PRP2_ECOLI
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 03-AUG-2022, entry version 146.
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; Proteobacteria; 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; P55799; -.
DR PRIDE; P55799; -.
DR EnsemblBacteria; AAC75776; AAC75776; b2734.
DR EnsemblBacteria; BAE76811; BAE76811; BAE76811.
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 PhylomeDB; P55799; -.
DR BioCyc; EcoCyc:G7415-MON; -.
DR BioCyc; MetaCyc:G7415-MON; -.
DR PRO; PR:P55799; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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 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 Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 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
