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O35016 (YFKJ_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. 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 YfkJ

Short name=LMPTP
EC=3.1.3.48
Gene names
Name:yfkJ
Ordered Locus Names:BSU07880
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length156 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 and N-ethylmaleimide, while the addition of Mg2+, Ca2+ or Fe3+ ions has minimal effect. Inhibited in a competitive manner by vanadate. Ref.3

Induction

By ethanol stress. Expression is sigma B-dependent. Ref.3

Sequence similarities

Belongs to the low molecular weight phosphotyrosine protein phosphatase family.

Biophysicochemical properties

Kinetic parameters:

KM=244 µM for p-nitrophenyl-phosphate (at 37 degrees Celsius) Ref.3

pH dependence:

Optimum pH is 6.0.

Ontologies

Keywords
   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 – 156156Low molecular weight protein-tyrosine-phosphatase YfkJ
PRO_0000234659

Sites

Active site81Nucleophile
Active site141
Active site1251Proton donor

Experimental info

Mutagenesis81C → S: Completely abolishes the tyrosine-phosphatase activity. Ref.3
Mutagenesis141R → K: Completely abolishes the tyrosine-phosphatase activity. Ref.3
Mutagenesis1251D → A: Completely abolishes the tyrosine-phosphatase activity. Ref.3

Secondary structure

....................... 156
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O35016 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 7CDC8C4D6D0FD528

FASTA15617,269
        10         20         30         40         50         60 
MISVLFVCLG NICRSPMAEA IFRDLAAKKG LEGKIKADSA GIGGWHIGNP PHEGTQEILR 

        70         80         90        100        110        120 
REGISFDGML ARQVSEQDLD DFDYIIAMDA ENIGSLRSMA GFKNTSHIKR LLDYVEDSDL 

       130        140        150 
ADVPDPYYTG NFEEVCQLIK TGCEQLLASI QKEKQL 

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]"Nucleotide sequence analysis of B. subtilis cromosome in 74 degree region."
Sekiguchi J., Yamamoto H., Uchiyama S., Fajar A.
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / AC327.
[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-8; ARG-14 AND ASP-125, CHARACTERIZATION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: 168 / JH642.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL009126 Genomic DNA. Translation: CAB12617.1.
D83967 Genomic DNA. Translation: BAA23400.1.
PIRE69808.
RefSeqNP_388669.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4ETMX-ray1.60A/B1-156[»]
ProteinModelPortalO35016.
SMRO35016. Positions 2-150.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224308.BSU07880.

Protein family/group databases

PptaseDBP3D0507171.

Proteomic databases

PaxDbO35016.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB12617; CAB12617; BSU07880.
GeneID939191.
KEGGbsu:BSU07880.
PATRIC18973226. VBIBacSub10457_0827.

Organism-specific databases

GenoListBSU07880.

Phylogenomic databases

eggNOGCOG0394.
HOGENOMHOG000273094.
KOK01104.
OMAGTGSWHV.
OrthoDBEOG6MH5JB.
ProtClustDBCLSK2502625.

Enzyme and pathway databases

BioCycBSUB:BSU07880-MONOMER.
SABIO-RKO35016.

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...

Entry information

Entry nameYFKJ_BACSU
AccessionPrimary (citable) accession number: O35016
Secondary accession number(s): Q79EX9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 79 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