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O35016

- YFKJ_BACSU

UniProt

O35016 - YFKJ_BACSU

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Protein

Low molecular weight protein-tyrosine-phosphatase YfkJ

Gene
yfkJ, BSU07880
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - 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.

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.

Protein family/group databases

PptaseDBiP3D0507171.

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: 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.1 Publication

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 – 1312
Helixi14 – 2815
Turni32 – 343
Beta strandi35 – 439
Turni45 – 484
Helixi53 – 619
Helixi76 – 816
Beta strandi83 – 897
Helixi90 – 10011
Beta strandi108 – 1103
Helixi111 – 1144
Helixi126 – 1294
Helixi132 – 15322

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ETMX-ray1.60A/B1-156[»]
ProteinModelPortaliO35016.
SMRiO35016. Positions 2-150.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0394.
HOGENOMiHOG000273094.
KOiK01104.
OMAiDSAGTHD.
OrthoDBiEOG6MH5JB.
PhylomeDBiO35016.

Family and domain databases

InterProiIPR023485. Ptyr_pPase_SF.
IPR000106. Tyr_phospatase/Ars_reductase.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]
PANTHERiPTHR11717. PTHR11717. 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

MISVLFVCLG NICRSPMAEA IFRDLAAKKG LEGKIKADSA GIGGWHIGNP    50
PHEGTQEILR REGISFDGML ARQVSEQDLD DFDYIIAMDA ENIGSLRSMA 100
GFKNTSHIKR LLDYVEDSDL ADVPDPYYTG NFEEVCQLIK TGCEQLLASI 150
QKEKQL 156
Length:156
Mass (Da):17,269
Last modified:January 1, 1998 - v1
Checksum:i7CDC8C4D6D0FD528
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL009126 Genomic DNA. Translation: CAB12617.1.
D83967 Genomic DNA. Translation: BAA23400.1.
PIRiE69808.
RefSeqiNP_388669.1. NC_000964.3.
WP_003243480.1. NZ_CM000487.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AL009126 Genomic DNA. Translation: CAB12617.1 .
D83967 Genomic DNA. Translation: BAA23400.1 .
PIRi E69808.
RefSeqi NP_388669.1. NC_000964.3.
WP_003243480.1. NZ_CM000487.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4ETM X-ray 1.60 A/B 1-156 [» ]
ProteinModelPortali O35016.
SMRi O35016. Positions 2-150.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU07880.

Protein family/group databases

PptaseDBi P3D0507171.

Proteomic databases

PaxDbi O35016.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB12617 ; CAB12617 ; BSU07880 .
GeneIDi 939191.
KEGGi bsu:BSU07880.
PATRICi 18973226. VBIBacSub10457_0827.

Organism-specific databases

GenoListi BSU07880.

Phylogenomic databases

eggNOGi COG0394.
HOGENOMi HOG000273094.
KOi K01104.
OMAi DSAGTHD.
OrthoDBi EOG6MH5JB.
PhylomeDBi O35016.

Enzyme and pathway databases

BioCyci BSUB:BSU07880-MONOMER.
RETL1328306-WGS:GSTH-4023-MONOMER.
SABIO-RK O35016.

Family and domain databases

InterProi IPR023485. Ptyr_pPase_SF.
IPR000106. Tyr_phospatase/Ars_reductase.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view ]
PANTHERi PTHR11717. PTHR11717. 1 hit.
Pfami PF01451. LMWPc. 1 hit.
[Graphical view ]
PRINTSi PR00719. LMWPTPASE.
SMARTi SM00226. LMWPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52788. SSF52788. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 82 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

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