UNG_STRA1
ID UNG_STRA1 Reviewed; 217 AA.
AC P0A4P5; Q3K0U4; Q9XDS8;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Uracil-DNA glycosylase;
DE Short=UDG;
DE EC=3.2.2.27;
GN Name=ung; OrderedLocusNames=SAK_1245;
OS Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC
OS SS700).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=205921;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=OI1 / Serotype Ia;
RX PubMed=10464185; DOI=10.1128/jb.181.17.5176-5184.1999;
RA Yamamoto S., Miyake K., Koike Y., Watanabe M., Machida Y., Ohta M.,
RA Iijima S.;
RT "Molecular characterization of type-specific capsular polysaccharide
RT biosynthesis genes of Streptococcus agalactiae type Ia.";
RL J. Bacteriol. 181:5176-5184(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27591 / A909 / CDC SS700;
RX PubMed=16172379; DOI=10.1073/pnas.0506758102;
RA Tettelin H., Masignani V., Cieslewicz M.J., Donati C., Medini D.,
RA Ward N.L., Angiuoli S.V., Crabtree J., Jones A.L., Durkin A.S., DeBoy R.T.,
RA Davidsen T.M., Mora M., Scarselli M., Margarit y Ros I., Peterson J.D.,
RA Hauser C.R., Sundaram J.P., Nelson W.C., Madupu R., Brinkac L.M.,
RA Dodson R.J., Rosovitz M.J., Sullivan S.A., Daugherty S.C., Haft D.H.,
RA Selengut J., Gwinn M.L., Zhou L., Zafar N., Khouri H., Radune D.,
RA Dimitrov G., Watkins K., O'Connor K.J., Smith S., Utterback T.R., White O.,
RA Rubens C.E., Grandi G., Madoff L.C., Kasper D.L., Telford J.L.,
RA Wessels M.R., Rappuoli R., Fraser C.M.;
RT "Genome analysis of multiple pathogenic isolates of Streptococcus
RT agalactiae: implications for the microbial 'pan-genome'.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13950-13955(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:0000250}.
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; AB028896; BAA82292.1; -; Genomic_DNA.
DR EMBL; CP000114; ABA45529.1; -; Genomic_DNA.
DR RefSeq; WP_000682955.1; NC_007432.1.
DR AlphaFoldDB; P0A4P5; -.
DR SMR; P0A4P5; -.
DR GeneID; 66886082; -.
DR KEGG; sak:SAK_1245; -.
DR HOGENOM; CLU_032162_3_1_9; -.
DR OMA; PDNGYLM; -.
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_0000176144"
FT ACT_SITE 62
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 217 AA; 24570 MW; EC6C29EF8732895B CRC64;
MKHSSWHDLI KRELPNHYYN KINTFMDAVY ESGIVYPPRD KVFNAIQITP LENVKVVIIG
QDPYHGPQQA QGLSFSVPDN LPAPPSLQNI LKELAEDIGS RSHHDLTSWA QQGVLLLNAC
LTVPEHQANG HAGLIWEPFT DAVIKVVNQK ETPVVFILWG GYARKKKSLI DNPIHHIIES
PHPSPLSAYR GFFGSRPFSR TNHFLEEEGI NEIDWLN