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P25052 (TENA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. 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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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thiaminase-2
EC=3.5.99.2
Alternative name(s):
Thiaminase II
Transcriptional activator tenA
Gene names
Name:tenA
Ordered Locus Names:BSU11650
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length236 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Stimulates the production of several extracellular degradative enzymes at the transcriptional level, probably by interfering with degS and degU, which are required for this effect. Is not an essential protein, but affects the sporulation frequency.

Catalytic activity

Thiamine + H2O = 4-amino-5-hydroxymethyl-2-methylpyrimidine + 5-(2-hydroxyethyl)-4-methylthiazole.

Pathway

Cofactor metabolism; thiamine degradation. [regulation]

Cofactor metabolism; thiamine degradation; 4-amino-5-hydroxymethyl-2-methylpyrimidine and 5-(2-hydroxyethyl)-4-methylthiazole from thiamine: step 1/1.

Subunit structure

Homotetramer.

Induction

Repressed by thiamine.

Sequence similarities

Belongs to the thiaminase-2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 236236Thiaminase-2
PRO_0000192046

Sites

Active site1351Nucleophile
Binding site441Thiamine
Binding site1391Thiamine
Binding site1631Thiamine

Secondary structure

1 ........................... 236
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P25052 [UniParc].

Last modified May 1, 1992. Version 1.
Checksum: 6815CFC95BDB07D6

FASTA23627,417
        10         20         30         40         50         60 
MKFSEECRSA AAEWWEGSFV HPFVQGIGDG TLPIDRFKYY VLQDSYYLTH FAKVQSFGAA 

        70         80         90        100        110        120 
YAKDLYTTGR MASHAQGTYE AEMALHREFA ELLEISEEER KAFKPSPTAY SYTSHMYRSV 

       130        140        150        160        170        180 
LSGNFAEILA ALLPCYWLYY EVGEKLLHCD PGHPIYQKWI GTYGGDWFRQ QVEEQINRFD 

       190        200        210        220        230 
ELAENSTEEV RAKMKENFVI SSYYEYQFWG MAYRKEGWSD SAIKEVEECG ASRHNG

« Hide

References

« Hide 'large scale' references
[1]"Cloning and characterization of a pair of novel genes that regulate production of extracellular enzymes in Bacillus subtilis."
Pang A.S.-H., Nathoo S., Wong S.-L.
J. Bacteriol. 173:46-54(1991) [PubMed: 1898926] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[3]"Structural characterization of the regulatory proteins TenA and TenI from Bacillus subtilis and identification of TenA as a thiaminase II."
Toms A.V., Haas A.L., Park J.-H., Begley T.P., Ealick S.E.
Biochemistry 44:2319-2329(2005) [PubMed: 15709744] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH HMP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M73546 Genomic DNA. Translation: AAA22848.1.
AL009126 Genomic DNA. Translation: CAB13022.1.
PIRXMBSTA. A39184.
RefSeqNP_389047.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1TO9X-ray2.40A/B1-236[»]
1TYHX-ray2.54A/B/D/E2-236[»]
1YAFX-ray2.60A/B/C/D1-236[»]
1YAKX-ray2.50A/B/C/D1-236[»]
2QCXX-ray2.20A/B1-236[»]
ProteinModelPortalP25052.
SMRP25052. Positions 1-226.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000001764; EBBACP00000001764; EBBACG00000001762.
GeneID939807.
GenomeReviewsGene locus BSU11650 in contig AL009126_GR.
KEGGbsu:BSU11650.
NMPDRfig|224308.1.peg.1166.
PATRIC18974047. VBIBacSub10457_1217.

Organism-specific databases

GenoListBSU11650. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000001428.
HOGENOMHBG317523.
OMAYTSHLYR.
PhylomeDBP25052.
ProtClustDBCLSK887073.

Enzyme and pathway databases

BioCycBSUB:BSU11650-MONOMER.

Family and domain databases

InterProIPR016084. Haem_Oase-like_multi-hlx.
IPR004305. TENA/THI4/PQQ_synthPqqC_dom.
[Graphical view]
Gene3DG3DSA:1.20.910.10. Haem_Oase-like_multi-hlx. 1 hit.
KOK03707.
PfamPF03070. TENA_THI-4. 1 hit.
[Graphical view]
SUPFAMSSF48613. Heme_oxygenase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameTENA_BACSU
AccessionPrimary (citable) accession number: P25052
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: January 25, 2012
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