PSTP_MYCTU
ID PSTP_MYCTU Reviewed; 514 AA.
AC P9WHW5; L0T2B3; P71588; Q8VKT2;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Serine/threonine protein phosphatase PstP {ECO:0000303|PubMed:27758870};
DE EC=3.1.3.16 {ECO:0000269|PubMed:12950916, ECO:0000269|PubMed:14575702, ECO:0000269|PubMed:15967413};
DE AltName: Full=Mycobacterial Ser/Thr phosphatase {ECO:0000303|PubMed:14575702};
DE Short=Mstp {ECO:0000303|PubMed:14575702};
DE AltName: Full=PP2C-family Ser/Thr phosphatase;
GN Name=pstP; Synonyms=mstp {ECO:0000303|PubMed:14575702}, ppp;
GN OrderedLocusNames=Rv0018c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION IN THE DEPHOSPHORYLATION OF PKNA AND PKNB, CATALYTIC ACTIVITY,
RP COFACTOR, AND ACTIVITY REGULATION.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=14575702; DOI=10.1016/j.bbrc.2003.09.173;
RA Chopra P., Singh B., Singh R., Vohra R., Koul A., Meena L.S., Koduri H.,
RA Ghildiyal M., Deol P., Das T.K., Tyagi A.K., Singh Y.;
RT "Phosphoprotein phosphatase of Mycobacterium tuberculosis dephosphorylates
RT serine-threonine kinases PknA and PknB.";
RL Biochem. Biophys. Res. Commun. 311:112-120(2003).
RN [3]
RP FUNCTION IN THE DEPHOSPHORYLATION OF PKNB, CATALYTIC ACTIVITY, AND DIVALENT
RP CATION-DEPENDENCE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12950916; DOI=10.1046/j.1365-2958.2003.03657.x;
RA Boitel B., Ortiz-Lombardia M., Duran R., Pompeo F., Cole S.T.,
RA Cervenansky C., Alzari P.M.;
RT "PknB kinase activity is regulated by phosphorylation in two Thr residues
RT and dephosphorylation by PstP, the cognate phospho-Ser/Thr phosphatase, in
RT Mycobacterium tuberculosis.";
RL Mol. Microbiol. 49:1493-1508(2003).
RN [4]
RP FUNCTION IN THE DEPHOSPHORYLATION OF PKNB; PKND; PKNE AND PKNF, AND
RP CATALYTIC ACTIVITY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15967413; DOI=10.1016/j.bbrc.2005.05.173;
RA Duran R., Villarino A., Bellinzoni M., Wehenkel A., Fernandez P.,
RA Boitel B., Cole S.T., Alzari P.M., Cervenansky C.;
RT "Conserved autophosphorylation pattern in activation loops and
RT juxtamembrane regions of Mycobacterium tuberculosis Ser/Thr protein
RT kinases.";
RL Biochem. Biophys. Res. Commun. 333:858-867(2005).
RN [5]
RP RETRACTED PAPER.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16436437; DOI=10.1099/mic.0.28630-0;
RA Dasgupta A., Datta P., Kundu M., Basu J.;
RT "The serine/threonine kinase PknB of Mycobacterium tuberculosis
RT phosphorylates PBPA, a penicillin-binding protein required for cell
RT division.";
RL Microbiology 152:493-504(2006).
RN [6]
RP RETRACTION NOTICE OF PUBMED:16436437.
RX PubMed=26231854; DOI=10.1099/mic.0.000110;
RA Dasgupta A., Datta P., Kundu M., Basu J.;
RL Microbiology 161:1537-1537(2015).
RN [7]
RP FUNCTION IN THE DEPHOSPHORYLATION OF PKNH AND EMBR.
RX PubMed=16817899; DOI=10.1111/j.1742-4658.2006.05289.x;
RA Sharma K., Gupta M., Krupa A., Srinivasan N., Singh Y.;
RT "EmbR, a regulatory protein with ATPase activity, is a substrate of
RT multiple serine/threonine kinases and phosphatase in Mycobacterium
RT tuberculosis.";
RL FEBS J. 273:2711-2721(2006).
