P39155 (YWLE_BACSU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Low molecular weight protein-tyrosine-phosphatase YwlE
Short name=LMPTP
EC=3.1.3.48

Gene names

Name:	ywlE
Ordered Locus Names:	BSU36930
ORF Names:	ipc-31d

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	150 AA.
Sequence status	Complete.
Protein existence	Evidence 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, sodium pyrophosphate and N-ethylmaleimide, while the addition of Mg2+, Ca2+ or Fe3+ ions has minimal effect. Inhibited in a competitive manner by vanadate. Ref.3
Sequence similarities	Belongs to the low molecular weight phosphotyrosine protein phosphatase family.
Biophysicochemical properties	Kinetic parameters: KM=0.157 mM for p-nitrophenyl-phosphate (at 37 degrees Celsius) Ref.3 Ref.4 KM=28 mM for p-nitrophenyl-phosphate (at 55 degrees Celsius) pH dependence: Optimum pH is 5.5.

Ontologies

Keywords
Domain	Coiled coil
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	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 – 150

150

Low molecular weight protein-tyrosine-phosphatase YwlE

PRO_0000046579

Regions

Coiled coil

121 – 150

30

Potential

Sites

Active site

7

1

Nucleophile

Active site

13

1

Active site

118

1

Proton donor

Experimental info

Mutagenesis

7

1

C → S: Completely abolishes the tyrosine-phosphatase activity. Ref.3

Mutagenesis

13

1

R → K: Completely abolishes the tyrosine-phosphatase activity. Ref.3

Mutagenesis

118

1

D → A: Completely abolishes the tyrosine-phosphatase activity. Ref.3

Secondary structure

1

.

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150

Helix Strand Turn

Details...

Beta strand

1 – 12

12

Helix

13 – 28

16

Beta strand

32 – 38

7

Helix

49 – 57

9

Helix

71 – 76

6

Beta strand

78 – 84

7

Helix

85 – 94

10

Helix

96 – 101

6

Beta strand

102 – 104

3

Helix

105 – 110

6

Beta strand

111 – 113

3

Helix

124 – 145

22

Turn

146 – 148

3

Sequences

	Sequence		Length	Mass (Da)
	P39155 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: E1BD5EA5231DED2C	FASTA	150	16,785
	10 20 30 40 50 60 MDIIFVCTGN TCRSPMAEAL FKSIAEREGL NVNVRSAGVF ASPNGKATPH AVEALFEKHI 70 80 90 100 110 120 ALNHVSSPLT EELMESADLV LAMTHQHKQI IASQFGRYRD KVFTLKEYVT GSHGDVLDPF 130 140 150 GGSIDIYKQT RDELEELLRQ LAKQLKKDRR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two genes encoding uracil phosphoribosyltransferase are present in Bacillus subtilis." Martinussen J., Glaser P., Andersen P.S., Saxild H.H. J. Bacteriol. 177:271-274(1995) [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]	"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-7; ARG-13 AND ASP-118, CHARACTERIZATION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: 168 / JH642.
[4]	"Solution structure of a low-molecular-weight protein tyrosine phosphatase from Bacillus subtilis." Xu H., Xia B., Jin C. J. Bacteriol. 188:1509-1517(2006) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-150, BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z38002 Genomic DNA. Translation: CAA86107.1.
AL009126 Genomic DNA. Translation: CAB15710.1.

PIR

S49360. I40479.

RefSeq

NP_391574.1. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZGG	NMR	-	A	1-150	[»]
4ETI	X-ray	1.80	A	1-150	[»]
4ETN	X-ray	1.10	A	1-150	[»]

ProteinModelPortal

P39155.

SMR

P39155. Positions 1-150.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-7148489.

STRING

224308.BSU36930.

Protein family/group databases

PptaseDB

P3D0507170.

Proteomic databases

PaxDb

P39155.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAB15710; CAB15710; BSU36930.

GeneID

937021.

KEGG

bsu:BSU36930.

PATRIC

18979420. VBIBacSub10457_3872.

Organism-specific databases

GenoList

BSU36930.

Phylogenomic databases

eggNOG

COG0394.

HOGENOM

HOG000273091.

KO

K01104.

OMA

SAFFPQK.

ProtClustDB

CLSK888045.

Enzyme and pathway databases

BioCyc

BSUB:BSU36930-MONOMER.

SABIO-RK

P39155.

Family and domain databases

InterPro

IPR023485. Ptyr_pPase_SF.
IPR000106. Tyr_phospatase/Ars_reductase.
IPR017867. Tyr_phospatase_low_mol_wt.
[Graphical view]

PANTHER

PTHR11717. PTHR11717. 1 hit.

Pfam

PF01451. LMWPc. 1 hit.
[Graphical view]

PRINTS

PR00719. LMWPTPASE.

SMART

SM00226. LMWPc. 1 hit.
[Graphical view]

SUPFAM

SSF52788. Tyr_Pase_low_mol_wt. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P39155.

Entry information

Entry name

YWLE_BACSU

Accession

Primary (citable) accession number: P39155

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 1, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program