Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Low molecular weight protein-tyrosine-phosphatase YfkJ

Gene

yfkJ

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Enzyme regulationi

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.1 Publication

Kineticsi

  1. KM=244 µM for p-nitrophenyl-phosphate (at 37 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 6.0.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei8 – 81Nucleophile
Active sitei14 – 141
Active sitei125 – 1251Proton donor

GO - Molecular functioni

  1. protein tyrosine phosphatase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BioCyciBSUB:BSU07880-MONOMER.
RETL1328306-WGS:GSTH-4023-MONOMER.
SABIO-RKO35016.

Names & Taxonomyi

Protein namesi
Recommended name:
Low molecular weight protein-tyrosine-phosphatase YfkJ (EC:3.1.3.48)
Short name:
LMPTP
Gene namesi
Name:yfkJ
Ordered Locus Names:BSU07880
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU07880.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81C → S: Completely abolishes the tyrosine-phosphatase activity. 1 Publication
Mutagenesisi14 – 141R → K: Completely abolishes the tyrosine-phosphatase activity. 1 Publication
Mutagenesisi125 – 1251D → A: Completely abolishes the tyrosine-phosphatase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 156156Low molecular weight protein-tyrosine-phosphatase YfkJPRO_0000234659Add
BLAST

Proteomic databases

PaxDbiO35016.

Expressioni

Inductioni

By ethanol stress. Expression is sigma B-dependent.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU07880.

Structurei

Secondary structure

1
156
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 1312Combined sources
Helixi14 – 2815Combined sources
Turni32 – 343Combined sources
Beta strandi35 – 439Combined sources
Turni45 – 484Combined sources
Helixi53 – 619Combined sources
Helixi76 – 816Combined sources
Beta strandi83 – 897Combined sources
Helixi90 – 10011Combined sources
Beta strandi108 – 1103Combined sources
Helixi111 – 1144Combined sources
Helixi126 – 1294Combined sources
Helixi132 – 15322Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ETMX-ray1.60A/B1-156[»]
ProteinModelPortaliO35016.
SMRiO35016. Positions 2-150.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0394.
HOGENOMiHOG000273094.
InParanoidiO35016.
KOiK01104.
OMAiGSWHIGK.
OrthoDBiEOG6MH5JB.
PhylomeDBiO35016.

Family and domain databases

InterProiIPR023485. Ptyr_pPase_SF.
IPR000106. Tyr_phospatase/Ars_reductase.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERiPTHR11717:SF7. PTHR11717:SF7. 1 hit.
PfamiPF01451. LMWPc. 1 hit.
[Graphical view]
PRINTSiPR00719. LMWPTPASE.
SMARTiSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMiSSF52788. SSF52788. 1 hit.

Sequencei

Sequence statusi: Complete.

O35016-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MISVLFVCLG NICRSPMAEA IFRDLAAKKG LEGKIKADSA GIGGWHIGNP
60 70 80 90 100
PHEGTQEILR REGISFDGML ARQVSEQDLD DFDYIIAMDA ENIGSLRSMA
110 120 130 140 150
GFKNTSHIKR LLDYVEDSDL ADVPDPYYTG NFEEVCQLIK TGCEQLLASI

QKEKQL
Length:156
Mass (Da):17,269
Last modified:January 1, 1998 - v1
Checksum:i7CDC8C4D6D0FD528
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB12617.1.
D83967 Genomic DNA. Translation: BAA23400.1.
PIRiE69808.
RefSeqiNP_388669.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB12617; CAB12617; BSU07880.
GeneIDi939191.
KEGGibsu:BSU07880.
PATRICi18973226. VBIBacSub10457_0827.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB12617.1.
D83967 Genomic DNA. Translation: BAA23400.1.
PIRiE69808.
RefSeqiNP_388669.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ETMX-ray1.60A/B1-156[»]
ProteinModelPortaliO35016.
SMRiO35016. Positions 2-150.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.BSU07880.

Proteomic databases

PaxDbiO35016.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12617; CAB12617; BSU07880.
GeneIDi939191.
KEGGibsu:BSU07880.
PATRICi18973226. VBIBacSub10457_0827.

Organism-specific databases

GenoListiBSU07880.

Phylogenomic databases

eggNOGiCOG0394.
HOGENOMiHOG000273094.
InParanoidiO35016.
KOiK01104.
OMAiGSWHIGK.
OrthoDBiEOG6MH5JB.
PhylomeDBiO35016.

Enzyme and pathway databases

BioCyciBSUB:BSU07880-MONOMER.
RETL1328306-WGS:GSTH-4023-MONOMER.
SABIO-RKO35016.

Family and domain databases

InterProiIPR023485. Ptyr_pPase_SF.
IPR000106. Tyr_phospatase/Ars_reductase.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERiPTHR11717:SF7. PTHR11717:SF7. 1 hit.
PfamiPF01451. LMWPc. 1 hit.
[Graphical view]
PRINTSiPR00719. LMWPTPASE.
SMARTiSM00226. LMWPc. 1 hit.
[Graphical view]
SUPFAMiSSF52788. SSF52788. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiYFKJ_BACSU
AccessioniPrimary (citable) accession number: O35016
Secondary accession number(s): Q79EX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: January 1, 1998
Last modified: April 29, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.