PP2C-family Ser/Thr phosphatase - Mycobacterium tuberculosis

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P71588 (PSTP_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 76. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
PP2C-family Ser/Thr phosphatase
EC=3.1.3.16

Alternative name(s):
Mycobacterial Ser/Thr phosphatase
Short name=Mstp
Possible serine/threonine phosphatase Ppp

Gene names

Name:	pstP
Synonyms:	mstp, ppp
Ordered Locus Names:	Rv0018c, MT0021

Organism

Mycobacterium tuberculosis

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	514 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The only predicted protein phosphatase in M.tuberculosis, it dephosphorylates at least 5 protein kinases (pknA, pknB, pknD, pknE and pknF) and the penicillin-binding protein PBPA. Ref.3 Ref.4 Ref.5 Ref.6
Catalytic activity	A phosphoprotein + H₂O = a protein + phosphate. Ref.3 Ref.4
Cofactor	Bind 3 Mn²⁺ ions per subunit. Ref.3
Enzyme regulation	Inhibited partially by NaF and cyclosporine.
Subcellular location	Cell membrane; Single-pass membrane protein Potential. Note: May be localized to the outside of the cell.
Miscellaneous	Was identified as a high-confidence drug target.
Sequence similarities	Contains 1 PP2C-like domain.
Caution	It is uncertain whether Met-1 or Val-4 is the initiator.
Sequence caution	The sequence AAK44243.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Ligand	Manganese Metal-binding
Molecular function	Hydrolase Protein phosphatase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	negative regulation of DNA binding Inferred from direct assay. Source: MTBBASE negative regulation of protein kinase activity Inferred from direct assay. Source: MTBBASE positive regulation of catalytic activity Inferred from direct assay. Source: MTBBASE protein dephosphorylation Inferred from direct assay. Source: MTBBASE
Cellular component	integral to plasma membrane Inferred from direct assay. Source: MTBBASE
Molecular function	magnesium ion binding Inferred from direct assay. Source: MTBBASE manganese ion binding Inferred from direct assay Ref.8. Source: MTBBASE phosphoprotein phosphatase activity Inferred from direct assay. Source: MTBBASE phosphoserine phosphatase activity Inferred from direct assay Ref.3. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 514

514

PP2C-family Ser/Thr phosphatase

PRO_0000344805

Regions

Topological domain

1 – 302

302

Cytoplasmic Potential

Transmembrane

303 – 323

Helical; Potential

Topological domain

324 – 514

191

Extracellular Potential

Domain

9 – 231

223

PP2C-like

Compositional bias

422 – 506

Pro-rich

Sites

Metal binding

Manganese 1

Metal binding

Manganese 2

Metal binding

Manganese 1; via carbonyl oxygen

Metal binding

118

Manganese 3

Metal binding

160

Manganese 3; via carbonyl oxygen

Metal binding

191

Manganese 2

Metal binding

191

Manganese 3

Metal binding

229

Manganese 2

Experimental info

Mutagenesis

118

D → N: Decreases affinity for Mn3 by 4-fold, no effect on hydrolysis of p-nitrophenyl phosphate. Ref.8

Mutagenesis

160

S → A: No change in affinity for Mn3, no effect on hydrolysis of p-nitrophenyl phosphate. Ref.8

Sequence conflict

463

P → S in AAK44243. Ref.2

Secondary structure

514

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P71588 [UniParc].

Last modified July 1, 1997. Version 2.
Checksum: DD78F54D2FC19D95
Show »

FASTA

514

53,812

        10         20         30         40         50         60 
MARVTLVLRY AARSDRGLVR ANNEDSVYAG ARLLALADGM GGHAAGEVAS QLVIAALAHL 

        70         80         90        100        110        120 
DDDEPGGDLL AKLDAAVRAG NSAIAAQVEM EPDLEGMGTT LTAILFAGNR LGLVHIGDSR 

       130        140        150        160        170        180 
GYLLRDGELT QITKDDTFVQ TLVDEGRITP EEAHSHPQRS LIMRALTGHE VEPTLTMREA 

       190        200        210        220        230        240 
RAGDRYLLCS DGLSDPVSDE TILEALQIPE VAESAHRLIE LALRGGGPDN VTVVVADVVD 

       250        260        270        280        290        300 
YDYGQTQPIL AGAVSGDDDQ LTLPNTAAGR ASAISQRKEI VKRVPPQADT FSRPRWSGRR 

       310        320        330        340        350        360 
LAFVVALVTV LMTAGLLIGR AIIRSNYYVA DYAGSVSIMR GIQGSLLGMS LHQPYLMGCL 

       370        380        390        400        410        420 
SPRNELSQIS YGQSGGPLDC HLMKLEDLRP PERAQVRAGL PAGTLDDAIG QLRELAANSL 

       430        440        450        460        470        480 
LPPCPAPRAT SPPGRPAPPT TSETTEPNVT SSPASPSPTT SAPAPTGTTP AIPTSASPAA 

