FPG_BACSU
ID FPG_BACSU Reviewed; 276 AA.
AC O34403;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Formamidopyrimidine-DNA glycosylase;
DE Short=Fapy-DNA glycosylase;
DE EC=3.2.2.23;
DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase MutM;
DE Short=AP lyase MutM;
DE EC=4.2.99.18;
GN Name=mutM; Synonyms=fpg, ytaE; OrderedLocusNames=BSU29080;
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=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
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 SEQUENCE REVISION TO N-TERMINUS.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=12483591; DOI=10.2323/jgam.46.183;
RA Sasaki M., Yonemura Y., Kurusu Y.;
RT "Genetic analysis of Bacillus subtilis mutator genes.";
RL J. Gen. Appl. Microbiol. 46:183-187(2000).
RN [5]
RP DISRUPTION PHENOTYPE IN STATIONARY PHASE CELLS.
RC STRAIN=168 / YB955;
RX PubMed=19011023; DOI=10.1128/jb.01210-08;
RA Vidales L.E., Cardenas L.C., Robleto E., Yasbin R.E., Pedraza-Reyes M.;
RT "Defects in the error prevention oxidized guanine system potentiate
RT stationary-phase mutagenesis in Bacillus subtilis.";
RL J. Bacteriol. 191:506-513(2009).
CC -!- FUNCTION: Involved in the GO system responsible for removing an
CC oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine, 8-oxo-
CC dGTP) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite
CC dA and dC residues of template DNA with almost equal efficiency thus
CC leading to A.T to G.C transversions (By similarity). Involved in base
CC excision repair of DNA damaged by oxidation or by mutagenic agents.
CC Acts as DNA glycosylase that recognizes and removes damaged bases. Has
CC a preference for oxidized purines, such as 8-oxo-dGTP. Has AP
CC (apurinic/apyrimidinic) lyase activity and introduces nicks in the DNA
CC strand. Cleaves the DNA backbone by beta-delta elimination to generate
CC a single-strand break at the site of the removed base. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of DNA containing ring-opened 7-methylguanine
CC residues, releasing 2,6-diamino-4-hydroxy-5-(N-
CC methyl)formamidopyrimidine.; EC=3.2.2.23;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-
CC deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-
CC dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-
CC 2'-deoxyribonucleoside-DNA + H(+); Xref=Rhea:RHEA:66592, Rhea:RHEA-
CC COMP:13180, Rhea:RHEA-COMP:16897, Rhea:RHEA-COMP:17067,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:136412, ChEBI:CHEBI:157695,
CC ChEBI:CHEBI:167181; EC=4.2.99.18;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have a 5-fold increased
CC spontaneous mutation frequency. A double mutM/mutY mutant has a 1000-
CC fold increased spontaneous mutation frequency (PubMed:12483591). Triple
CC ytkD/mutM/mutY disrupted strains show increased mutation rates during
CC both exponential and stationary phase (PubMed:19011023).
CC {ECO:0000269|PubMed:12483591, ECO:0000269|PubMed:19011023}.
CC -!- SIMILARITY: Belongs to the FPG family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC00351.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF008220; AAC00351.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB14868.2; -; Genomic_DNA.
DR PIR; B69663; B69663.
DR RefSeq; NP_390786.2; NC_000964.3.
DR RefSeq; WP_003246122.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34403; -.
DR SMR; O34403; -.
DR STRING; 224308.BSU29080; -.
DR PaxDb; O34403; -.
DR EnsemblBacteria; CAB14868; CAB14868; BSU_29080.
DR GeneID; 936741; -.
DR KEGG; bsu:BSU29080; -.
DR PATRIC; fig|224308.43.peg.3042; -.
DR eggNOG; COG0266; Bacteria.
DR InParanoid; O34403; -.
DR OMA; GVHLRMT; -.
DR PhylomeDB; O34403; -.
DR BioCyc; BSUB:BSU29080-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0034039; F:8-oxo-7,8-dihydroguanine DNA N-glycosylase activity; IBA:GO_Central.
DR GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0019104; F:DNA N-glycosylase activity; IBA:GO_Central.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR Gene3D; 3.20.190.10; -; 1.
DR HAMAP; MF_00103; Fapy_DNA_glycosyl; 1.
DR InterPro; IPR015886; DNA_glyclase/AP_lyase_DNA-bd.
DR InterPro; IPR015887; DNA_glyclase_Znf_dom_DNA_BS.
DR InterPro; IPR020629; Formamido-pyr_DNA_Glyclase.
DR InterPro; IPR012319; FPG_cat.
DR InterPro; IPR035937; MutM-like_N-ter.
DR InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR InterPro; IPR000214; Znf_DNA_glyclase/AP_lyase.
DR InterPro; IPR010663; Znf_FPG/IleRS.
DR Pfam; PF01149; Fapy_DNA_glyco; 1.
DR Pfam; PF06831; H2TH; 1.
DR Pfam; PF06827; zf-FPG_IleRS; 1.
DR SMART; SM00898; Fapy_DNA_glyco; 1.
DR SMART; SM01232; H2TH; 1.
DR SUPFAM; SSF46946; SSF46946; 1.
DR SUPFAM; SSF81624; SSF81624; 1.
DR TIGRFAMs; TIGR00577; fpg; 1.
DR PROSITE; PS51068; FPG_CAT; 1.
DR PROSITE; PS01242; ZF_FPG_1; 1.
DR PROSITE; PS51066; ZF_FPG_2; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA-binding; Glycosidase; Hydrolase; Lyase;
KW Metal-binding; Multifunctional enzyme; Reference proteome; Zinc;
KW Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..276
FT /note="Formamidopyrimidine-DNA glycosylase"
FT /id="PRO_0000170811"
FT ZN_FING 240..274
FT /note="FPG-type"
FT ACT_SITE 2
FT /note="Schiff-base intermediate with DNA"
FT /evidence="ECO:0000250"
FT ACT_SITE 3
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 60
FT /note="Proton donor; for beta-elimination activity"
FT /evidence="ECO:0000250"
FT ACT_SITE 264
FT /note="Proton donor; for delta-elimination activity"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
SQ SEQUENCE 276 AA; 31002 MW; A9B745DBAB295314 CRC64;
MPELPEVETV RRTLTGLVKG KTIKSVEIRW PNIIKRPAEP EEFARKLAGE TIQSIGRRGK
FLLFHLDHYV MVSHLRMEGK YGLHQAEEPD DKHVHVIFTM TDGTQLRYRD VRKFGTMHLF
KPGEEAGELP LSQLGPEPDA EEFTSAYLKD RLAKTNRAVK TALLDQKTVV GLGNIYVDEA
LFRAGVHPET KANQLSDKTI KTLHAEIKNT LQEAIDAGGS TVRSYINSQG EIGMFQLQHF
VYGKKDEPCK NCGTMISKIV VGGRGTHFCA KCQTKK
