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PP2C-family Ser/Thr phosphatase (EC 3.1.3.16) (Mycobacterial Ser/Thr phosphatase) (Mstp) (Possible serine/threonine phosphatase Ppp)

 PSTP_MYCTU              Reviewed;         514 AA.
P9WHW5; L0T2B3; P71588; Q8VKT2;
16-APR-2014, integrated into UniProtKB/Swiss-Prot.
16-APR-2014, sequence version 1.
12-SEP-2018, entry version 24.
RecName: Full=PP2C-family Ser/Thr phosphatase;
EC=3.1.3.16;
AltName: Full=Mycobacterial Ser/Thr phosphatase;
Short=Mstp;
AltName: Full=Possible serine/threonine phosphatase Ppp;
Name=pstP; Synonyms=mstp, ppp; OrderedLocusNames=Rv0018c;
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium; Mycobacterium tuberculosis complex.
NCBI_TaxID=83332;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 25618 / H37Rv;
PubMed=9634230; DOI=10.1038/31159;
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.;
"Deciphering the biology of Mycobacterium tuberculosis from the
complete genome sequence.";
Nature 393:537-544(1998).
[2]
ENZYMATIC ACTIVITY, COFACTOR, ENZYME INHIBITION, AND FUNCTION IN THE
DEPHOSPHORYLATION OF PKNA AND PKNB.
STRAIN=ATCC 25618 / H37Rv;
PubMed=14575702; DOI=10.1016/j.bbrc.2003.09.173;
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.;
"Phosphoprotein phosphatase of Mycobacterium tuberculosis
dephosphorylates serine-threonine kinases PknA and PknB.";
Biochem. Biophys. Res. Commun. 311:112-120(2003).
[3]
ENZYMATIC ACTIVITY, DIVALENT CATION-DEPENDENCE, AND FUNCTION IN THE
DEPHOSPHORYLATION OF PKNB.
STRAIN=ATCC 25618 / H37Rv;
PubMed=12950916; DOI=10.1046/j.1365-2958.2003.03657.x;
Boitel B., Ortiz-Lombardia M., Duran R., Pompeo F., Cole S.T.,
Cervenansky C., Alzari P.M.;
"PknB kinase activity is regulated by phosphorylation in two Thr
residues and dephosphorylation by PstP, the cognate phospho-Ser/Thr
phosphatase, in Mycobacterium tuberculosis.";
Mol. Microbiol. 49:1493-1508(2003).
[4]
FUNCTION IN THE DEPHOSPHORYLATION OF PKNB; PKND; PKNE AND PKNF.
STRAIN=ATCC 25618 / H37Rv;
PubMed=15967413; DOI=10.1016/j.bbrc.2005.05.173;
Duran R., Villarino A., Bellinzoni M., Wehenkel A., Fernandez P.,
Boitel B., Cole S.T., Alzari P.M., Cervenansky C.;
"Conserved autophosphorylation pattern in activation loops and
juxtamembrane regions of Mycobacterium tuberculosis Ser/Thr protein
kinases.";
Biochem. Biophys. Res. Commun. 333:858-867(2005).
[5]
FUNCTION IN THE DEPHOSPHORYLATION OF PBPA.
STRAIN=ATCC 25618 / H37Rv;
PubMed=16436437; DOI=10.1099/mic.0.28630-0;
Dasgupta A., Datta P., Kundu M., Basu J.;
"The serine/threonine kinase PknB of Mycobacterium tuberculosis
phosphorylates PBPA, a penicillin-binding protein required for cell
division.";
Microbiology 152:493-504(2006).
[6]
IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
PubMed=19099550; DOI=10.1186/1752-0509-2-109;
Raman K., Yeturu K., Chandra N.;
"targetTB: a target identification pipeline for Mycobacterium
tuberculosis through an interactome, reactome and genome-scale
structural analysis.";
BMC Syst. Biol. 2:109-109(2008).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ATCC 25618 / H37Rv;
PubMed=21969609; DOI=10.1074/mcp.M111.011627;
Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B.,
Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
Dash D., Pandey A.;
"Proteogenomic analysis of Mycobacterium tuberculosis by high
resolution mass spectrometry.";
Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
[8]
X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 5-237, AND MUTAGENESIS OF
ASP-118 AND SER-160.
