NTPPA_BACSU
ID NTPPA_BACSU Reviewed; 189 AA.
AC Q02169; P37576;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=dTTP/UTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00528, ECO:0000305};
DE Short=dTTPase/UTPase {ECO:0000255|HAMAP-Rule:MF_00528, ECO:0000305};
DE EC=3.6.1.9 {ECO:0000255|HAMAP-Rule:MF_00528, ECO:0000269|PubMed:24210219};
DE AltName: Full=Multicopy associated filamentation protein {ECO:0000303|PubMed:8387996};
DE AltName: Full=Nucleoside triphosphate pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00528, ECO:0000303|PubMed:24210219};
DE AltName: Full=Nucleotide pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00528, ECO:0000303|PubMed:24210219};
DE Short=Nucleotide PPase {ECO:0000255|HAMAP-Rule:MF_00528, ECO:0000305};
DE AltName: Full=Septum formation protein Maf {ECO:0000305};
GN Name=maf {ECO:0000303|PubMed:8387996}; OrderedLocusNames=BSU28050;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], OVEREXPRESSION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168;
RX PubMed=8387996; DOI=10.1128/jb.175.10.3139-3145.1993;
RA Butler Y.X., Abhayawardhane Y., Stewart G.C.;
RT "Amplification of the Bacillus subtilis maf gene results in arrested septum
RT formation.";
RL J. Bacteriol. 175:3139-3145(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1400224; DOI=10.1128/jb.174.21.6717-6728.1992;
RA Levin P.A., Margolis P.S., Setlow P., Losick R., Sun D.;
RT "Identification of Bacillus subtilis genes for septum placement and shape
RT determination.";
RL J. Bacteriol. 174:6717-6728(1992).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-35.
RC STRAIN=168 / PY79;
RX PubMed=8419299; DOI=10.1128/jb.175.2.528-540.1993;
RA Margolis P.S., Driks A., Losick R.;
RT "Sporulation gene spoIIB from Bacillus subtilis.";
RL J. Bacteriol. 175:528-540(1993).
RN [5] {ECO:0007744|PDB:1EX2, ECO:0007744|PDB:1EXC}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP DUTP, AND SUBUNIT.
RX PubMed=10841541; DOI=10.1073/pnas.97.12.6328;
RA Minasov G., Teplova M., Stewart G.C., Koonin E.V., Anderson W.F., Egli M.;
RT "Functional implications from crystal structures of the conserved Bacillus
RT subtilis protein Maf with and without dUTP.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:6328-6333(2000).
RN [6] {ECO:0007744|PDB:4HEB}
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVE SITE, AND MUTAGENESIS OF ARG-14;
RP GLU-34; LYS-53; ASP-70 AND LYS-82.
RX PubMed=24210219; DOI=10.1016/j.chembiol.2013.09.011;
RA Tchigvintsev A., Tchigvintsev D., Flick R., Popovic A., Dong A., Xu X.,
RA Brown G., Lu W., Wu H., Cui H., Dombrowski L., Joo J.C., Beloglazova N.,
RA Min J., Savchenko A., Caudy A.A., Rabinowitz J.D., Murzin A.G.,
RA Yakunin A.F.;
RT "Biochemical and structural studies of conserved Maf proteins revealed
RT nucleotide pyrophosphatases with a preference for modified nucleotides.";
RL Chem. Biol. 20:1386-1398(2013).
CC -!- FUNCTION: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP
CC and UTP. Can also hydrolyze CTP and the modified nucleotides pseudo-
CC UTP, 5-methyl-CTP (m(5)CTP) and 5-methyl-UTP (m(5)UTP)
CC (PubMed:24210219). May have a dual role in cell division arrest and in
CC preventing the incorporation of modified nucleotides into cellular
CC nucleic acids (PubMed:24210219). {ECO:0000269|PubMed:24210219}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTTP + H2O = diphosphate + dTMP + H(+); Xref=Rhea:RHEA:28534,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37568, ChEBI:CHEBI:63528; EC=3.6.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00528,
CC ECO:0000269|PubMed:24210219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + UTP = diphosphate + H(+) + UMP; Xref=Rhea:RHEA:29395,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:46398, ChEBI:CHEBI:57865; EC=3.6.1.9;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00528,
CC ECO:0000269|PubMed:24210219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H2O = CMP + diphosphate + H(+); Xref=Rhea:RHEA:27762,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:37563, ChEBI:CHEBI:60377; EC=3.6.1.9;
CC Evidence={ECO:0000269|PubMed:24210219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + psi-UTP = diphosphate + H(+) + psi-UMP;
CC Xref=Rhea:RHEA:58740, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58380, ChEBI:CHEBI:142798;
CC Evidence={ECO:0000269|PubMed:24210219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-methyl-CTP + H2O = 5-methyl-CMP + diphosphate + H(+);
CC Xref=Rhea:RHEA:58732, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:142795, ChEBI:CHEBI:142796;
CC Evidence={ECO:0000269|PubMed:24210219};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + TTP = 5-methyl-UMP + diphosphate + H(+);
CC Xref=Rhea:RHEA:58736, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:63527, ChEBI:CHEBI:142797;
CC Evidence={ECO:0000269|PubMed:24210219};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00528};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=50.6 uM for dTTP {ECO:0000269|PubMed:24210219};
CC KM=72.4 uM for UTP {ECO:0000269|PubMed:24210219};
CC KM=25.0 uM for CTP {ECO:0000269|PubMed:24210219};
CC KM=4.7 uM for m(5)UTP {ECO:0000269|PubMed:24210219};
CC KM=7.8 uM for m(5)CTP {ECO:0000269|PubMed:24210219};
CC KM=5.7 uM for pseudo-UTP {ECO:0000269|PubMed:24210219};
CC Note=kcat is 11.6 sec(-1) with dTTP as substrate. kcat is 4.9 sec(-1)
CC with UTP as substrate. kcat is 7.1 sec(-1) with CTP as substrate.
CC kcat is 2.4 sec(-1) with m(5)UTP as substrate. kcat is 8.5 sec(-1)
CC with m(5)CTP as substrate. kcat is 7.2 sec(-1) with pseudo-UTP as
CC substrate. {ECO:0000269|PubMed:24210219};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10841541}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00528,
CC ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Not essential for cell division.
CC {ECO:0000269|PubMed:8387996}.
CC -!- MISCELLANEOUS: Overexpression results in extensive filamentation caused
CC by a disruption and subsequent inhibition of the septation process.
CC {ECO:0000269|PubMed:8387996}.
CC -!- SIMILARITY: Belongs to the Maf family. YhdE subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00528, ECO:0000305|PubMed:24210219}.
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DR EMBL; L08793; AAA22582.1; -; Genomic_DNA.
DR EMBL; M96343; AAA22395.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14765.1; -; Genomic_DNA.
DR EMBL; L04519; AAB59027.1; -; Genomic_DNA.
DR PIR; A45239; A45239.
DR RefSeq; NP_390683.1; NC_000964.3.
DR RefSeq; WP_004398496.1; NZ_JNCM01000036.1.
DR PDB; 1EX2; X-ray; 1.85 A; A/B=1-189.
DR PDB; 1EXC; X-ray; 2.70 A; A/B=1-189.
DR PDB; 4HEB; X-ray; 2.26 A; A/B=1-189.
DR PDBsum; 1EX2; -.
DR PDBsum; 1EXC; -.
DR PDBsum; 4HEB; -.
DR AlphaFoldDB; Q02169; -.
DR SMR; Q02169; -.
DR STRING; 224308.BSU28050; -.
DR DrugBank; DB02333; Deoxyuridine-5'-Triphosphate.
DR PaxDb; Q02169; -.
DR PRIDE; Q02169; -.
DR DNASU; 936605; -.
DR EnsemblBacteria; CAB14765; CAB14765; BSU_28050.
DR GeneID; 936605; -.
DR KEGG; bsu:BSU28050; -.
DR PATRIC; fig|224308.179.peg.3047; -.
DR eggNOG; COG0424; Bacteria.
DR InParanoid; Q02169; -.
DR OMA; RIDGDFY; -.
DR PhylomeDB; Q02169; -.
DR BioCyc; BSUB:BSU28050-MON; -.
DR EvolutionaryTrace; Q02169; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0036218; F:dTTP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0035529; F:NADH pyrophosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IBA:GO_Central.
DR GO; GO:0036221; F:UTP diphosphatase activity; IEA:RHEA.
DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00555; Maf; 1.
DR Gene3D; 3.90.950.10; -; 1.
DR HAMAP; MF_00528; Maf; 1.
DR InterPro; IPR029001; ITPase-like_fam.
DR InterPro; IPR003697; Maf-like.
DR PANTHER; PTHR43213; PTHR43213; 1.
DR Pfam; PF02545; Maf; 1.
DR PIRSF; PIRSF006305; Maf; 1.
DR SUPFAM; SSF52972; SSF52972; 1.
DR TIGRFAMs; TIGR00172; maf; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Disulfide bond; Hydrolase; Nucleotide metabolism;
KW Reference proteome.
FT CHAIN 1..189
FT /note="dTTP/UTP pyrophosphatase"
FT /id="PRO_0000122974"
FT ACT_SITE 70
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528,
FT ECO:0000305|PubMed:24210219"
FT SITE 13
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528,
FT ECO:0000305|PubMed:24210219"
FT SITE 71
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528,
FT ECO:0000305|PubMed:24210219"
FT SITE 153
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00528,
FT ECO:0000305|PubMed:24210219"
FT DISULFID 74..79
FT MUTAGEN 14
FT /note="R->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 34
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 53
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 70
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT MUTAGEN 82
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:24210219"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:1EX2"
FT HELIX 12..19
FT /evidence="ECO:0007829|PDB:1EX2"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:1EXC"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1EXC"
FT HELIX 42..60
FT /evidence="ECO:0007829|PDB:1EX2"
FT STRAND 64..75
FT /evidence="ECO:0007829|PDB:1EX2"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:1EX2"
FT HELIX 86..96
FT /evidence="ECO:0007829|PDB:1EX2"
FT STRAND 99..111
FT /evidence="ECO:0007829|PDB:1EX2"
FT STRAND 114..126
FT /evidence="ECO:0007829|PDB:1EX2"
FT HELIX 131..138
FT /evidence="ECO:0007829|PDB:1EX2"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:1EX2"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1EX2"
FT HELIX 154..158
FT /evidence="ECO:0007829|PDB:1EX2"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:1EX2"
FT HELIX 167..171
FT /evidence="ECO:0007829|PDB:1EX2"
FT HELIX 175..182
FT /evidence="ECO:0007829|PDB:1EX2"
SQ SEQUENCE 189 AA; 21295 MW; 176A871B94FAEEE9 CRC64;
MTKPLILASQ SPRRKELLDL LQLPYSIIVS EVEEKLNRNF SPEENVQWLA KQKAKAVADL
HPHAIVIGAD TMVCLDGECL GKPQDQEEAA SMLRRLSGRS HSVITAVSIQ AENHSETFYD
KTEVAFWSLS EEEIWTYIET KEPMDKAGAY GIQGRGALFV KKIDGDYYSV MGLPISKTMR
ALRHFDIRA
