MUG_ECOL6
ID MUG_ECOL6 Reviewed; 168 AA.
AC P0A9H2; P43342;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
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}; OrderedLocusNames=c3822;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN82267.1; -; Genomic_DNA.
DR RefSeq; WP_000228937.1; NC_004431.1.
DR AlphaFoldDB; P0A9H2; -.
DR SMR; P0A9H2; -.
DR STRING; 199310.c3822; -.
DR EnsemblBacteria; AAN82267; AAN82267; c3822.
DR GeneID; 66673033; -.
DR KEGG; ecc:c3822; -.
DR eggNOG; COG3663; Bacteria.
DR HOGENOM; CLU_042829_3_1_6; -.
DR OMA; FWPVLHL; -.
DR BioCyc; ECOL199310:C3822-MON; -.
DR Proteomes; UP000001410; 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.
FT CHAIN 1..168
FT /note="G/U mismatch-specific DNA glycosylase"
FT /id="PRO_0000185775"
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