MUG_ECOHS
ID MUG_ECOHS Reviewed; 168 AA.
AC A8A4M5;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 74.
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=EcHS_A3249;
OS Escherichia coli O9:H4 (strain HS).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331112;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS;
RX PubMed=18676672; DOI=10.1128/jb.00619-08;
RA Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA Henderson I.R., Sperandio V., Ravel J.;
RT "The pangenome structure of Escherichia coli: comparative genomic analysis
RT of E. coli commensal and pathogenic isolates.";
RL J. Bacteriol. 190:6881-6893(2008).
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; CP000802; ABV07479.1; -; Genomic_DNA.
DR RefSeq; WP_000228941.1; NC_009800.1.
DR AlphaFoldDB; A8A4M5; -.
DR SMR; A8A4M5; -.
DR KEGG; ecx:EcHS_A3249; -.
DR HOGENOM; CLU_042829_3_1_6; -.
DR OMA; FWPVLHL; -.
DR Proteomes; UP000001123; 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_1000070788"
SQ SEQUENCE 168 AA; 18646 MW; 4F3D87E33CE11BBB CRC64;
MVEDILAPGL RVVFCGINPG LSSAGTGFPF AHPANRFWKV IYQAGFTDRQ LKPQEAQHLL
DYRCGVTKLV DRPTVQASEV SKQELHAGGR KLIEKIEDYQ PQALAILGKQ AYEQGFSQRG
AQWGKQTLTI GSTQIWVLPN PSGLSRVSLE KLVEAYRELD QALVVRGR