       490        500        510 
PASPPTPWPV TSSPTMAALP PPPPQPGIDC RAAA

« Hide

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. 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. 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]	"Phosphoprotein phosphatase of Mycobacterium tuberculosis dephosphorylates serine-threonine kinases PknA and PknB." Chopra P., Singh B., Singh R., Vohra R., Koul A., Meena L.S., Koduri H., Ghildiyal M., Deol P., Das T.K., Tyagi A.K., Singh Y. Biochem. Biophys. Res. Commun. 311:112-120(2003) [PubMed: 14575702] [Abstract] Cited for: ENZYMATIC ACTIVITY, COFACTOR, ENZYME INHIBITION, FUNCTION IN THE DEPHOSPHORYLATION OF PKNA AND PKNB. Strain: ATCC 25618 / H37Rv.
[4]	"PknB kinase activity is regulated by phosphorylation in two Thr residues and dephosphorylation by PstP, the cognate phospho-Ser/Thr phosphatase, in Mycobacterium tuberculosis." Boitel B., Ortiz-Lombardia M., Duran R., Pompeo F., Cole S.T., Cervenansky C., Alzari P.M. Mol. Microbiol. 49:1493-1508(2003) [PubMed: 12950916] [Abstract] Cited for: ENZYMATIC ACTIVITY, DIVALENT CATION-DEPENDENCE, FUNCTION IN THE DEPHOSPHORYLATION OF PKNB. Strain: ATCC 25618 / H37Rv.
[5]	"Conserved autophosphorylation pattern in activation loops and juxtamembrane regions of Mycobacterium tuberculosis Ser/Thr protein kinases." Duran R., Villarino A., Bellinzoni M., Wehenkel A., Fernandez P., Boitel B., Cole S.T., Alzari P.M., Cervenansky C. Biochem. Biophys. Res. Commun. 333:858-867(2005) [PubMed: 15967413] [Abstract] Cited for: FUNCTION IN THE DEPHOSPHORYLATION OF PKNB; PKND; PKNE AND PKNF. Strain: ATCC 25618 / H37Rv.
[6]	"The serine/threonine kinase PknB of Mycobacterium tuberculosis phosphorylates PBPA, a penicillin-binding protein required for cell division." Dasgupta A., Datta P., Kundu M., Basu J. Microbiology 152:493-504(2006) [PubMed: 16436437] [Abstract] Cited for: FUNCTION IN THE DEPHOSPHORYLATION OF PBPA. Strain: ATCC 25618 / H37Rv.
[7]	"targetTB: a target identification pipeline for Mycobacterium tuberculosis through an interactome, reactome and genome-scale structural analysis." Raman K., Yeturu K., Chandra N. BMC Syst. Biol. 2:109-109(2008) [PubMed: 19099550] [Abstract] Cited for: IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
[8]	"An alternate conformation and a third metal in PstP/Ppp, the M. tuberculosis PP2C-Family Ser/Thr protein phosphatase." Pullen K.E., Ng H.-L., Sung P.-Y., Good M.C., Smith S.M., Alber T. Structure 12:1947-1954(2004) [PubMed: 15530359] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 5-237, MUTAGENESIS OF ASP-118 AND SER-160. Strain: ATCC 25618 / H37Rv.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BX842572 Genomic DNA. Translation: CAB02438.1.
AE000516 Genomic DNA. Translation: AAK44243.1. Different initiation.

PIR

H70699.

RefSeq

NP_214532.1. NC_000962.2.
NP_334429.1. NC_002755.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TXO	X-ray	1.95	A/B	5-237	[»]
2CM1	X-ray	2.00	A	1-240	[»]

ProteinModelPortal

P71588.

SMR

P71588. Positions 5-238.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-59021N.

Protein family/group databases

PptaseDB

P3D0410141.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBMYCT00000003854; EBMYCP00000003854; EBMYCG00000003852.
EBMYCT00000070846; EBMYCP00000068905; EBMYCG00000070841.

GeneID

887070.
922470.

GenomeReviews

Gene locus MT0021 in contig AE000516_GR.
Gene locus Rv0018c in contig AL123456_GR.

KEGG

mtc:MT0021.
mtu:Rv0018c.

PATRIC

18121772. VBIMycTub22151_0022.

TIGR

MT0021.

Organism-specific databases

TubercuList

Rv0018c.

Phylogenomic databases

GeneTree

EBGT00050000014898.

HOGENOM

HBG688775.

OMA

PEDVSTH.

PhylomeDB

P71588.

ProtClustDB

CLSK790196.

Family and domain databases

InterPro

IPR001932. PP2C-like.
IPR015655. Protein_Pase_2C.
[Graphical view]

Gene3D

G3DSA:3.60.40.10. PP2C-related. 1 hit.

K01090.

PANTHER

PTHR13832. PP2C. 1 hit.

Pfam

PF00481. PP2C. 1 hit.
[Graphical view]

SMART

SM00331. PP2C_SIG. 1 hit.
SM00332. PP2Cc. 1 hit.
[Graphical view]

SUPFAM

SSF81606. PP2C-related. 1 hit.

ProtoNet

Search...

Entry information

Entry name

PSTP_MYCTU

Accession

Primary (citable) accession number: P71588
Secondary accession number(s): Q8VKT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 22, 2008
Last sequence update:	July 1, 1997
Last modified:	January 25, 2012
This is version 76 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents