MUTT_BACSU
ID MUTT_BACSU Reviewed; 149 AA.
AC P96590; Q797M2;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Putative 8-oxo-dGTP diphosphatase;
DE Short=8-oxo-dGTPase;
DE EC=3.6.1.55;
DE AltName: Full=7,8-dihydro-8-oxoguanine-triphosphatase;
DE AltName: Full=Mutator protein MutT;
DE AltName: Full=dGTP pyrophosphohydrolase;
GN Name=mutT; OrderedLocusNames=BSU04330;
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;
RA Kasahara Y., Nakai S., Lee S., Sadaie Y., Ogasawara N.;
RT "A 148 kbp sequence of the region between 35 and 47 degree of the Bacillus
RT subtilis genome.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
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 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 [4]
RP DISRUPTION PHENOTYPE IN GROWING CELLS.
RC STRAIN=168 / PS832;
RX PubMed=16513759; DOI=10.1128/jb.188.6.2285-2289.2006;
RA Castellanos-Juarez F.X., Alvarez-Alvarez C., Yasbin R.E., Setlow B.,
RA Setlow P., Pedraza-Reyes M.;
RT "YtkD and MutT protect vegetative cells but not spores of Bacillus subtilis
RT from oxidative stress.";
RL J. Bacteriol. 188:2285-2289(2006).
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: May be 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. MutT specifically degrades 8-oxo-
CC dGTP to the monophosphate (By similarity). Functions, in conjunction
CC with ytkD, to protect vegetatively growing cells from DNA-damaging
CC agents such as H(2)O(2) or t-BHP (t-butylhydroperoxide). The 2 proteins
CC do not however protect spores. {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+);
CC Xref=Rhea:RHEA:31575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:63224, ChEBI:CHEBI:77896; EC=3.6.1.55;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- DISRUPTION PHENOTYPE: Growing cells lacking this gene have an unchanged
CC spontaneous mutation frequency, even in triple mutT/yjhB/yvcI
CC disruptions (PubMed:12483591), however they are more sensitive to DNA-
CC damaging agents such as H(2)O(2) or t-BHP (PubMed:16513759). A double
CC ytkD/mutT disruption has a greater mutation frequency than the ytkD
CC disruption, as well as an increased sensitivity to DNA-damaging agents
CC (PubMed:16513759). These properties are also seen in stationary phase
CC cells (PubMed:19011023). {ECO:0000269|PubMed:12483591,
CC ECO:0000269|PubMed:16513759, ECO:0000269|PubMed:19011023}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; AB001488; BAA19270.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12240.1; -; Genomic_DNA.
DR PIR; D69663; D69663.
DR RefSeq; NP_388314.1; NC_000964.3.
DR RefSeq; WP_003246544.1; NZ_JNCM01000031.1.
DR AlphaFoldDB; P96590; -.
DR SMR; P96590; -.
DR STRING; 224308.BSU04330; -.
DR PaxDb; P96590; -.
DR PRIDE; P96590; -.
DR EnsemblBacteria; CAB12240; CAB12240; BSU_04330.
DR GeneID; 938242; -.
DR KEGG; bsu:BSU04330; -.
DR PATRIC; fig|224308.179.peg.459; -.
DR eggNOG; COG0494; Bacteria.
DR InParanoid; P96590; -.
DR OMA; YDIHPSM; -.
DR PhylomeDB; P96590; -.
DR BioCyc; BSUB:BSU04330-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0035539; F:8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA replication; Hydrolase; Magnesium; Manganese;
KW Metal-binding; Mutator protein; Reference proteome.
FT CHAIN 1..149
FT /note="Putative 8-oxo-dGTP diphosphatase"
FT /id="PRO_0000379972"
FT DOMAIN 1..123
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 33..54
FT /note="Nudix box"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 149 AA; 16398 MW; CAF9B56E42BB2E46 CRC64;
MYTQGAFVIV LNESQQILLV KRKDVPLWDL PGGRVDPGES AEEAAVREIL EETGYNAALS
AKIGVYQRPK FQDEQHLFFG SITGGQAMAD GTETAGLKWV SPGRLPLFMV PNRKRQINDF
KNGAQDVNVT VKDSGLLAAI DLLKRRLGK
