ID   PRP2_SALTY              Reviewed;         218 AA.
AC   Q8ZMH3; Q79S89;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Serine/threonine-protein phosphatase 2;
DE            EC=3.1.3.16;
GN   Name=pphB; Synonyms=prpB; OrderedLocusNames=STM2907;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=11717262; DOI=10.1128/jb.183.24.7053-7057.2001;
RA   Shi L., Kehres D.G., Maguire M.E.;
RT   "The PPP-family protein phosphatases PrpA and PrpB of Salmonella enterica
RT   serovar Typhimurium possess distinct biochemical properties.";
RL   J. Bacteriol. 183:7053-7057(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Can hydrolyze phosphorylated Ser-, Thr- or Tyr-substrates in
CC       vitro. The natural substrate is unknown.
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;
CC   -!- ACTIVITY REGULATION: Inhibited by cadmium, copper, zinc when added
CC       activity but with less efficiency.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5-8.5.;
CC       Temperature dependence:
CC         Optimum temperature is 30-37 degrees Celsius.;
CC   -!- MISCELLANEOUS: Neither magnesium nor calcium stimulates activity.
CC   -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC       {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; AY049951; AAL09832.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL21787.1; -; Genomic_DNA.
DR   RefSeq; NP_461828.1; NC_003197.2.
DR   RefSeq; WP_000420452.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZMH3; -.
DR   SMR; Q8ZMH3; -.
DR   STRING; 99287.STM2907; -.
DR   PaxDb; 99287-STM2907; -.
DR   GeneID; 1254430; -.
DR   KEGG; stm:STM2907; -.
DR   PATRIC; fig|99287.12.peg.3061; -.
DR   HOGENOM; CLU_023125_1_1_6; -.
DR   OMA; NTSWFIS; -.
DR   PhylomeDB; Q8ZMH3; -.
DR   BioCyc; SENT99287:STM2907-MONOMER; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0008803; F:bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity; IBA:GO_Central.
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:0016791; F:phosphatase activity; IBA:GO_Central.
DR   GO; GO:0110154; P:RNA decapping; IBA:GO_Central.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   PANTHER; PTHR42850; METALLOPHOSPHOESTERASE; 1.
DR   PANTHER; PTHR42850:SF8; SERINE_THREONINE-PROTEIN PHOSPHATASE 2; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Manganese; Metal-binding; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..218
FT                   /note="Serine/threonine-protein phosphatase 2"
FT                   /id="PRO_0000058911"
FT   ACT_SITE        78
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         22
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         24
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         51
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         77
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   218 AA;  25025 MW;  723B98837426E350 CRC64;
     MELIRYADIN SDLYRHIWVV GDIHGCYSLL LTRLAQLNFS PDTDLLISTG DNIDRGKENL
     ETLRLLNTPW FISVVGNHEA MALDAFETQD GNFWYVNGGY WYDSVTEKDR QEATELLLTF
     KQRPHIIEVE TSSKKYVIAH ADYPDDSYDY GKQVDIDSVL WSRDRLLGSL QGNIHPIRGA
     DTFIFGHMIV DYTTTFANQI YIDTGSFCSG NLSFFKIK
//