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P96717

- YWQE_BACSU

UniProt

P96717 - YWQE_BACSU

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Protein

Tyrosine-protein phosphatase YwqE

Gene
ywqE, BSU36240
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Dephosphorylates the phosphotyrosine-containing proteins YwqD, YwqF and Ssb.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Cofactori

Manganese.

Enzyme regulationi

Inhibited by vanadate and sodium pyrophosphate. Not inhibited by sodium fluoride.

pH dependencei

Optimally active at alkaline pHs. Activity increases with increasing pHs.

GO - Molecular functioni

  1. manganese ion binding Source: InterPro
  2. protein tyrosine phosphatase activity Source: UniProtKB-EC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Ligandi

Manganese

Enzyme and pathway databases

BioCyciBSUB:BSU36240-MONOMER.
SABIO-RKP96717.

Protein family/group databases

PptaseDBiP3D0505166.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase YwqE (EC:3.1.3.48)
Gene namesi
Name:ywqE
Ordered Locus Names:BSU36240
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU36240.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi3 – 31D → A: Large decrease in activity. 1 Publication
Mutagenesisi5 – 51H → A: Large decrease in activity. 1 Publication
Mutagenesisi7 – 71H → A: Large decrease in activity.
Mutagenesisi42 – 421H → A: Large decrease in activity. 1 Publication
Mutagenesisi136 – 1361H → A: Large decrease in activity. 1 Publication
Mutagenesisi194 – 1941D → A: Large decrease in activity. 1 Publication
Mutagenesisi196 – 1961H → A: Large decrease in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 254254Tyrosine-protein phosphatase YwqEPRO_0000057893Add
BLAST

Proteomic databases

PaxDbiP96717.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU36240.

Structurei

Secondary structure

1
254
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65
Beta strandi12 – 154
Helixi19 – 3113
Beta strandi36 – 383
Beta strandi42 – 454
Helixi52 – 6817
Beta strandi74 – 763
Beta strandi80 – 823
Helixi87 – 926
Helixi99 – 1013
Beta strandi102 – 1087
Helixi118 – 12710
Beta strandi131 – 1355
Helixi137 – 1393
Helixi141 – 1455
Helixi148 – 1558
Beta strandi159 – 1635
Helixi164 – 1685
Turni169 – 1713
Helixi173 – 18412
Beta strandi190 – 1923
Beta strandi197 – 2015
Helixi205 – 21612
Helixi219 – 23214

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QY6X-ray1.80A1-254[»]
3QY7X-ray1.62A1-254[»]
ProteinModelPortaliP96717.
SMRiP96717. Positions 1-237.

Miscellaneous databases

EvolutionaryTraceiP96717.

Family & Domainsi

Sequence similaritiesi

Belongs to the CpsB/CapC family.

Phylogenomic databases

eggNOGiCOG4464.
HOGENOMiHOG000007624.
KOiK01104.
OMAiTPHTLNG.
OrthoDBiEOG6PKFDD.
PhylomeDBiP96717.

Family and domain databases

InterProiIPR016667. Caps_polysacc_synth_CpsB/CapC.
IPR004013. PHP_C.
IPR016195. Pol/histidinol_Pase-like.
[Graphical view]
PfamiPF02811. PHP. 1 hit.
[Graphical view]
PIRSFiPIRSF016557. Caps_synth_CpsB. 1 hit.
SUPFAMiSSF89550. SSF89550. 1 hit.

Sequencei

Sequence statusi: Complete.

P96717-1 [UniParc]FASTAAdd to Basket

« Hide

MIDIHCHILP AMDDGAGDSA DSIEMARAAV RQGIRTIIAT PHHNNGVYKN    50
EPAAVREAAD QLNKRLIKED IPLHVLPGQE IRIYGEVEQD LAKRQLLSLN 100
DTKYILIEFP FDHVPRYAEQ LFYDLQLKGY IPVIAHPERN REIRENPSLL 150
YHLVEKGAAS QITSGSLAGI FGKQLKAFSL RLVEANLIHF VASDAHNVKT 200
RNFHTQEALY VLEKEFGSEL PYMLTENAEL LLRNQTIFRQ PPQPVKRRKL 250
FGFF 254
Length:254
Mass (Da):28,958
Last modified:May 1, 1997 - v1
Checksum:iE2625AE51E0E9A94
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z92952 Genomic DNA. Translation: CAB07456.1.
AL009126 Genomic DNA. Translation: CAB15641.1.
PIRiH70066.
RefSeqiNP_391505.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB15641; CAB15641; BSU36240.
GeneIDi936893.
KEGGibsu:BSU36240.
PATRICi18979268. VBIBacSub10457_3796.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z92952 Genomic DNA. Translation: CAB07456.1 .
AL009126 Genomic DNA. Translation: CAB15641.1 .
PIRi H70066.
RefSeqi NP_391505.1. NC_000964.3.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3QY6 X-ray 1.80 A 1-254 [» ]
3QY7 X-ray 1.62 A 1-254 [» ]
ProteinModelPortali P96717.
SMRi P96717. Positions 1-237.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU36240.

Protein family/group databases

PptaseDBi P3D0505166.

Proteomic databases

PaxDbi P96717.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB15641 ; CAB15641 ; BSU36240 .
GeneIDi 936893.
KEGGi bsu:BSU36240.
PATRICi 18979268. VBIBacSub10457_3796.

Organism-specific databases

GenoListi BSU36240.

Phylogenomic databases

eggNOGi COG4464.
HOGENOMi HOG000007624.
KOi K01104.
OMAi TPHTLNG.
OrthoDBi EOG6PKFDD.
PhylomeDBi P96717.

Enzyme and pathway databases

BioCyci BSUB:BSU36240-MONOMER.
SABIO-RK P96717.

Miscellaneous databases

EvolutionaryTracei P96717.

Family and domain databases

InterProi IPR016667. Caps_polysacc_synth_CpsB/CapC.
IPR004013. PHP_C.
IPR016195. Pol/histidinol_Pase-like.
[Graphical view ]
Pfami PF02811. PHP. 1 hit.
[Graphical view ]
PIRSFi PIRSF016557. Caps_synth_CpsB. 1 hit.
SUPFAMi SSF89550. SSF89550. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334 degrees)."
    Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V., Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G., Kunst F., Danchin A., Glaser P.
    Microbiology 143:3313-3328(1997) [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.
    , 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. "In vitro characterization of the Bacillus subtilis protein tyrosine phosphatase YwqE."
    Mijakovic I., Musumeci L., Tautz L., Petranovic D., Edwards R.A., Jensen P.R., Mustelin T., Deutscher J., Bottini N.
    J. Bacteriol. 187:3384-3390(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, MUTAGENESIS OF ASP-3; HIS-5; HIS-42; HIS-136; ASP-194 AND HIS-196.
  4. "Bacterial single-stranded DNA-binding proteins are phosphorylated on tyrosine."
    Mijakovic I., Petranovic D., Macek B., Cepo T., Mann M., Davies J., Jensen P.R., Vujaklija D.
    Nucleic Acids Res. 34:1588-1596(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiYWQE_BACSU
AccessioniPrimary (citable) accession number: P96717
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: May 1, 1997
Last modified: July 9, 2014
This is version 83 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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