ID   PRP1_ECOLI              Reviewed;         218 AA.
AC   P55798; P76276;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 159.
DE   RecName: Full=Serine/threonine-protein phosphatase 1;
DE            EC=3.1.3.16;
GN   Name=pphA; Synonyms=prpA, yebX; OrderedLocusNames=b1838, JW1827;
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 ASP-24; HIS-26 AND
RP   LEU-107.
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 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
RN   [3]
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   [4]
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: Plays a key role in signaling protein misfolding via the
CC       CpxR/CPXA transducing system. It also modulates the phosphorylated
CC       status of many phosphoproteins in E.coli, some of which acting as major
CC       chaperones. 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. PP-1 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U51991; AAB53934.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74908.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15649.2; -; Genomic_DNA.
DR   PIR; F64945; F64945.
DR   RefSeq; NP_416352.4; NC_000913.3.
DR   RefSeq; WP_000812724.1; NZ_STEB01000009.1.
DR   AlphaFoldDB; P55798; -.
DR   SMR; P55798; -.
DR   BioGRID; 4261399; 7.
DR   IntAct; P55798; 1.
DR   STRING; 511145.b1838; -.
DR   PaxDb; 511145-b1838; -.
DR   EnsemblBacteria; AAC74908; AAC74908; b1838.
DR   GeneID; 66674272; -.
DR   GeneID; 946356; -.
DR   KEGG; ecj:JW1827; -.
DR   KEGG; eco:b1838; -.
DR   PATRIC; fig|1411691.4.peg.412; -.
DR   EchoBASE; EB3780; -.
DR   eggNOG; COG0639; Bacteria.
DR   HOGENOM; CLU_023125_1_1_6; -.
DR   InParanoid; P55798; -.
DR   OMA; MNGGDWY; -.
DR   OrthoDB; 5296354at2; -.
DR   PhylomeDB; P55798; -.
DR   BioCyc; EcoCyc:G7011-MONOMER; -.
DR   BioCyc; MetaCyc:G7011-MONOMER; -.
DR   BRENDA; 3.1.3.16; 2026.
DR   BRENDA; 3.1.3.48; 2026.
DR   PRO; PR:P55798; -.
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:0009266; P:response to temperature stimulus; IEP:EcoCyc.
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   InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR   PANTHER; PTHR42850; METALLOPHOSPHOESTERASE; 1.
DR   PANTHER; PTHR42850:SF4; METALLOPHOSPHOESTERASE YNL217W-RELATED; 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 1"
FT                   /id="PRO_0000058908"
FT   ACT_SITE        80
FT                   /note="Proton donor"
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         26
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         53
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         79
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         24
FT                   /note="D->V: Loss of function."
FT                   /evidence="ECO:0000269|PubMed:9130712"
FT   MUTAGEN         26
FT                   /note="H->L: Loss of function."
FT                   /evidence="ECO:0000269|PubMed:9130712"
FT   MUTAGEN         26
FT                   /note="H->N: Loss of function."
FT                   /evidence="ECO:0000269|PubMed:9130712"
FT   MUTAGEN         107
FT                   /note="L->Q: Loss of function."
FT                   /evidence="ECO:0000269|PubMed:9130712"
SQ   SEQUENCE   218 AA;  25274 MW;  9E6C452168004521 CRC64;
     MKQPAPVYQR IAGHQWRHIW LSGDIHGCLE QLRRKLWHCR FDPWRDLLIS VGDVIDRGPQ
     SLRCLQLLEQ HWVCAVRGNH EQMAMDALAS QQMSLWLMNG GDWFIALADN QQKQAKTALE
     KCQHLPFILE VHSRTGKHVI AHADYPDDVY EWQKDVDLHQ VLWSRSRLGE RQKGQGITGA
     DHFWFGHTPL RHRVDIGNLH YIDTGAVFGG ELTLVQLQ
//