P65716 (PTPA_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Probable low molecular weight protein-tyrosine-phosphatase
Short name=PTPase
EC=3.1.3.48

Gene names

Name:	ptpA
Ordered Locus Names:	Rv2234, MT2293
ORF Names:	MTCY427.15

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	163 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Mediates host-pathogen interaction and interferes with vesicular trafficking in the infected macrophage. Inhibits host phagolysosomal fusion in M.tuberculosis-infected macrophages to promote bacteria survival. Dephosphorylates host VPS33B protein, which induces a block of the host phagosome maturation within macrophage cells. Acts on tyrosine phosphorylated proteins, low-MW aryl phosphates and natural and synthetic acyl phosphates. Ref.3
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subunit structure	Interacts with the host VPS33B; interaction occurs in M. tuberculosis-infected macrophages. Ref.3
Subcellular location	Host endosome. Host cytoplasm. Note: Translocates into the host cytosol by crossing the host phagosome membrane during human macrophage infection. Colocalizes with host VPS33B in macrophage cytosol and associates with phagosomes. Ref.3
Sequence similarities	Belongs to the low molecular weight phosphotyrosine protein phosphatase family.

Ontologies

Keywords
Biological process	Virulence
Cellular component	Host cytoplasm Host endosome
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	modification by symbiont of host morphology or physiology via secreted substance Inferred from mutant phenotype. Source: MTBBASE negative regulation by symbiont of host cell-mediated immune response Inferred from experiment Ref.3. Source: MTBBASE pathogenesis Inferred from mutant phenotype Ref.3. Source: MTBBASE
Cellular component	host cell endosome Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: MTBBASE
Molecular function	protein binding Inferred from physical interaction Ref.3. Source: MTBBASE protein tyrosine phosphatase activity Inferred from direct assay. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 163

163

Probable low molecular weight protein-tyrosine-phosphatase

PRO_0000046567

Sites

Active site

11

1

Nucleophile By similarity

Active site

17

1

By similarity

Active site

126

1

Proton donor By similarity

Experimental info

Mutagenesis

11

1

C → A: Loss of phosphatase activity. Inhibits its dephosphorylation activity on human VPS33B. Reduces its effect on phagolysosome fusion in infected macrophages. Ref.3

Mutagenesis

17

1

R → A: Loss of phosphatase activity. Inhibits its dephosphorylation activity on human VPS33B. Ref.3

Mutagenesis

126

1

D → A: Loss of phosphatase activity. Inhibits its dephosphorylation activity on human VPS33B. Reduces its effect on phagolysosome fusion in infected macrophages. Ref.3

Secondary structure

1

.

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163

Helix Strand Turn

Details...

Beta strand

5 – 16

12

Helix

17 – 31

15

Turn

35 – 37

3

Beta strand

38 – 46

9

Turn

48 – 51

4

Helix

56 – 64

9

Helix

78 – 81

4

Beta strand

83 – 90

8

Helix

91 – 99

9

Helix

104 – 106

3

Beta strand

107 – 109

3

Helix

110 – 113

4

Helix

132 – 158

27

Sequences

	Sequence		Length	Mass (Da)
	P65716 [UniParc]. Last modified October 11, 2004. Version 1. Checksum: 9D1CF0DB24CA8E27	FASTA	163	17,892
	10 20 30 40 50 60 MSDPLHVTFV CTGNICRSPM AEKMFAQQLR HRGLGDAVRV TSAGTGNWHV GSCADERAAG 70 80 90 100 110 120 VLRAHGYPTD HRAAQVGTEH LAADLLVALD RNHARLLRQL GVEAARVRML RSFDPRSGTH 130 140 150 160 ALDVEDPYYG DHSDFEEVFA VIESALPGLH DWVDERLARN GPS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed: 9634230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed: 12218036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Mycobacterium tuberculosis virulence is mediated by PtpA dephosphorylation of human vacuolar protein sorting 33B." Bach H., Papavinasasundaram K.G., Wong D., Hmama Z., Av-Gay Y. Cell Host Microbe 3:316-322(2008) [PubMed: 18474358] [Abstract] Cited for: FUNCTION, INTERACTION WITH THE HUMAN VPS33B, MUTAGENESIS OF CYS-11; ARG-17 AND ASP-126, SUBCELLULAR LOCATION. Strain: ATCC 25618 / H37Rv.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX842579 Genomic DNA. Translation: CAA94656.1.
AE000516 Genomic DNA. Translation: AAK46577.1.

PIR

F70777.

RefSeq

NP_216750.1. NC_000962.2.
NP_336763.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U2P	X-ray	1.90	A	1-163	[»]
1U2Q	X-ray	2.50	A	1-163	[»]
1ZOJ	model	-	A	1-163	[»]

ProteinModelPortal

P65716.

SMR

P65716. Positions 4-159.

ModBase

Search...

Protein family/group databases

PptaseDB

P3D0410139.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000003929; EBMYCP00000003929; EBMYCG00000003927.
EBMYCT00000072860; EBMYCP00000070919; EBMYCG00000072855.

GeneID

887373.
924133.

GenomeReviews

Gene locus MT2293 in contig AE000516_GR.
Gene locus Rv2234 in contig AL123456_GR.

KEGG

mtc:MT2293.
mtu:Rv2234.

PATRIC

18126791. VBIMycTub22151_2507.

TIGR

MT2293.

Organism-specific databases

TubercuList

Rv2234.

Phylogenomic databases

GeneTree

EBGT00050000015868.

HOGENOM

HBG730979.

OMA

EDPWYGG.

PhylomeDB

P65716.

ProtClustDB

CLSK791711.

Family and domain databases

InterPro

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

KO

K01104.

PANTHER

PTHR11717. Low_mwt_PTPase. 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...

Entry information

Entry name

PTPA_MYCTU

Accession

Primary (citable) accession number: P65716
Secondary accession number(s): Q10507

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 11, 2004
Last sequence update:	October 11, 2004
Last modified:	January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program