ID   PRP2_ECOLI              Reviewed;         218 AA.
AC   P55799; Q2MA95;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Serine/threonine-protein phosphatase 2;
DE            EC=3.1.3.16;
GN   Name=pphB; Synonyms=prpB, ygbH; OrderedLocusNames=b2734, JW2704;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF HIS-78.
RC   STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX   PubMed=9130712; DOI=10.1093/emboj/16.7.1670;
RA   Missiakas D., Raina S.;
RT   "Signal transduction pathways in response to protein misfolding in the
RT   extracytoplasmic compartments of E. coli: role of two new phosphoprotein
RT   phosphatases PrpA and PrpB.";
RL   EMBO J. 16:1670-1685(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
CC   -!- FUNCTION: Has been shown, in vitro, to act on Ser, Thr and Tyr-
CC       phosphorylated substrates.
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   -!- SIMILARITY: Belongs to the PPP phosphatase family. {ECO:0000305}.
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DR   EMBL; U51682; AAB53933.1; -; Genomic_DNA.
DR   EMBL; U29579; AAA69244.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75776.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76811.1; -; Genomic_DNA.
DR   PIR; B65054; B65054.
DR   RefSeq; NP_417214.1; NC_000913.3.
DR   RefSeq; WP_001141337.1; NZ_LN832404.1.
DR   AlphaFoldDB; P55799; -.
DR   SMR; P55799; -.
DR   BioGRID; 4261420; 15.
DR   IntAct; P55799; 5.
DR   STRING; 511145.b2734; -.
DR   PaxDb; 511145-b2734; -.
DR   EnsemblBacteria; AAC75776; AAC75776; b2734.
DR   GeneID; 947196; -.
DR   KEGG; ecj:JW2704; -.
DR   KEGG; eco:b2734; -.
DR   PATRIC; fig|1411691.4.peg.4006; -.
DR   EchoBASE; EB2905; -.
DR   eggNOG; COG0639; Bacteria.
DR   HOGENOM; CLU_023125_1_1_6; -.
DR   InParanoid; P55799; -.
DR   OMA; NTSWFIS; -.
DR   OrthoDB; 5296354at2; -.
DR   PhylomeDB; P55799; -.
DR   BioCyc; EcoCyc:G7415-MONOMER; -.
DR   BioCyc; MetaCyc:G7415-MONOMER; -.
DR   PRO; PR:P55799; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; 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:0008138; F:protein tyrosine/serine/threonine phosphatase activity; IDA:EcoCyc.
DR   GO; GO:0110154; P:RNA decapping; IBA:GO_Central.
DR   CDD; cd07424; MPP_PrpA_PrpB; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
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.
DR   PROSITE; PS00125; SER_THR_PHOSPHATASE; 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_0000058910"
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"
FT   MUTAGEN         78
FT                   /note="H->N: In prpB17; loss of function."
FT                   /evidence="ECO:0000269|PubMed:9130712"
SQ   SEQUENCE   218 AA;  25098 MW;  965B7935E01FAE33 CRC64;
     MPSTRYQKIN AHHYRHIWVV GDIHGEYQLL QSRLHQLSFF PKIDLLISVG DNIDRGPESL
     DVLRLLNQPW FTSVKGNHEA MALEAFETGD GNMWLASGGD WFFDLNDSEQ QEAIDLLLKF
     HHLPHIIEIT NDNIKYAIAH ADYPGSEYLF GKEIAESELL WPVDRVQKSL NGELQQINGA
     DYFIFGHMMF DNIQTFANQI YIDTGSPNSG RLSFYKIK
//