MUG_ESCF3
ID MUG_ESCF3 Reviewed; 168 AA.
AC B7LQE3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=EFER_3010;
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928158; CAQ90503.1; -; Genomic_DNA.
DR RefSeq; WP_000228925.1; NC_011740.1.
DR AlphaFoldDB; B7LQE3; -.
DR SMR; B7LQE3; -.
DR EnsemblBacteria; CAQ90503; CAQ90503; EFER_3010.
DR KEGG; efe:EFER_3010; -.
DR HOGENOM; CLU_042829_3_1_6; -.
DR OMA; FWPVLHL; -.
DR OrthoDB; 2034230at2; -.
DR BioCyc; EFER585054:EFER_RS15160-MON; -.
DR Proteomes; UP000000745; 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_1000188960"
SQ SEQUENCE 168 AA; 18765 MW; 22A4F232BE1B3987 CRC64;
MVEDILAPGL RVVFCGINPG LSSAEKGFPF AHPANRFWKV IHQAGFTDRQ LKPQEAQLLL
DYRCGVTKLV DRPTVQANEV TKLELHAGGR KLIEKIEDYQ PQALAILGKQ AYEQGFSQRG
TQWGKQTHTI GATQIWVLPN PSGLSRVSLE KLVEAYRELD QSLVMRGL