RN [8]
RP FUNCTION IN THE DEPHOSPHORYLATION OF OPRA/RV0516C.
RX PubMed=17411339; DOI=10.1371/journal.ppat.0030049;
RA Greenstein A.E., MacGurn J.A., Baer C.E., Falick A.M., Cox J.S., Alber T.;
RT "M. tuberculosis Ser/Thr protein kinase D phosphorylates an anti-anti-sigma
RT factor homolog.";
RL PLoS Pathog. 3:E49-E49(2007).
RN [9]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [10]
RP FUNCTION IN THE DEPHOSPHORYLATION OF PAPA5.
RX PubMed=19826007; DOI=10.1074/jbc.m109.058834;
RA Gupta M., Sajid A., Arora G., Tandon V., Singh Y.;
RT "Forkhead-associated domain-containing protein Rv0019c and polyketide-
RT associated protein PapA5, from substrates of serine/threonine protein
RT kinase PknB to interacting proteins of Mycobacterium tuberculosis.";
RL J. Biol. Chem. 284:34723-34734(2009).
RN [11]
RP FUNCTION IN THE DEPHOSPHORYLATION OF PKNJ AND PYK.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20520732; DOI=10.1371/journal.pone.0010772;
RA Arora G., Sajid A., Gupta M., Bhaduri A., Kumar P., Basu-Modak S.,
RA Singh Y.;
RT "Understanding the role of PknJ in Mycobacterium tuberculosis: biochemical
RT characterization and identification of novel substrate pyruvate kinase A.";
RL PLoS ONE 5:E10772-E10772(2010).
RN [12]
RP FUNCTION IN THE DEPHOSPHORYLATION OF PKNA AND PKNB, ACTIVITY REGULATION,
RP PHOSPHORYLATION AT THR-137; THR-141; THR-174 AND THR-290, AND MUTAGENESIS
RP OF THR-5; ARG-20; ASP-38; THR-141 AND ASP-229.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21423706; DOI=10.1371/journal.pone.0017871;
RA Sajid A., Arora G., Gupta M., Upadhyay S., Nandicoori V.K., Singh Y.;
RT "Phosphorylation of Mycobacterium tuberculosis Ser/Thr phosphatase by PknA
RT and PknB.";
RL PLoS ONE 6:E17871-E17871(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [14]
RP FUNCTION IN VIRULENCE, DISRUPTION PHENOTYPE, AND OVEREXPRESSION.
RX PubMed=27758870; DOI=10.1074/jbc.m116.754531;
RA Sharma A.K., Arora D., Singh L.K., Gangwal A., Sajid A., Molle V.,
RA Singh Y., Nandicoori V.K.;
RT "Serine/threonine protein phosphatase PstP of Mycobacterium tuberculosis is
RT necessary for accurate cell division and survival of pathogen.";
RL J. Biol. Chem. 291:24215-24230(2016).
RN [15]
RP FUNCTION, INTERACTION WITH ETHR, AND PROTEOME MICROARRAY.
RX PubMed=31958639; DOI=10.1016/j.jprot.2020.103650;
RA Li K.K., Qu D.H., Zhang H.N., Chen F.Y., Xu L., Wang M.Y., Su H.Y.,
RA Tao S.C., Wu F.L.;
RT "Global discovery the PstP interactions using Mtb proteome microarray and
RT revealing novel connections with EthR.";
RL J. Proteomics 215:103650-103650(2020).
RN [16] {ECO:0007744|PDB:1TXO}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 5-237 IN COMPLEX WITH MANGANESE,
RP COFACTOR, AND MUTAGENESIS OF ASP-118 AND SER-160.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=15530359; DOI=10.1016/j.str.2004.09.008;
RA Pullen K.E., Ng H.-L., Sung P.-Y., Good M.C., Smith S.M., Alber T.;
RT "An alternate conformation and a third metal in PstP/Ppp, the M.
