UNG_BACSU
ID UNG_BACSU Reviewed; 225 AA.
AC P39615;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Uracil-DNA glycosylase;
DE Short=UDG;
DE EC=3.2.2.27;
GN Name=ung; Synonyms=ywdG; OrderedLocusNames=BSU37970; ORFNames=ipa-57d;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7934828; DOI=10.1111/j.1365-2958.1993.tb01963.x;
RA Glaser P., Kunst F., Arnaud M., Coudart M.P., Gonzales W., Hullo M.-F.,
RA Ionescu M., Lubochinsky B., Marcelino L., Moszer I., Presecan E.,
RA Santana M., Schneider E., Schweizer J., Vertes A., Rapoport G., Danchin A.;
RT "Bacillus subtilis genome project: cloning and sequencing of the 97 kb
RT region from 325 degrees to 333 degrees.";
RL Mol. Microbiol. 10:371-384(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP INTERACTION WITH BACILLUS PHAGE PHI29 P56.
RX PubMed=17698500; DOI=10.1093/nar/gkm584;
RA Serrano-Heras G., Ruiz-Maso J.A., del Solar G., Espinosa M., Bravo A.,
RA Salas M.;
RT "Protein p56 from the Bacillus subtilis phage phi29 inhibits DNA-binding
RT ability of uracil-DNA glycosylase.";
RL Nucleic Acids Res. 35:5393-5401(2007).
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 -!- SUBUNIT: Interacts with bacillus phage phi29 protein p56; this
CC interaction inhibits the uracil-DNA glycosylase.
CC {ECO:0000269|PubMed:17698500}.
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; X73124; CAA51613.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15823.1; -; Genomic_DNA.
DR PIR; S39712; S39712.
DR RefSeq; NP_391676.1; NC_000964.3.
DR RefSeq; WP_003242965.1; NZ_JNCM01000034.1.
DR PDB; 3ZOQ; X-ray; 1.45 A; A=1-225.
DR PDB; 3ZOR; X-ray; 2.95 A; A=1-225.
DR PDBsum; 3ZOQ; -.
DR PDBsum; 3ZOR; -.
DR AlphaFoldDB; P39615; -.
DR SMR; P39615; -.
DR STRING; 224308.BSU37970; -.
DR PaxDb; P39615; -.
DR PRIDE; P39615; -.
DR EnsemblBacteria; CAB15823; CAB15823; BSU_37970.
DR GeneID; 937265; -.
DR KEGG; bsu:BSU37970; -.
DR PATRIC; fig|224308.179.peg.4111; -.
DR eggNOG; COG0692; Bacteria.
DR InParanoid; P39615; -.
DR OMA; PDNGYLM; -.
DR PhylomeDB; P39615; -.
DR BioCyc; BSUB:BSU37970-MON; -.
DR SABIO-RK; P39615; -.
DR Proteomes; UP000001570; 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..225
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176067"
FT ACT_SITE 65
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT HELIX 7..17
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT HELIX 20..35
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT HELIX 47..51
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT HELIX 112..116
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT TURN 133..138
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT HELIX 166..169
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT HELIX 170..174
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT HELIX 193..195
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:3ZOQ"
FT HELIX 202..212
FT /evidence="ECO:0007829|PDB:3ZOQ"
SQ SEQUENCE 225 AA; 26047 MW; 649052A9C2904F9C CRC64;
MKQLLQDSWW NQLKEEFEKP YYQELREMLK REYAEQTIYP DSRDIFNALH YTSYDDVKVV
ILGQDPYHGP GQAQGLSFSV KPGVKQPPSL KNIFLELQQD IGCSIPNHGS LVSWAKQGVL
LLNTVLTVRR GQANSHKGKG WERLTDRIID VLSERERPVI FILWGRHAQM KKERIDTSKH
FIIESTHPSP FSARNGFFGS RPFSRANAYL EKMGEAPIDW CIKDL
