Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P39155 (YWLE_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Low molecular weight protein-tyrosine-phosphatase YwlE

Short name=LMPTP
EC=3.1.3.48
Gene names
Name:ywlE
Ordered Locus Names:BSU36930
ORF Names:ipc-31d
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length150 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Dephosphorylates the phosphotyrosine-containing proteins. Involved in ethanol stress resistance.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulation

Efficiently inhibited by Cu2+ ion, Zn2+ ion, sodium pyrophosphate and N-ethylmaleimide, while the addition of Mg2+, Ca2+ or Fe3+ ions has minimal effect. Inhibited in a competitive manner by vanadate. Ref.3

Sequence similarities

Belongs to the low molecular weight phosphotyrosine protein phosphatase family.

Biophysicochemical properties

Kinetic parameters:

KM=0.157 mM for p-nitrophenyl-phosphate (at 37 degrees Celsius) Ref.3 Ref.4

KM=28 mM for p-nitrophenyl-phosphate (at 55 degrees Celsius)

pH dependence:

Optimum pH is 5.5.

Ontologies

Keywords
   DomainCoiled coil
   Molecular functionHydrolase
Protein phosphatase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Molecular_functionprotein tyrosine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 150150Low molecular weight protein-tyrosine-phosphatase YwlE
PRO_0000046579

Regions

Coiled coil121 – 15030 Potential

Sites

Active site71Nucleophile
Active site131
Active site1181Proton donor

Experimental info

Mutagenesis71C → S: Completely abolishes the tyrosine-phosphatase activity. Ref.3
Mutagenesis131R → K: Completely abolishes the tyrosine-phosphatase activity. Ref.3
Mutagenesis1181D → A: Completely abolishes the tyrosine-phosphatase activity. Ref.3

Secondary structure

.................... 150
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P39155 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: E1BD5EA5231DED2C

FASTA15016,785
        10         20         30         40         50         60 
MDIIFVCTGN TCRSPMAEAL FKSIAEREGL NVNVRSAGVF ASPNGKATPH AVEALFEKHI 

        70         80         90        100        110        120 
ALNHVSSPLT EELMESADLV LAMTHQHKQI IASQFGRYRD KVFTLKEYVT GSHGDVLDPF 

       130        140        150 
GGSIDIYKQT RDELEELLRQ LAKQLKKDRR 

« Hide

References

« Hide 'large scale' references
[1]"Two genes encoding uracil phosphoribosyltransferase are present in Bacillus subtilis."
Martinussen J., Glaser P., Andersen P.S., Saxild H.H.
J. Bacteriol. 177:271-274(1995) [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]"Low-molecular-weight protein tyrosine phosphatases of Bacillus subtilis."
Musumeci L., Bongiorni C., Tautz L., Edwards R.A., Osterman A., Perego M., Mustelin T., Bottini N.
J. Bacteriol. 187:4945-4956(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-7; ARG-13 AND ASP-118, CHARACTERIZATION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: 168 / JH642.
[4]"Solution structure of a low-molecular-weight protein tyrosine phosphatase from Bacillus subtilis."
Xu H., Xia B., Jin C.
J. Bacteriol. 188:1509-1517(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-150, BIOPHYSICOCHEMICAL PROPERTIES.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z38002 Genomic DNA. Translation: CAA86107.1.
AL009126 Genomic DNA. Translation: CAB15710.1.
PIRS49360. I40479.
RefSeqNP_391574.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZGGNMR-A1-150[»]
4ETIX-ray1.80A1-150[»]
4ETNX-ray1.10A1-150[»]
4KK3X-ray1.70A1-150[»]
4KK4X-ray1.80A1-150[»]
ProteinModelPortalP39155.
SMRP39155. Positions 1-150.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-7148489.
STRING224308.BSU36930.

Protein family/group databases

PptaseDBP3D0507170.

Proteomic databases

PaxDbP39155.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB15710; CAB15710; BSU36930.
GeneID937021.
KEGGbsu:BSU36930.
PATRIC18979420. VBIBacSub10457_3872.

Organism-specific databases

GenoListBSU36930.

Phylogenomic databases

eggNOGCOG0394.
HOGENOMHOG000273091.
KOK01104.
OMAPMAMALL.
OrthoDBEOG6MH5JB.
ProtClustDBCLSK888045.

Enzyme and pathway databases

BioCycBSUB:BSU36930-MONOMER.
SABIO-RKP39155.

Family and domain databases

InterProIPR023485. Ptyr_pPase_SF.
IPR000106. Tyr_phospatase/Ars_reductase.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERPTHR11717. PTHR11717. 1 hit.
PfamPF01451. LMWPc. 1 hit.
[Graphical view]
PRINTSPR00719. LMWPTPASE.
SMARTSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMSSF52788. SSF52788. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP39155.

Entry information

Entry nameYWLE_BACSU
AccessionPrimary (citable) accession number: P39155
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Bacillus subtilis

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