PRP1_ECOLI
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 03-AUG-2022, entry version 151.
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; Proteobacteria; 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; P55798; -.
DR PRIDE; P55798; -.
DR EnsemblBacteria; AAC74908; AAC74908; b1838.
DR EnsemblBacteria; BAA15649; BAA15649; BAA15649.
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 PhylomeDB; P55798; -.
DR BioCyc; EcoCyc:G7011-MON; -.
DR BioCyc; MetaCyc:G7011-MON; -.
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: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 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 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
