UNG_LACAC
ID UNG_LACAC Reviewed; 232 AA.
AC Q5FL46;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_00148};
DE Short=UDG {ECO:0000255|HAMAP-Rule:MF_00148};
DE EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_00148};
GN Name=ung {ECO:0000255|HAMAP-Rule:MF_00148}; OrderedLocusNames=LBA0703;
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
CC -!- FUNCTION: Excises uracil residues from the DNA which can arise as a
CC result of misincorporation of dUMP residues by DNA polymerase or due to
CC deamination of cytosine. {ECO:0000255|HAMAP-Rule:MF_00148}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes single-stranded DNA or mismatched double-stranded
CC DNA and polynucleotides, releasing free uracil.; EC=3.2.2.27;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00148};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00148}.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC UNG family. {ECO:0000255|HAMAP-Rule:MF_00148}.
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DR EMBL; CP000033; AAV42578.1; -; Genomic_DNA.
DR RefSeq; WP_003546612.1; NC_006814.3.
DR RefSeq; YP_193609.1; NC_006814.3.
DR AlphaFoldDB; Q5FL46; -.
DR SMR; Q5FL46; -.
DR STRING; 272621.LBA0703; -.
DR EnsemblBacteria; AAV42578; AAV42578; LBA0703.
DR GeneID; 56942335; -.
DR KEGG; lac:LBA0703; -.
DR PATRIC; fig|272621.13.peg.673; -.
DR eggNOG; COG0692; Bacteria.
DR HOGENOM; CLU_032162_3_0_9; -.
DR OMA; PDNGYLM; -.
DR BioCyc; LACI272621:G1G49-725-MON; -.
DR Proteomes; UP000006381; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-UniRule.
DR CDD; cd10027; UDG-F1-like; 1.
DR Gene3D; 3.40.470.10; -; 1.
DR HAMAP; MF_00148; UDG; 1.
DR InterPro; IPR002043; UDG_fam1.
DR InterPro; IPR018085; Ura-DNA_Glyclase_AS.
DR InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR PANTHER; PTHR11264; PTHR11264; 1.
DR Pfam; PF03167; UDG; 1.
DR SMART; SM00986; UDG; 1.
DR SUPFAM; SSF52141; SSF52141; 1.
DR TIGRFAMs; TIGR00628; ung; 1.
DR PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Cytoplasm; DNA damage; DNA repair; Hydrolase; Reference proteome.
FT CHAIN 1..232
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176105"
FT ACT_SITE 66
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00148"
SQ SEQUENCE 232 AA; 26237 MW; 7F735695D7BE6E6C CRC64;
MAKELIGNDW DQILNPIFTS DKYHELHNFL KKEYSTRQIY PDMYHIFTAF KLTPFNKTKV
VILGQDPYHN PGQANGMSFS VMPGAQLPPS LRNIYKELYD DVGAIPVNHG YLKKWADQGV
LLLNAVLTVP YGHANGHQGK GWEDVTDAAI KALSKRGKVV FILWGRFAQN KIPLIDQSKN
FIIKSSHPSP FSADRGFFGS RPFSRCNTAL INFGETPIDW QLPEKVSKSD LI