STRAIN=ATCC 25618 / H37Rv;
PubMed=15530359; DOI=10.1016/j.str.2004.09.008;
Pullen K.E., Ng H.-L., Sung P.-Y., Good M.C., Smith S.M., Alber T.;
"An alternate conformation and a third metal in PstP/Ppp, the M.
tuberculosis PP2C-Family Ser/Thr protein phosphatase.";
Structure 12:1947-1954(2004).
-!- 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. {ECO:0000269|PubMed:12950916,
ECO:0000269|PubMed:14575702, ECO:0000269|PubMed:15967413,
ECO:0000269|PubMed:16436437}.
-!- CATALYTIC ACTIVITY: [a protein]-serine/threonine phosphate + H(2)O
= [a protein]-serine/threonine + phosphate.
{ECO:0000269|PubMed:12950916, ECO:0000269|PubMed:14575702}.
-!- COFACTOR:
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:14575702};
Note=Binds 3 Mn(2+) ions per subunit.
{ECO:0000269|PubMed:14575702};
-!- ACTIVITY REGULATION: Inhibited partially by NaF and cyclosporine.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
membrane protein {ECO:0000305}. Note=May be localized to the
outside of the cell.
-!- MISCELLANEOUS: Was identified as a high-confidence drug target.
-!- CAUTION: It is uncertain whether Met-1 or Val-4 is the initiator.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AL123456; CCP42740.1; -; Genomic_DNA.
PIR; H70699; H70699.
RefSeq; NP_214532.1; NC_000962.3.
RefSeq; WP_010886062.1; NZ_KK339370.1.
PDB; 1TXO; X-ray; 1.95 A; A/B=5-237.
PDB; 2CM1; X-ray; 2.00 A; A=1-240.
PDBsum; 1TXO; -.
PDBsum; 2CM1; -.
ProteinModelPortal; P9WHW5; -.
SMR; P9WHW5; -.
IntAct; P9WHW5; 2.
STRING; 83332.Rv0018c; -.
PaxDb; P9WHW5; -.
EnsemblBacteria; CCP42740; CCP42740; Rv0018c.
GeneID; 887070; -.
KEGG; mtu:Rv0018c; -.
KEGG; mtv:RVBD_0018c; -.
PATRIC; fig|83332.111.peg.22; -.
TubercuList; Rv0018c; -.
eggNOG; ENOG4108ZF3; Bacteria.
eggNOG; COG0631; LUCA.
KO; K20074; -.
OMA; ITQDHTW; -.
PhylomeDB; P9WHW5; -.
Proteomes; UP000001584; Chromosome.
GO; GO:0005618; C:cell wall; IDA:MTBBASE.
GO; GO:0016021; C:integral component of membrane; IDA:MTBBASE.
GO; GO:0005887; C:integral component of plasma membrane; IDA:MTBBASE.
GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
GO; GO:0030145; F:manganese ion binding; IDA:MTBBASE.
GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:MTBBASE.
GO; GO:0004647; F:phosphoserine phosphatase activity; IDA:MTBBASE.
GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
GO; GO:0043086; P:negative regulation of catalytic activity; IDA:MTBBASE.
GO; GO:0043392; P:negative regulation of DNA binding; IDA:MTBBASE.
GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:MTBBASE.
GO; GO:0043085; P:positive regulation of catalytic activity; IDA:MTBBASE.
GO; GO:0006470; P:protein dephosphorylation; IDA:MTBBASE.
CDD; cd00143; PP2Cc; 1.
Gene3D; 3.60.40.10; -; 1.
InterPro; IPR015655; PP2C.
InterPro; IPR036457; PPM-type_dom_sf.
InterPro; IPR001932; PPM-type_phosphatase_dom.
PANTHER; PTHR13832; PTHR13832; 1.
SMART; SM00331; PP2C_SIG; 1.
SMART; SM00332; PP2Cc; 1.
SUPFAM; SSF81606; SSF81606; 1.
PROSITE; PS51746; PPM_2; 1.
1: Evidence at protein level;
3D-structure; Cell membrane; Complete proteome; Hydrolase; Manganese;
Membrane; Metal-binding; Protein phosphatase; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 514 PP2C-family Ser/Thr phosphatase.
