UDGB_MYCTU
ID UDGB_MYCTU Reviewed; 268 AA.
AC P9WM53; L0T7R5; P64785; Q11059;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Type-5 uracil-DNA glycosylase {ECO:0000305};
DE EC=3.2.2.- {ECO:0000269|PubMed:17588829};
GN Name=udgB {ECO:0000303|PubMed:17588829}; OrderedLocusNames=Rv1259;
GN ORFNames=MTCY50.23c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP IRON-SULFUR CLUSTER.
RX PubMed=17588829; DOI=10.1016/j.dnarep.2007.05.001;
RA Srinath T., Bharti S.K., Varshney U.;
RT "Substrate specificities and functional characterization of a thermo-
RT tolerant uracil DNA glycosylase (UdgB) from Mycobacterium tuberculosis.";
RL DNA Repair 6:1517-1528(2007).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: DNA glycosylase with broad substrate specificity. Can remove
CC uracil from double-stranded DNA containing either a U/G, U/A, U/C or
CC U/T base pair. Can also excise ethenocytosine and hypoxanthine from
CC double-stranded DNA. {ECO:0000269|PubMed:17588829}.
CC -!- ACTIVITY REGULATION: Product inhibited by AP-site containing dsDNA but
CC not by uracil. {ECO:0000269|PubMed:17588829}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Thermo-tolerant. {ECO:0000269|PubMed:17588829};
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC Type 5 (UDGb) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP44015.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL123456; CCP44015.1; ALT_INIT; Genomic_DNA.
DR PIR; C70753; C70753.
DR RefSeq; NP_215775.1; NC_000962.3.
DR AlphaFoldDB; P9WM53; -.
DR SMR; P9WM53; -.
DR STRING; 83332.Rv1259; -.
DR PaxDb; P9WM53; -.
DR GeneID; 887047; -.
DR KEGG; mtu:Rv1259; -.
DR PATRIC; fig|83332.12.peg.1410; -.
DR TubercuList; Rv1259; -.
DR eggNOG; COG1573; Bacteria.
DR OMA; CVPPQNK; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0033958; F:DNA-deoxyinosine glycosylase activity; IDA:MTBBASE.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IDA:MTBBASE.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IDA:MTBBASE.
DR GO; GO:0006284; P:base-excision repair; IDA:MTBBASE.
DR CDD; cd10031; UDG-F5_TTUDGB_like; 1.
DR Gene3D; 3.40.470.10; -; 1.
DR InterPro; IPR044147; UdgB-like.
DR InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR Pfam; PF03167; UDG; 1.
DR SMART; SM00986; UDG; 1.
DR SUPFAM; SSF52141; SSF52141; 1.
PE 1: Evidence at protein level;
KW 4Fe-4S; DNA damage; DNA repair; Hydrolase; Iron; Iron-sulfur;
KW Metal-binding; Reference proteome.
FT CHAIN 1..268
FT /note="Type-5 uracil-DNA glycosylase"
FT /id="PRO_0000103774"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 57
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q5SJ65"
FT BINDING 60
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q5SJ65"
FT BINDING 161
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q5SJ65"
FT BINDING 176
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q5SJ65"
SQ SEQUENCE 268 AA; 28500 MW; 6F2C31C9C561E7FD CRC64;
MHPKTGRAFR SPVEPGSGWP GDPATPQTPV AADAAQVSAL AGGAGSICEL NALISVCRAC
PRLVSWREEV AVVKRRAFAD QPYWGRPVPG WGSKRPRLLI LGLAPAAHGA NRTGRMFTGD
RSGDQLYAAL HRAGLVNSPV SVDAADGLRA NRIRITAPVR CAPPGNSPTP AERLTCSPWL
NAEWRLVSDH IRAIVALGGF AWQVALRLAG ASGTPKPRFG HGVVTELGAG VRLLGCYHPS
QQNMFTGRLT PTMLDDIFRE AKKLAGIE