RT tuberculosis PP2C-Family Ser/Thr protein phosphatase.";
RL Structure 12:1947-1954(2004).
RN [17] {ECO:0007744|PDB:2CM1}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-240 IN COMPLEX WITH MANGANESE,
RP AND COFACTOR.
RX PubMed=17961594; DOI=10.1016/j.jmb.2007.09.076;
RA Wehenkel A., Bellinzoni M., Schaeffer F., Villarino A., Alzari P.M.;
RT "Structural and binding studies of the three-metal center in two
RT mycobacterial PPM Ser/Thr protein phosphatases.";
RL J. Mol. Biol. 374:890-898(2007).
CC -!- FUNCTION: Plays an important role in regulating cell division and
CC growth by reversible phosphorylation signaling (PubMed:14575702,
CC PubMed:12950916, PubMed:27758870). May play important roles in
CC regulating cellular metabolism and signaling pathways, which could
CC mediate the growth and development of the cell (PubMed:31958639). Plays
CC a role in establishing and maintaining infection (PubMed:27758870).
CC Dephosphorylates several proteins, including the kinases PknA, PknB,
CC PknD, PknE, PknF, PknH, PknJ and Pyk, the transcriptional regulatory
CC proteins EmbR and EthR, the osmosensory protein OprA and the
CC dimycocerosyl transferase PapA5 (PubMed:14575702, PubMed:12950916,
CC PubMed:15967413, PubMed:16817899, PubMed:17411339, PubMed:19826007,
CC PubMed:20520732, PubMed:21423706, PubMed:31958639). In vitro,
CC dephosphorylates the phosphorylated Ser/Thr residues of myelin basic
CC protein (MBP), histone and casein phosphorylated at Ser/Thr residues,
CC but fails to dephosphorylate phosphotyrosine residue of these
CC substrates (PubMed:14575702, PubMed:12950916).
CC {ECO:0000269|PubMed:12950916, ECO:0000269|PubMed:14575702,
CC ECO:0000269|PubMed:15967413, ECO:0000269|PubMed:16817899,
CC ECO:0000269|PubMed:17411339, ECO:0000269|PubMed:19826007,
CC ECO:0000269|PubMed:20520732, ECO:0000269|PubMed:21423706,
CC ECO:0000269|PubMed:27758870, ECO:0000269|PubMed:31958639}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:12950916, ECO:0000269|PubMed:14575702,
CC ECO:0000269|PubMed:15967413};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC Evidence={ECO:0000269|PubMed:12950916, ECO:0000269|PubMed:14575702,
CC ECO:0000269|PubMed:15967413};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:14575702, ECO:0000269|PubMed:15530359,
CC ECO:0000269|PubMed:17961594};
CC Note=Binds 3 Mn(2+) ions per subunit (PubMed:15530359). The third
CC manganese ion is unlikely to be involved in catalysis but contributes
CC instead to stabilize a flap segment, which is partially disordered in
CC the absence of bound metal (PubMed:17961594).
CC {ECO:0000269|PubMed:15530359, ECO:0000269|PubMed:17961594};
CC -!- ACTIVITY REGULATION: Activity is modulated by phosphorylation
CC (PubMed:21423706). Phosphorylated phosphatase is more active than its
CC unphosphorylated equivalent (PubMed:21423706). Inhibited partially by
CC NaF and cyclosporine (PubMed:14575702). Also inhibited by zinc ions and
CC inorganic phosphate (PubMed:21423706). {ECO:0000269|PubMed:14575702,
CC ECO:0000269|PubMed:21423706}.
CC -!- SUBUNIT: 78 interactors between PstP and Mtb proteins were identified
CC using Mtb proteome microarray, including proteins involved in diverse
CC aspects of cellular pathways and biological processes, which contain
CC cellular metabolic process, biosynthetic process, gene expression and
CC transcription regulation processes (PubMed:31958639). Interacts with
CC EthR and may interfere with its DNA binding activity (PubMed:31958639).
CC {ECO:0000269|PubMed:31958639}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- PTM: Phosphorylated on several threonine residues by PknA and PknB.
CC {ECO:0000269|PubMed:21423706}.
CC -!- DISRUPTION PHENOTYPE: Depletion of PstP compromises mycobacterial
CC growth and causes marginal elongation of cells. Depletion of PstP in
CC M.tuberculosis negatively impacts its survival in mice and decreases
CC the bacillary load even in an established infection.
CC {ECO:0000269|PubMed:27758870}.
CC -!- MISCELLANEOUS: Overexpression leads to elongated cells and partially
CC compromised survival. {ECO:0000269|PubMed:27758870}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC {ECO:0000269|PubMed:19099550}.
CC -!- CAUTION: It is uncertain whether Met-1 or Val-4 is the initiator.
CC {ECO:0000305}.
CC -!- CAUTION: Was reported to dephosphorylate the penicillin-binding protein
CC PBPA. However, this publication has been retracted because the
CC published versions of some figures were modified prior to publication.
CC {ECO:0000305|PubMed:16436437, ECO:0000305|PubMed:26231854}.
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DR EMBL; AL123456; CCP42740.1; -; Genomic_DNA.
DR PIR; H70699; H70699.
DR RefSeq; NP_214532.1; NC_000962.3.
DR RefSeq; WP_010886062.1; NC_000962.3.
DR PDB; 1TXO; X-ray; 1.95 A; A/B=5-237.
DR PDB; 2CM1; X-ray; 2.00 A; A=1-240.
DR PDBsum; 1TXO; -.
DR PDBsum; 2CM1; -.
DR AlphaFoldDB; P9WHW5; -.
DR SMR; P9WHW5; -.
DR IntAct; P9WHW5; 2.
DR STRING; 83332.Rv0018c; -.
DR PaxDb; P9WHW5; -.
DR GeneID; 887070; -.
DR KEGG; mtu:Rv0018c; -.
DR PATRIC; fig|83332.111.peg.22; -.
DR TubercuList; Rv0018c; -.
DR eggNOG; COG0631; Bacteria.
DR eggNOG; COG3266; Bacteria.
DR OMA; ITQDHTW; -.
DR PhylomeDB; P9WHW5; -.
DR BRENDA; 3.1.3.16; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IDA:MTBBASE.
DR GO; GO:0005887; C:integral component of plasma membrane; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0030145; F:manganese ion binding; IDA:MTBBASE.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IDA:MTBBASE.
DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IDA:GO_Central.
DR GO; GO:0043086; P:negative regulation of catalytic activity; IDA:MTBBASE.
DR GO; GO:0043392; P:negative regulation of DNA binding; IDA:MTBBASE.
DR GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:MTBBASE.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IDA:MTBBASE.
DR GO; GO:0006470; P:protein dephosphorylation; IDA:MTBBASE.
DR CDD; cd00143; PP2Cc; 1.
DR Gene3D; 3.60.40.10; -; 1.
DR InterPro; IPR015655; PP2C.
DR InterPro; IPR036457; PPM-type_dom_sf.
DR InterPro; IPR001932; PPM-type_phosphatase_dom.
DR PANTHER; PTHR13832; PTHR13832; 1.
DR SMART; SM00331; PP2C_SIG; 1.
DR SMART; SM00332; PP2Cc; 1.
DR SUPFAM; SSF81606; SSF81606; 1.
