P96717 (YWQE_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tyrosine-protein phosphatase YwqE
EC=3.1.3.48

Gene names

Name:	ywqE
Ordered Locus Names:	BSU36240

Organism

Bacillus subtilis (strain 168) [Reference proteome] [HAMAP]

Taxonomic identifier

224308 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus subtilis group › Bacillus subtilis › Bacillus subtilis subsp. subtilis

Protein attributes

Sequence length	254 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Dephosphorylates the phosphotyrosine-containing proteins YwqD, YwqF and Ssb. Ref.4
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Cofactor	Manganese.
Enzyme regulation	Inhibited by vanadate and sodium pyrophosphate. Not inhibited by sodium fluoride.
Sequence similarities	Belongs to the CpsB/CapC family.
Biophysicochemical properties	pH dependence: Optimally active at alkaline pHs. Activity increases with increasing pHs.

Ontologies

Keywords
Ligand	Manganese
Molecular function	Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	peptidyl-tyrosine dephosphorylation Inferred from electronic annotation. Source: GOC
Molecular_function	manganese ion binding Inferred from electronic annotation. Source: InterPro protein tyrosine phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 254

254

Tyrosine-protein phosphatase YwqE

PRO_0000057893

Experimental info

Mutagenesis

3

1

D → A: Large decrease in activity. Ref.3

Mutagenesis

5

1

H → A: Large decrease in activity. Ref.3

Mutagenesis

7

1

H → A: Large decrease in activity.

Mutagenesis

42

1

H → A: Large decrease in activity. Ref.3

Mutagenesis

136

1

H → A: Large decrease in activity. Ref.3

Mutagenesis

194

1

D → A: Large decrease in activity. Ref.3

Mutagenesis

196

1

H → A: Large decrease in activity. Ref.3

Secondary structure

1

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254

Helix Strand Turn

Details...

Beta strand

2 – 6

5

Beta strand

12 – 15

4

Helix

19 – 31

13

Beta strand

36 – 38

3

Beta strand

42 – 45

4

Helix

52 – 68

17

Beta strand

74 – 76

3

Beta strand

80 – 82

3

Helix

87 – 92

6

Helix

99 – 101

3

Beta strand

102 – 108

7

Helix

118 – 127

10

Beta strand

131 – 135

5

Helix

137 – 139

3

Helix

141 – 145

5

Helix

148 – 155

8

Beta strand

159 – 163

5

Helix

164 – 168

5

Turn

169 – 171

3

Helix

173 – 184

12

Beta strand

190 – 192

3

Beta strand

197 – 201

5

Helix

205 – 216

12

Helix

219 – 232

14

Sequences

	Sequence		Length	Mass (Da)
	P96717 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: E2625AE51E0E9A94	FASTA	254	28,958
	10 20 30 40 50 60 MIDIHCHILP AMDDGAGDSA DSIEMARAAV RQGIRTIIAT PHHNNGVYKN EPAAVREAAD 70 80 90 100 110 120 QLNKRLIKED IPLHVLPGQE IRIYGEVEQD LAKRQLLSLN DTKYILIEFP FDHVPRYAEQ 130 140 150 160 170 180 LFYDLQLKGY IPVIAHPERN REIRENPSLL YHLVEKGAAS QITSGSLAGI FGKQLKAFSL 190 200 210 220 230 240 RLVEANLIHF VASDAHNVKT RNFHTQEALY VLEKEFGSEL PYMLTENAEL LLRNQTIFRQ 250 PPQPVKRRKL FGFF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z92952 Genomic DNA. Translation: CAB07456.1.
AL009126 Genomic DNA. Translation: CAB15641.1.

PIR

H70066.

RefSeq

NP_391505.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3QY6	X-ray	1.80	A	1-254	[»]
3QY7	X-ray	1.62	A	1-254	[»]

ProteinModelPortal

P96717.

SMR

P96717. Positions 1-237.

ModBase

Search...

Protein-protein interaction databases

STRING

224308.BSU36240.

Protein family/group databases

PptaseDB

P3D0505166.

Proteomic databases

PaxDb

P96717.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB15641; CAB15641; BSU36240.

GeneID

936893.

KEGG

bsu:BSU36240.

PATRIC

18979268. VBIBacSub10457_3796.

Organism-specific databases

GenoList

BSU36240.

Phylogenomic databases

eggNOG

COG4464.

HOGENOM

HOG000007624.

KO

K01104.

OMA

MIDVHSH.

ProtClustDB

CLSK2460963.

Enzyme and pathway databases

BioCyc

BSUB:BSU36240-MONOMER.

SABIO-RK

P96717.

Family and domain databases

InterPro

IPR016667. Caps_polysacc_synth_CpsB/CapC.
IPR004013. PHP_C.
IPR016195. Pol/histidinol_Pase-like.
[Graphical view]

Pfam

PF02811. PHP. 1 hit.
[Graphical view]

PIRSF

PIRSF016557. Caps_synth_CpsB. 1 hit.

SUPFAM

SSF89550. PHP-like. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P96717.

Entry information

Entry name

YWQE_BACSU

Accession

Primary (citable) accession number: P96717

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 2003
Last sequence update:	May 1, 1997
Last modified:	May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program