ID   UNG_COXBU               Reviewed;         229 AA.
AC   Q83CW4;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=CBU_0988;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; AE016828; AAO90509.1; -; Genomic_DNA.
DR   RefSeq; NP_819995.1; NC_002971.3.
DR   RefSeq; WP_010957938.1; NC_002971.4.
DR   PDB; 3TR7; X-ray; 2.20 A; A=1-229.
DR   PDBsum; 3TR7; -.
DR   AlphaFoldDB; Q83CW4; -.
DR   SMR; Q83CW4; -.
DR   STRING; 227377.CBU_0988; -.
DR   DNASU; 1208883; -.
DR   EnsemblBacteria; AAO90509; AAO90509; CBU_0988.
DR   GeneID; 1208883; -.
DR   KEGG; cbu:CBU_0988; -.
DR   PATRIC; fig|227377.7.peg.984; -.
DR   eggNOG; COG0692; Bacteria.
DR   HOGENOM; CLU_032162_3_0_6; -.
DR   OMA; PDNGYLM; -.
DR   Proteomes; UP000002671; 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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; DNA damage; DNA repair; Hydrolase;
KW   Reference proteome.
FT   CHAIN           1..229
FT                   /note="Uracil-DNA glycosylase"
FT                   /id="PRO_0000176089"
FT   ACT_SITE        67
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00148"
FT   HELIX           10..13
FT                   /evidence="ECO:0007829|PDB:3TR7"
FT   HELIX           15..19
FT                   /evidence="ECO:0007829|PDB:3TR7"
FT   HELIX           21..35
FT                   /evidence="ECO:0007829|PDB:3TR7"
FT   STRAND          40..42
FT                   /evidence="ECO:0007829|PDB:3TR7"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:3TR7"
FT   HELIX           49..53
FT                   /evidence="ECO:0007829|PDB:3TR7"
FT   HELIX           56..58
FT                   /evidence="ECO:0007829|PDB:3TR7"
FT   STRAND          61..67
FT                   /evidence="ECO:0007829|PDB:3TR7"
FT   TURN            72..74
FT                   /evidence="ECO:0007829|PDB:3TR7"
FT   STRAND          76..80
FT                   /evidence="ECO:0007829|PDB:3TR7"
FT   HELIX           90..103
FT                   /evidence="ECO:0007829|PDB:3TR7"
FT   HELIX           114..118
FT                   /evidence="ECO:0007829|PDB:3TR7"
FT   STRAND          121..128
FT                   /evidence="ECO:0007829|PDB:3TR7"
FT   TURN            135..140
FT                   /evidence="ECO:0007829|PDB:3TR7"
FT   HELIX           143..153
FT                   /evidence="ECO:0007829|PDB:3TR7"
FT   HELIX           154..156
FT                   /evidence="ECO:0007829|PDB:3TR7"
FT   STRAND          162..167
FT                   /evidence="ECO:0007829|PDB:3TR7"
FT   HELIX           168..172
FT                   /evidence="ECO:0007829|PDB:3TR7"
FT   HELIX           173..176
FT                   /evidence="ECO:0007829|PDB:3TR7"
FT   STRAND          182..187
FT                   /evidence="ECO:0007829|PDB:3TR7"
FT   HELIX           204..214
FT                   /evidence="ECO:0007829|PDB:3TR7"
SQ   SEQUENCE   229 AA;  25667 MW;  A1B27E419D025552 CRC64;
     MTTMAETQTW QTVLGEEKQE PYFQEILDFV KKERKAGKII YPPQKDIFNA LKLTPYEAIK
     VVILGQDPYH GPNQAHGLAF SVRPGVPAPP SLQNIFKELH ADLGVSIPSH GFLEKWAKQG
     VLLLNAALTV EAGKPQSHAN IGWHRFTDKV IESLNDHPEG IVFLLWGSYA QKKSQLITNL
     RHRILKAPHP SPLSAARGFL GCRHFSKANQ LLHEMGRGEI DWALDEKVS