PHPP_STRP2
ID PHPP_STRP2 Reviewed; 246 AA.
AC Q04J42;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
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; OrderedLocusNames=SPD_1543;
OS Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=373153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D39 / NCTC 7466;
RX PubMed=17041037; DOI=10.1128/jb.01148-06;
RA Lanie J.A., Ng W.-L., Kazmierczak K.M., Andrzejewski T.M., Davidsen T.M.,
RA Wayne K.J., Tettelin H., Glass J.I., Winkler M.E.;
RT "Genome sequence of Avery's virulent serotype 2 strain D39 of Streptococcus
RT pneumoniae and comparison with that of unencapsulated laboratory strain
RT R6.";
RL J. Bacteriol. 189:38-51(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=D39 / NCTC 7466;
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). Also dephosphorylates DivIVA in vivo.
CC {ECO:0000250, ECO:0000269|PubMed:22431591}.
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:22431591};
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:22431591};
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 in a StkP-dependent
CC manner, since PhpP is present at midcell only when StkP is active.
CC -!- SIMILARITY: Belongs to the PP2C family. {ECO:0000305}.
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DR EMBL; CP000410; ABJ54228.1; -; Genomic_DNA.
DR RefSeq; WP_000406247.1; NC_008533.2.
DR AlphaFoldDB; Q04J42; -.
DR SMR; Q04J42; -.
DR STRING; 373153.SPD_1543; -.
DR EnsemblBacteria; ABJ54228; ABJ54228; SPD_1543.
DR GeneID; 60234038; -.
DR KEGG; spd:SPD_1543; -.
DR eggNOG; COG0631; Bacteria.
DR HOGENOM; CLU_034545_4_1_9; -.
DR OMA; EDHTWVA; -.
DR OrthoDB; 1835483at2; -.
DR BioCyc; SPNE373153:G1G6V-1666-MON; -.
DR Proteomes; UP000001452; 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; 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_0000418149"
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
