MUG_KLEP7
ID MUG_KLEP7 Reviewed; 168 AA.
AC A6TE50;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=KPN78578_34100; ORFNames=KPN_03475;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR78871.1; -; Genomic_DNA.
DR RefSeq; WP_002917636.1; NC_009648.1.
DR AlphaFoldDB; A6TE50; -.
DR SMR; A6TE50; -.
DR STRING; 272620.KPN_03475; -.
DR EnsemblBacteria; ABR78871; ABR78871; KPN_03475.
DR GeneID; 61334832; -.
DR GeneID; 64293485; -.
DR KEGG; kpn:KPN_03475; -.
DR HOGENOM; CLU_042829_3_1_6; -.
DR OMA; FWPVLHL; -.
DR Proteomes; UP000000265; 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 SMART; SM00986; 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_1000070794"
SQ SEQUENCE 168 AA; 18635 MW; DDA6063E08093167 CRC64;
MISDILAPGL RVVFCGINPG KSSAHTGFHF AHPGNRFWKV IHQAGFTDRQ LRPEEELQLL
DTRCGITMLV ERPTVQASEV ALQELRSGGR ELVRKIEEYQ PQALAVLGKQ AFELAFNQRG
AKWGKQAMTI GTTQVWVLPN PSGLNRATLD KLVAAYRELD DALATRGQ
