ID   FPG2_MYCTU              Reviewed;         158 AA.
AC   L0T864;
DT   03-APR-2013, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2013, sequence version 1.
DT   25-MAY-2022, entry version 42.
DE   RecName: Full=Uncharacterized formamidopyrimidine-DNA glycosylase-like protein;
GN   Name=fpg2; OrderedLocusNames=Rv0944;
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   DISCUSSION OF FUNCTION.
RC   STRAIN=KHA94;
RX   PubMed=18457574; DOI=10.1134/s0006297908040093;
RA   Sidorenko V.S., Rot M.A., Filipenko M.L., Nevinsky G.A., Zharkov D.O.;
RT   "Novel DNA glycosylases from Mycobacterium tuberculosis.";
RL   Biochemistry (Mosc.) 73:442-450(2008).
RN   [3]
RP   DISCUSSION OF FUNCTION, AND LACK OF DNA-BINDING.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=20031487; DOI=10.1016/j.dnarep.2009.11.008;
RA   Guo Y., Bandaru V., Jaruga P., Zhao X., Burrows C.J., Iwai S.,
RA   Dizdaroglu M., Bond J.P., Wallace S.S.;
RT   "The oxidative DNA glycosylases of Mycobacterium tuberculosis exhibit
RT   different substrate preferences from their Escherichia coli counterparts.";
RL   DNA Repair 9:177-190(2010).
RN   [4]
RP   REVIEW.
RX   PubMed=21764637; DOI=10.1016/j.tube.2011.06.005;
RA   Kurthkoti K., Varshney U.;
RT   "Base excision and nucleotide excision repair pathways in mycobacteria.";
RL   Tuberculosis 91:533-543(2011).
CC   -!- CAUTION: May be non-functional, contains only the C-terminal section of
CC       a formamidopyrimidine-DNA glycosylase and has no detectable DNA-binding
CC       activity. {ECO:0000305}.
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DR   EMBL; AL123456; CCP43692.1; -; Genomic_DNA.
DR   PIR; F70715; F70715.
DR   RefSeq; NP_215459.1; NC_000962.3.
DR   RefSeq; WP_003404828.1; NZ_NVQJ01000001.1.
DR   AlphaFoldDB; L0T864; -.
DR   SMR; L0T864; -.
DR   STRING; 83332.Rv0944; -.
DR   PaxDb; L0T864; -.
DR   GeneID; 885888; -.
DR   KEGG; mtu:Rv0944; -.
DR   TubercuList; Rv0944; -.
DR   eggNOG; COG0266; Bacteria.
DR   InParanoid; L0T864; -.
DR   OMA; NAMSADY; -.
DR   PhylomeDB; L0T864; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; HDA:UniProtKB.
DR   GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IDA:UniProtKB.
DR   GO; GO:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0034599; P:cellular response to oxidative stress; IMP:UniProtKB.
DR   GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR   GO; GO:0006289; P:nucleotide-excision repair; IMP:UniProtKB.
DR   InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR   InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR   InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR   InterPro; IPR010663; Znf_FPG/IleRS.
DR   Pfam; PF06831; H2TH; 1.
DR   Pfam; PF06827; zf-FPG_IleRS; 1.
DR   SMART; SM01232; H2TH; 1.
DR   SUPFAM; SSF46946; SSF46946; 1.
DR   PROSITE; PS51066; ZF_FPG_2; 1.
PE   1: Evidence at protein level;
KW   Metal-binding; Reference proteome; Zinc; Zinc-finger.
FT   CHAIN           1..158
FT                   /note="Uncharacterized formamidopyrimidine-DNA glycosylase-
FT                   like protein"
FT                   /id="PRO_0000421384"
FT   ZN_FING         109..143
FT                   /note="FPG-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00391"
SQ   SEQUENCE   158 AA;  16495 MW;  6BA9BF572AF38E52 CRC64;
     MAGTPQPRAL GPDALDVSTD DLAGLLAGNT GRIKTVITDQ KVIAGIGNAY SDEILHVAKI
     SPFATAGKLS GAQLTCLHEA MASVLSDAVR RSVGQGAAML KGEKRSGLRV HARTGLPCPV
     CGDTVREVSF ADKSFQYCPT CQTGGKALAD RRMSRLLK