UNG_STRPN
ID UNG_STRPN Reviewed; 217 AA.
AC P23379;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Uracil-DNA glycosylase;
DE Short=UDG;
DE EC=3.2.2.27;
GN Name=ung; OrderedLocusNames=SP_1169;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=R6 / R800;
RX PubMed=2251133; DOI=10.1093/nar/18.22.6693;
RA Mejean V., Rives I., Claverys J.-P.;
RT "Nucleotide sequence of the Streptococcus pneumoniae ung gene encoding
RT uracil-DNA glycosylase.";
RL Nucleic Acids Res. 18:6693-6693(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC UNG family. {ECO:0000305}.
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DR EMBL; X55651; CAA39182.1; -; Genomic_DNA.
DR EMBL; Z21702; CAA79806.1; -; Genomic_DNA.
DR EMBL; AE005672; AAK75278.1; -; Genomic_DNA.
DR PIR; E95135; E95135.
DR PIR; S13591; S13591.
DR RefSeq; WP_000401326.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; P23379; -.
DR SMR; P23379; -.
DR STRING; 170187.SP_1169; -.
DR EnsemblBacteria; AAK75278; AAK75278; SP_1169.
DR GeneID; 66806293; -.
DR KEGG; spn:SP_1169; -.
DR eggNOG; COG0692; Bacteria.
DR OMA; PDNGYLM; -.
DR PhylomeDB; P23379; -.
DR BioCyc; SPNE170187:G1FZB-1189-MON; -.
DR Proteomes; UP000000585; 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.
FT CHAIN 1..217
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176152"
FT ACT_SITE 62
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT CONFLICT 203
FT /note="A -> T (in Ref. 1; CAA39182/CAA79806)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 217 AA; 24050 MW; FBACF83550CF74E0 CRC64;
MEHSSWHALI KAQLPEGYFG KINQFMEQVY SQGIIYPPKE KVFQALLTTL LEEVKVVILG
QDPYHGPGQA QGLSFSVPDS IPAPPSLQNI LKELSDDIGV KKSHDLTAWA EQGVLLLNAC
LTVPAGQANG HAGQIWEPFT DAVIQVVNHL DRPVVFVLWG AYARKKKALV TNPHHLIIES
AHPSPLSVYR GFWGSKPFSK ANAFLKETGQ EPIDWLR