UNG_STRR6
ID UNG_STRR6 Reviewed; 217 AA.
AC Q8DPQ4;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 2.
DT 25-MAY-2022, entry version 101.
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=spr1055;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(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. {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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK99859.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE007317; AAK99859.1; ALT_INIT; Genomic_DNA.
DR PIR; G98003; G98003.
DR RefSeq; NP_358649.1; NC_003098.1.
DR RefSeq; WP_000401328.1; NC_003098.1.
DR AlphaFoldDB; Q8DPQ4; -.
DR SMR; Q8DPQ4; -.
DR STRING; 171101.spr1055; -.
DR EnsemblBacteria; AAK99859; AAK99859; spr1055.
DR GeneID; 60233164; -.
DR KEGG; spr:spr1055; -.
DR PATRIC; fig|171101.6.peg.1147; -.
DR eggNOG; COG0692; Bacteria.
DR HOGENOM; CLU_032162_3_1_9; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IBA:GO_Central.
DR GO; GO:0097510; P:base-excision repair, AP site formation via deaminated base removal; IBA:GO_Central.
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..217
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176153"
FT ACT_SITE 62
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00148"
SQ SEQUENCE 217 AA; 24080 MW; FBACF83550CF64E1 CRC64;
MEHSSWHALI KAQLPEGYFG KINQFMEQVY SQGIIYPPKE KVFQALLTTL LEEVKVVILG
QDPYHGPGQA QGLSFSVPDS IPAPPSLQNI LKELSDDIGV KKSHDLTAWA EQGVLLLNAC
LTVPAGQANG HAGQIWEPFT DAVIQVVNHL DRPVVFVLWG AYARKKKALV TNPHHLIIES
AHPSPLSVYR GFWGSKPFSK ANTFLKETGQ EPIDWLR