PHPP_STRR6
ID PHPP_STRR6 Reviewed; 246 AA.
AC Q8DNR9;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
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; Synonyms=pppL; OrderedLocusNames=spr1578;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [2]
RP SUBCELLULAR LOCATION, AND OVEREXPRESSION.
RC STRAIN=ATCC BAA-255 / R6;
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).
CC -!- FUNCTION: Protein phosphatase able to dephosphorylate StkP-P and other
CC phosphorylated protein substrates. PhpP and its cognate protein kinase
CC StkP appear to constitute a functional signaling couple in vivo, PhpP's
CC primary role being probably to control phosphorylation levels of StkP
CC and of its targets. PhpP thus performs an essential control of StkP
CC activity (By similarity). {ECO:0000250}.
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 -!- 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22431591}.
CC Note=Mainly localizes to the midcell division sites. Delocalizes from
CC the septum in the presence of antibiotics that target the latest stages
CC of cell-wall biosynthesis and in cells that have stopped dividing.
CC -!- MISCELLANEOUS: Overexpression of PhpP leads to a phenotype comparable
CC to cells lacking stkP, with an increased cell length.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; AE007317; AAL00381.1; -; Genomic_DNA.
DR PIR; H95201; H95201.
DR PIR; H98068; H98068.
DR RefSeq; NP_359170.1; NC_003098.1.
DR RefSeq; WP_000406247.1; NC_003098.1.
DR AlphaFoldDB; Q8DNR9; -.
DR SMR; Q8DNR9; -.
DR STRING; 171101.spr1578; -.
DR EnsemblBacteria; AAL00381; AAL00381; spr1578.
DR GeneID; 60234038; -.
DR KEGG; spr:spr1578; -.
DR PATRIC; fig|171101.6.peg.1705; -.
DR eggNOG; COG0631; Bacteria.
DR HOGENOM; CLU_034545_4_1_9; -.
DR OMA; EDHTWVA; -.
DR Proteomes; UP000000586; Chromosome.
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; IBA:GO_Central.
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 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Manganese; Metal-binding; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..246
FT /note="Protein phosphatase PhpP"
FT /id="PRO_0000418148"
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"
SQ SEQUENCE 246 AA; 27103 MW; C7D368C6ECE86E94 CRC64;
MEISLLTDVG QKRTNNQDYV NHYVNRAGRT MIILADGMGG HRAGNIASEM AVTDLGVAWV
DTQIDTVNEV REWFAHYLEI ENQKIHQLGQ DEAYRGMGTT LEVLAIIDNQ AIYAHIGDSR
IGLIRGEEYH QLTSDHSLVN ELLKAGQLTP EEAEAHPQKN IITQSIGQKD EIQPDFGTVI
LESGDYLLLN SDGLTNMISG SEIRDIVTSD IPLADKTETL VRFANNAGGL DNITVALVSM
NEEDAE
