PP2C-family Ser/Thr phosphatase - Mycobacterium tuberculosis

Contribute

Send feedback

Read comments (?) or add your own

P71588 (PSTP_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 88. History...

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

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

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 [Reference proteome] [HAMAP]

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	Binds 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 PubMed 16817899. Source: MTBBASE negative regulation of protein kinase activity Inferred from direct assay PubMed 10200974. Source: MTBBASE positive regulation of catalytic activity Inferred from direct assay PubMed 16873379. Source: MTBBASE protein dephosphorylation Inferred from direct assay PubMed 10200974. Source: MTBBASE
Cellular_component	cell wall Inferred from direct assay PubMed 20825248. Source: MTBBASE integral to plasma membrane Inferred from direct assay PubMed 15952732. Source: MTBBASE
Molecular_function	magnesium ion binding Inferred from direct assay PubMed 10200974. Source: MTBBASE manganese ion binding Inferred from direct assay PubMed 10200974 Ref.8. Source: MTBBASE phosphoprotein phosphatase activity Inferred from direct assay PubMed 10200974 PubMed 16817899 PubMed 16873379 PubMed 17411339 PubMed 19826007. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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.
AL123456 Genomic DNA. Translation: CCP42740.1.

PIR

H70699.

RefSeq

NP_214532.1. NC_000962.3.
NP_334429.1. NC_002755.2.
YP_006513332.1. NC_018143.1.

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.

STRING

83332.Rv0018c.

Protein family/group databases

PptaseDB

P3D0410141.

Proteomic databases

PRIDE

P71588.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAK44243; AAK44243; MT0021.

GeneID

13315995.
887070.
922470.

KEGG

mtc:MT0021.
mtu:Rv0018c.
mtv:RVBD_0018c.

PATRIC

18121772. VBIMycTub22151_0022.

Organism-specific databases

TubercuList

Rv0018c.

Phylogenomic databases

eggNOG

COG0631.

HOGENOM

HOG000235782.

K01090.

OMA

PEDVSTH.

ProtClustDB

CLSK790196.

Family and domain databases

Gene3D

3.60.40.10. 1 hit.

InterPro

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

PANTHER

PTHR13832. PTHR13832. 1 hit.

SMART

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

SUPFAM

SSF81606. PP2C-related. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P71588.

Entry information

Entry name

PSTP_MYCTU

Accession

Primary (citable) accession number: P71588
Secondary accession number(s): L0T2B3, Q8VKT2

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 22, 2008
Last sequence update:	July 1, 1997
Last modified:	May 1, 2013
This is version 88 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

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh

Mycobacterium tuberculosis strains ATCC 25618 / H37Rv and CDC 1551 / Oshkosh: entries and gene names

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

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Other

Entry information

Relevant documents