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O34919 (YOSS_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
SPBc2 prophage-derived deoxyuridine 5'-triphosphate nucleotidohydrolase YosS
Short name=dUTPase
EC=3.6.1.23
Alternative name(s):
dUTP pyrophosphatase
Gene names
Name:yosS
Synonyms:yojU
Ordered Locus Names:BSU20020
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length142 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.

Catalytic activity

dUTP + H2O = dUMP + diphosphate.

Cofactor

Magnesium. Ref.3

Pathway

Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP (dUTP route): step 2/2.

Subunit structure

Homotrimer. Ref.3

Sequence similarities

Belongs to the dUTPase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.6 µM for dUTP Ref.3

pH dependence:

Optimum pH is 5.5.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 142142SPBc2 prophage-derived deoxyuridine 5'-triphosphate nucleotidohydrolase YosS
PRO_0000389002

Regions

Region61 – 633Substrate binding By similarity
Region78 – 803Substrate binding By similarity

Sites

Binding site741Substrate By similarity

Secondary structure

1 ............................. 142
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O34919 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: A986C4CCF2364B74

FASTA14216,148
        10         20         30         40         50         60 
MQIKIKYLDE TQTRINKMEQ GDWIDLRAAE DVAIKKDEFK LVPLGVAMEL PEGYEAHVVP 

        70         80         90        100        110        120 
RSSTYKNFGV IQTNSMGVID ESYKGDNDFW FFPAYALRDT KIKKGDRICQ FRIMKKMPAV 

       130        140 
DLIEVDRLGN GDRGGHGSTG TK

« Hide

References

« Hide 'large scale' references
[1]"An 8 kb nucleotide sequence at the 3' flanking region of the sspC gene (184 degrees) on the Bacillus subtilis 168 chromosome containing an intein and an intron."
Ghim S.-Y., Choi S.-K., Shin B.-S., Park S.-H.
DNA Res. 5:121-126(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Cloning, expression, purification, and characterisation of the dUTPase encoded by the integrated Bacillus subtilis temperate bacteriophage SPbeta."
Persson R., McGeehan J., Wilson K.S.
Protein Expr. Purif. 42:92-99(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT.
[4]"Crystallization and preliminary crystallographic analysis of deoxyuridine 5'-triphosphate nucleotidohydrolase from Bacillus subtilis."
Persson R., Harkiolaki M., McGeehan J., Wilson K.S.
Acta Crystallogr. D 57:876-878(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY CRYSTALLIZATION.
[5]"Crystallization and preliminary X-ray analysis of three dUTPases from Gram-positive bacteria."
Li G.-L., Wang J., Li L.-F., Su X.-D.
Acta Crystallogr. F 65:339-342(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF012906 Genomic DNA. Translation: AAB92488.1.
AL009126 Genomic DNA. Translation: CAB13893.1.
RefSeqNP_389883.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BAZX-ray2.30A/B/C1-142[»]
2XX6X-ray1.74A/B/C/D1-142[»]
2XY3X-ray2.55A/B/C/D/E/F1-142[»]
2Y1TX-ray1.89A/B/C/D/E/F1-142[»]
ProteinModelPortalO34919.
SMRO34919. Positions 1-128.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU20020.

Proteomic databases

PaxDbO34919.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13893; CAB13893; BSU20020.
GeneID939536.
KEGGbsu:BSU20020.
PATRIC18975849. VBIBacSub10457_2115.

Organism-specific databases

GenoListBSU20020.

Phylogenomic databases

eggNOGCOG0756.
HOGENOMHOG000028966.
KOK01520.
ProtClustDBCLSK887343.

Enzyme and pathway databases

BioCycBSUB:BSU20020-MONOMER.
UniPathwayUPA00610; UER00666.

Family and domain databases

InterProIPR008180. dUTP_pyroPase.
IPR008181. dUTP_pyroPase_sf.
[Graphical view]
PANTHERPTHR11241. PTHR11241. 1 hit.
PfamPF00692. dUTPase. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO34919.

Entry information

Entry nameYOSS_BACSU
AccessionPrimary (citable) accession number: O34919
Secondary accession number(s): Q7BVP9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: January 1, 1998
Last modified: May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents