PHPP_STREE
ID PHPP_STREE Reviewed; 246 AA.
AC Q8KY51;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Protein phosphatase PhpP;
DE EC=3.1.3.16;
DE AltName: Full=PP2C-type phosphatase;
DE AltName: Full=Ser/Thr phosphoprotein phosphatase;
DE Short=STPP;
GN Name=phpP;
OS Streptococcus pneumoniae.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1313;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Rx / Cp1015;
RA Echenique J.R., Trombe M.C.;
RT "A serine/threonine kinase involved in competence regulation.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, OPERON
RP STRUCTURE, AND MUTAGENESIS OF ASP-192 AND ASP-231.
RC STRAIN=Rx / Cp1015;
RX PubMed=15720398; DOI=10.1111/j.1742-4658.2005.04560.x;
RA Novakova L., Saskova L., Pallova P., Janecek J., Novotna J., Ulrych A.,
RA Echenique J., Trombe M.C., Branny P.;
RT "Characterization of a eukaryotic type serine/threonine protein kinase and
RT protein phosphatase of Streptococcus pneumoniae and identification of
RT kinase substrates.";
RL FEBS J. 272:1243-1254(2005).
RN [3]
RP FUNCTION, INTERACTION WITH STKP, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=Rx / Cp1015;
RX PubMed=19502404; DOI=10.1128/jb.00196-09;
RA Osaki M., Arcondeguy T., Bastide A., Touriol C., Prats H., Trombe M.C.;
RT "The StkP/PhpP signaling couple in Streptococcus pneumoniae: cellular
RT organization and physiological characterization.";
RL J. Bacteriol. 191:4943-4950(2009).
RN [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=Rx1;
RX PubMed=22431591; DOI=10.1073/pnas.1119172109;
RA Beilharz K., Novakova L., Fadda D., Branny P., Massidda O., Veening J.W.;
RT "Control of cell division in Streptococcus pneumoniae by the conserved
RT Ser/Thr protein kinase StkP.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E905-E913(2012).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP ASP-192 AND ASP-231.
RC STRAIN=Rx1;
RX PubMed=27776484; DOI=10.1186/s12866-016-0865-6;
RA Ulrych A., Holeckova N., Goldova J., Doubravova L., Benada O.,
RA Kofronova O., Halada P., Branny P.;
RT "Characterization of pneumococcal Ser/Thr protein phosphatase phpP mutant
RT and identification of a novel PhpP substrate, putative RNA binding protein
RT Jag.";
RL BMC Microbiol. 16:247-247(2016).
CC -!- FUNCTION: Protein phosphatase able to dephosphorylate StkP-P and a
CC phosphothreonine residue in a phosphopeptide synthetic substrate. PhpP
CC and its cognate protein kinase StkP appear to constitute a functional
CC signaling couple in vivo, PhpP's primary role probably being to control
CC phosphorylation levels of StkP and of its targets (which include LocZ,
CC DivIVA and KhpB (also called EloR/Jag)). PhpP thus performs an
CC essential control of StkP activity. Overexpression confers an stkP
CC deletion-like phenotype. {ECO:0000269|PubMed:15720398,
CC ECO:0000269|PubMed:19502404, ECO:0000269|PubMed:27776484}.
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:15720398};
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:15720398};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:15720398};
CC Note=Binds 2 manganese ions per subunit. Other divalent cations, such
CC as Mg(2+) or Ca(2+), cannot serve as cofactors.
CC {ECO:0000269|PubMed:15720398};
CC -!- ACTIVITY REGULATION: Phosphatase activity is inhibited by NaF but not
CC by okadaic acid. {ECO:0000269|PubMed:15720398}.
CC -!- SUBUNIT: Interacts with the kinase domain of StkP.
CC {ECO:0000269|PubMed:19502404}.
CC -!- INTERACTION:
CC Q8KY51; A0A0H2UNK2: SP_0376; NbExp=2; IntAct=EBI-6405646, EBI-6507368;
CC Q8KY51; Q8KY50: stkP; Xeno; NbExp=2; IntAct=EBI-6405646, EBI-6405629;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19502404,
CC ECO:0000269|PubMed:22431591}. Note=Mainly localizes to the midcell
CC division sites. PhpP and StkP interact within a membrane-associated
CC protein complex facing the cytoplasm.
CC -!- INDUCTION: The phpP and stkP genes form an operon.
CC {ECO:0000269|PubMed:15720398}.
CC -!- DISRUPTION PHENOTYPE: Attempts to construct an in-frame deletion of the
CC phpP gene were unsuccessful and an allele encoding inactive D231A PhpP
CC phosphatase is lethal in a wild-type genetic background. This suggests
CC that PhpP is essential (PubMed:19502404). Another group has generated a
CC phpP deletion using a two-step negative selection strategy, which has a
CC hyper-phosphorylated phenotype. Cells grow more slowly, are smaller and
CC form short chains, reach a lower final density, are more sensitive to
CC oxidative stress, growth is impaired at 40 degrees Celsius, competence
CC is decreased and mild defects are seen in cell division. Unlike the
CC stkP deletion, cells are unaffected by high salt, acidic and basic pH
CC (PubMed:27776484). {ECO:0000269|PubMed:19502404,
CC ECO:0000269|PubMed:27776484}.
CC -!- MISCELLANEOUS: Strain Rx1 is unencapsulated.
CC {ECO:0000305|PubMed:19502404, ECO:0000305|PubMed:27776484}.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF285441; AAM47529.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8KY51; -.
DR SMR; Q8KY51; -.
DR IntAct; Q8KY51; 2.
DR STRING; 170187.SP_1733; -.
DR eggNOG; COG0631; Bacteria.
DR BRENDA; 3.1.3.16; 16490.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006470; P:protein dephosphorylation; IEA:InterPro.
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 Cytoplasm; Hydrolase; Manganese; Metal-binding; Protein phosphatase.
FT CHAIN 1..246
FT /note="Protein phosphatase PhpP"
FT /id="PRO_0000418147"
FT DOMAIN 2..240
FT /note="PPM-type phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01082"
FT BINDING 36
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 37
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 231
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MUTAGEN 192
FT /note="D->A: Loss of phosphatase activity, partially
FT associates with cell membrane."
FT /evidence="ECO:0000269|PubMed:15720398,
FT ECO:0000269|PubMed:27776484"
FT MUTAGEN 231
FT /note="D->A: Loss of phosphatase activity, loss of
FT association with cell membrane."
FT /evidence="ECO:0000269|PubMed:15720398,
FT ECO:0000269|PubMed:27776484"
SQ SEQUENCE 246 AA; 27104 MW; CDD968CCE6E86E94 CRC64;
MEISLLTDVG QKRTNNQDYV NHYVNRAGRT MIILADGMGG HRAGNIASEM AVTDLGVAWV
DTQIDTVNEV REWFAHYLEI ENQKIHQLGQ DEAYRGMGTT LEVLAIIDNQ AIYAHIGDSR
IGLIRGEEYH QLTSDHSLVN ELLKAGQLTP EEAEAHPQKN IITQSIGQKD EIQPDFGTVI
LESGDYLLLD SDGLTNMISG SEIRDIVTSD IPLADKTETL VRFANNAGGL DNITVALVSM
NEEDAE