DR PROSITE; PS51746; PPM_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Hydrolase; Manganese; Membrane; Metal-binding;
KW Phosphoprotein; Protein phosphatase; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..514
FT /note="Serine/threonine protein phosphatase PstP"
FT /id="PRO_0000344805"
FT TOPO_DOM 1..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..514
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 9..238
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT REGION 420..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..440
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 477..508
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15530359,
FT ECO:0000269|PubMed:17961594, ECO:0007744|PDB:1TXO,
FT ECO:0007744|PDB:2CM1"
FT BINDING 38
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15530359,
FT ECO:0000269|PubMed:17961594, ECO:0007744|PDB:1TXO,
FT ECO:0007744|PDB:2CM1"
FT BINDING 39
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:15530359,
FT ECO:0000269|PubMed:17961594, ECO:0007744|PDB:1TXO,
FT ECO:0007744|PDB:2CM1"
FT BINDING 118
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15530359,
FT ECO:0007744|PDB:1TXO"
FT BINDING 160
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15530359,
FT ECO:0007744|PDB:1TXO"
FT BINDING 191
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15530359,
FT ECO:0000269|PubMed:17961594, ECO:0007744|PDB:1TXO,
FT ECO:0007744|PDB:2CM1"
FT BINDING 191
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:15530359,
FT ECO:0007744|PDB:1TXO"
FT BINDING 229
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:15530359,
FT ECO:0000269|PubMed:17961594, ECO:0007744|PDB:1TXO,
FT ECO:0007744|PDB:2CM1"
FT MOD_RES 137
FT /note="Phosphothreonine; by PknA and PknB"
FT /evidence="ECO:0000269|PubMed:21423706"
FT MOD_RES 141
FT /note="Phosphothreonine; by PknB"
FT /evidence="ECO:0000269|PubMed:21423706"
FT MOD_RES 174
FT /note="Phosphothreonine; by PknA and PknB"
FT /evidence="ECO:0000269|PubMed:21423706"
FT MOD_RES 290
FT /note="Phosphothreonine; by PknB"
FT /evidence="ECO:0000269|PubMed:21423706"
FT MUTAGEN 5
FT /note="T->A: No change in activity."
FT /evidence="ECO:0000269|PubMed:21423706"
FT MUTAGEN 20
FT /note="R->G: 60% loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:21423706"
FT MUTAGEN 38
FT /note="D->G: 90% loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:21423706"
FT MUTAGEN 118
FT /note="D->N: Decreases affinity for Mn3 by 4-fold, no
FT effect on hydrolysis of p-nitrophenyl phosphate."
FT /evidence="ECO:0000269|PubMed:15530359"
FT MUTAGEN 141
FT /note="T->E: No change in activity."
FT /evidence="ECO:0000269|PubMed:21423706"
FT MUTAGEN 160
FT /note="S->A: No change in affinity for Mn3, no effect on
FT hydrolysis of p-nitrophenyl phosphate."
FT /evidence="ECO:0000269|PubMed:15530359"
FT MUTAGEN 229
FT /note="D->G: 90% loss of phosphatase activity."
FT /evidence="ECO:0000269|PubMed:21423706"
FT STRAND 7..15
FT /evidence="ECO:0007829|PDB:1TXO"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:1TXO"
FT STRAND 31..40
FT /evidence="ECO:0007829|PDB:1TXO"
FT TURN 42..44
FT /evidence="ECO:0007829|PDB:1TXO"
FT HELIX 45..57
FT /evidence="ECO:0007829|PDB:1TXO"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:1TXO"
FT HELIX 69..90
FT /evidence="ECO:0007829|PDB:1TXO"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:1TXO"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:1TXO"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:1TXO"
FT STRAND 120..125
FT /evidence="ECO:0007829|PDB:1TXO"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:1TXO"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:1TXO"
FT HELIX 152..155
FT /evidence="ECO:0007829|PDB:1TXO"
FT TURN 157..160
FT /evidence="ECO:0007829|PDB:1TXO"
FT STRAND 166..169
FT /evidence="ECO:0007829|PDB:1TXO"
FT STRAND 174..179
FT /evidence="ECO:0007829|PDB:1TXO"
FT STRAND 185..189
FT /evidence="ECO:0007829|PDB:1TXO"
FT HELIX 191..194
FT /evidence="ECO:0007829|PDB:1TXO"
FT HELIX 199..206
FT /evidence="ECO:0007829|PDB:1TXO"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:1TXO"
FT HELIX 211..224
FT /evidence="ECO:0007829|PDB:1TXO"
FT STRAND 231..239
FT /evidence="ECO:0007829|PDB:1TXO"
SQ 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