/FTId=PRO_0000344805.
TOPO_DOM 1 302 Cytoplasmic. {ECO:0000255}.
TRANSMEM 303 323 Helical. {ECO:0000255}.
TOPO_DOM 324 514 Extracellular. {ECO:0000255}.
DOMAIN 9 238 PPM-type phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU01082}.
COMPBIAS 422 506 Pro-rich.
METAL 38 38 Manganese 1.
METAL 38 38 Manganese 2.
METAL 39 39 Manganese 1; via carbonyl oxygen.
METAL 118 118 Manganese 3.
METAL 160 160 Manganese 3; via carbonyl oxygen.
METAL 191 191 Manganese 2.
METAL 191 191 Manganese 3.
METAL 229 229 Manganese 2.
MUTAGEN 118 118 D->N: Decreases affinity for Mn3 by 4-
fold, no effect on hydrolysis of p-
nitrophenyl phosphate.
{ECO:0000269|PubMed:15530359}.
MUTAGEN 160 160 S->A: No change in affinity for Mn3, no
effect on hydrolysis of p-nitrophenyl
phosphate. {ECO:0000269|PubMed:15530359}.
STRAND 7 15 {ECO:0000244|PDB:1TXO}.
STRAND 25 29 {ECO:0000244|PDB:1TXO}.
STRAND 31 40 {ECO:0000244|PDB:1TXO}.
TURN 42 44 {ECO:0000244|PDB:1TXO}.
HELIX 45 57 {ECO:0000244|PDB:1TXO}.
HELIX 58 61 {ECO:0000244|PDB:1TXO}.
HELIX 69 90 {ECO:0000244|PDB:1TXO}.
HELIX 92 94 {ECO:0000244|PDB:1TXO}.
STRAND 101 107 {ECO:0000244|PDB:1TXO}.
STRAND 110 118 {ECO:0000244|PDB:1TXO}.
STRAND 120 125 {ECO:0000244|PDB:1TXO}.
STRAND 128 131 {ECO:0000244|PDB:1TXO}.
HELIX 138 144 {ECO:0000244|PDB:1TXO}.
HELIX 152 155 {ECO:0000244|PDB:1TXO}.
TURN 157 160 {ECO:0000244|PDB:1TXO}.
STRAND 166 169 {ECO:0000244|PDB:1TXO}.
STRAND 174 179 {ECO:0000244|PDB:1TXO}.
STRAND 185 189 {ECO:0000244|PDB:1TXO}.
HELIX 191 194 {ECO:0000244|PDB:1TXO}.
HELIX 199 206 {ECO:0000244|PDB:1TXO}.
STRAND 208 210 {ECO:0000244|PDB:1TXO}.
HELIX 211 224 {ECO:0000244|PDB:1TXO}.
STRAND 231 239 {ECO:0000244|PDB:1TXO}.
SEQUENCE 514 AA; 53812 MW; DD78F54D2FC19D95 CRC64;
MARVTLVLRY AARSDRGLVR ANNEDSVYAG ARLLALADGM GGHAAGEVAS QLVIAALAHL
DDDEPGGDLL AKLDAAVRAG NSAIAAQVEM EPDLEGMGTT LTAILFAGNR LGLVHIGDSR
GYLLRDGELT QITKDDTFVQ TLVDEGRITP EEAHSHPQRS LIMRALTGHE VEPTLTMREA
RAGDRYLLCS DGLSDPVSDE TILEALQIPE VAESAHRLIE LALRGGGPDN VTVVVADVVD
YDYGQTQPIL AGAVSGDDDQ LTLPNTAAGR ASAISQRKEI VKRVPPQADT FSRPRWSGRR
LAFVVALVTV LMTAGLLIGR AIIRSNYYVA DYAGSVSIMR GIQGSLLGMS LHQPYLMGCL
SPRNELSQIS YGQSGGPLDC HLMKLEDLRP PERAQVRAGL PAGTLDDAIG QLRELAANSL
LPPCPAPRAT SPPGRPAPPT TSETTEPNVT SSPASPSPTT SAPAPTGTTP AIPTSASPAA
PASPPTPWPV TSSPTMAALP PPPPQPGIDC RAAA


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