ID   PRP3_ECOLI              Reviewed;         253 AA.
AC   P76395; Q2MAX7;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Serine/threonine-protein phosphatase 3 {ECO:0000305};
DE            EC=3.1.3.16 {ECO:0000269|PubMed:29967116};
DE   AltName: Full=PP2C-like Ser/Thr phosphatase {ECO:0000303|PubMed:29967116};
DE   AltName: Full=Protein phosphatase C {ECO:0000303|PubMed:29967116};
GN   Name=pphC {ECO:0000303|PubMed:29967116}; Synonyms=yegK;
GN   OrderedLocusNames=b2072, JW2057;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
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   [2]
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).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION, AND MUTAGENESIS OF ASP-46.
RX   PubMed=29967116; DOI=10.1128/jb.00225-18;
RA   Rajagopalan K., Dworkin J.;
RT   "Identification and biochemical characterization of a novel PP2C-like
RT   Ser/Thr phosphatase in E. coli.";
RL   J. Bacteriol. 200:E00225-E00225(2018).
CC   -!- FUNCTION: PP2C-like phosphatase that can dephosphorylate YegI. In
CC       vitro, can hydrolyze p-nitrophenyl phosphate (pNPP) to p-nitrophenol.
CC       {ECO:0000269|PubMed:29967116}.
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:29967116};
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:29967116};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:29967116};
CC   -!- ACTIVITY REGULATION: Activity dramatically decreases in the presence of
CC       the general protein phosphatase inhibitor sodium phosphate. Slightly
CC       inhibited by sodium fluoride. Activity decreases in the presence of the
CC       metal chelator EDTA. {ECO:0000269|PubMed:29967116}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.21 mM for pNPP {ECO:0000269|PubMed:29967116};
CC         Vmax=99.85 pmol/min/mg enzyme with pNPP as substrate
CC         {ECO:0000269|PubMed:29967116};
CC         Note=kcat is 0.093 sec(-1) with pNPP as substrate.
CC         {ECO:0000269|PubMed:29967116};
CC   -!- PTM: Phosphorylated by YegI. {ECO:0000269|PubMed:29967116}.
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DR   EMBL; U00096; AAC75133.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76579.1; -; Genomic_DNA.
DR   PIR; G64973; G64973.
DR   RefSeq; NP_416576.1; NC_000913.3.
DR   RefSeq; WP_000119090.1; NZ_LN832404.1.
DR   AlphaFoldDB; P76395; -.
DR   SMR; P76395; -.
DR   BioGRID; 4260424; 9.
DR   STRING; 511145.b2072; -.
DR   PaxDb; P76395; -.
DR   PRIDE; P76395; -.
DR   EnsemblBacteria; AAC75133; AAC75133; b2072.
DR   EnsemblBacteria; BAE76579; BAE76579; BAE76579.
DR   GeneID; 947269; -.
DR   KEGG; ecj:JW2057; -.
DR   KEGG; eco:b2072; -.
DR   PATRIC; fig|511145.12.peg.2149; -.
DR   EchoBASE; EB3807; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_066842_1_1_6; -.
DR   OMA; CQDAHHW; -.
DR   BioCyc; EcoCyc:G7111-MON; -.
DR   BioCyc; MetaCyc:G7111-MON; -.
DR   BRENDA; 3.1.3.16; 2026.
DR   SABIO-RK; P76395; -.
DR   PRO; PR:P76395; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016791; F:phosphatase activity; IDA:EcoCyc.
DR   Gene3D; 3.60.40.10; -; 1.
DR   InterPro; IPR036457; PPM-type_dom_sf.
DR   SUPFAM; SSF81606; SSF81606; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Manganese; Phosphoprotein; Protein phosphatase;
KW   Reference proteome.
FT   CHAIN           1..253
FT                   /note="Serine/threonine-protein phosphatase 3"
FT                   /id="PRO_0000169126"
FT   MUTAGEN         46
FT                   /note="D->N: Loss of phosphatase activity."
FT                   /evidence="ECO:0000269|PubMed:29967116"
SQ   SEQUENCE   253 AA;  27208 MW;  DC828DD5AD67E7E0 CRC64;
     MSWRLVYAST VGTSHISADL PCQDACQMQI AWLNDQQPLL SVFVADGAGS VSQGGEGAML
     AVNEAMAYMS QKVQGGELGL NDVLATNMVL TIRQRLFAEA EAKELAVRDF ACTFLGLISS
     PDGTLIMQIG DGGVVVDLGH GLQLPLTPMA GEYANMTHFI TDEDAVSRLE TFTSTGRAHK
     VAAFTDGIQR LALNMLDNSP HVPFFTPFFN GLAAATQEQL DLLPELLKQF LSSPAVNERT
     DDDKTLALAL WAE