacteria; BAE77119; BAE77119; BAE77119.
DR GeneID; 66673033; -.
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 PhylomeDB; P0A9H1; -.
DR BioCyc; EcoCyc:EG12717-MON; -.
DR BioCyc; MetaCyc:EG12717-MON; -.
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:0008263; F:pyrimidine-specific mismatch base pair DNA N-glycosylase activity; IDA:EcoCyc.
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; -; 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; PTHR12159; 1.
DR Pfam; PF03167; UDG; 1.
DR SUPFAM; SSF52141; SSF52141; 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
