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MUG_ECO57
ID   MUG_ECO57               Reviewed;         168 AA.
AC   Q8XAN4; Q7AAP7;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=G/U mismatch-specific DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_01956};
DE            EC=3.2.2.28 {ECO:0000255|HAMAP-Rule:MF_01956};
DE   AltName: Full=Double-strand-specific uracil glycosylase {ECO:0000255|HAMAP-Rule:MF_01956};
DE   AltName: Full=Mismatch-specific uracil DNA-glycosylase {ECO:0000255|HAMAP-Rule:MF_01956};
DE            Short=MUG {ECO:0000255|HAMAP-Rule:MF_01956};
GN   Name=mug {ECO:0000255|HAMAP-Rule:MF_01956};
GN   OrderedLocusNames=Z4421, ECs3951;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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:0000255|HAMAP-
CC       Rule:MF_01956}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Specifically hydrolyzes mismatched double-stranded DNA and
CC         polynucleotides, releasing free uracil.; EC=3.2.2.28;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01956};
CC   -!- SUBUNIT: Binds DNA as a monomer. {ECO:0000255|HAMAP-Rule:MF_01956}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01956}.
CC   -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC       TDG/mug family. {ECO:0000255|HAMAP-Rule:MF_01956}.
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DR   EMBL; BA000007; BAB37374.1; -; Genomic_DNA.
DR   EMBL; AE005174; AAG58202.1; -; Genomic_DNA.
DR   PIR; F85967; F85967.
DR   PIR; G91122; G91122.
DR   RefSeq; NP_311978.1; NC_002695.1.
DR   RefSeq; WP_000228926.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8XAN4; -.
DR   SMR; Q8XAN4; -.
DR   STRING; 155864.EDL933_4290; -.
DR   EnsemblBacteria; AAG58202; AAG58202; Z4421.
DR   EnsemblBacteria; BAB37374; BAB37374; ECs_3951.
DR   GeneID; 916221; -.
DR   KEGG; ece:Z4421; -.
DR   KEGG; ecs:ECs_3951; -.
DR   PATRIC; fig|386585.9.peg.4122; -.
DR   eggNOG; COG3663; Bacteria.
DR   HOGENOM; CLU_042829_3_1_6; -.
DR   OMA; FWPVLHL; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; IEA:UniProtKB-UniRule.
DR   GO; GO:0006285; P:base-excision repair, AP site formation; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Cytoplasm; DNA damage; DNA excision; DNA repair; DNA-binding; Hydrolase;
KW   Reference proteome.
FT   CHAIN           1..168
FT                   /note="G/U mismatch-specific DNA glycosylase"
FT                   /id="PRO_0000238680"
SQ   SEQUENCE   168 AA;  18654 MW;  29E3EEDFCF3439A8 CRC64;
     MVEDILAPGL RVVFCGINPG LSSAGTGFPF AHPANRFWKV IYQAGFTDHQ LKPQEAQHLL
     DYRCGVTKLV DRPTVQANEI SKQELHAGGR KLIEKIEDYQ PQALAILGKQ AYEQGFSQRG
     AQWGKQTLSI GSTQIWVLPN PSGLSRVSLE KLVEAYRELD QALVVRGR
 
 
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