PRP1_SALTY
ID PRP1_SALTY Reviewed; 216 AA.
AC Q8ZNY9; Q8VPE2;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Serine/threonine-protein phosphatase 1;
DE EC=3.1.3.16;
GN Name=pphA; Synonyms=prpA; OrderedLocusNames=STM1853;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX PubMed=11717262; DOI=10.1128/jb.183.24.7053-7057.2001;
RA Shi L., Kehres D.G., Maguire M.E.;
RT "The PPP-family protein phosphatases PrpA and PrpB of Salmonella enterica
RT serovar Typhimurium possess distinct biochemical properties.";
RL J. Bacteriol. 183:7053-7057(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Can hydrolyze phosphorylated Ser-, Thr- or Tyr-substrates in
CC vitro. The natural substrate is unknown.
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;
CC -!- ACTIVITY REGULATION: Inhibited by cadmium, copper, zinc when added
CC cobalt when added concomitantly with manganese.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6-7.;
CC Temperature dependence:
CC Optimum temperature is 45-55 degrees Celsius. Thermostable.;
CC -!- MISCELLANEOUS: Neither magnesium nor calcium stimulates activity.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL09831.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY049950; AAL09831.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE006468; AAL20768.1; -; Genomic_DNA.
DR RefSeq; NP_460809.1; NC_003197.2.
DR RefSeq; WP_000986176.1; NC_003197.2.
DR AlphaFoldDB; Q8ZNY9; -.
DR SMR; Q8ZNY9; -.
DR STRING; 99287.STM1853; -.
DR PaxDb; Q8ZNY9; -.
DR EnsemblBacteria; AAL20768; AAL20768; STM1853.
DR GeneID; 1253372; -.
DR KEGG; stm:STM1853; -.
DR PATRIC; fig|99287.12.peg.1956; -.
DR HOGENOM; CLU_023125_1_1_6; -.
DR PhylomeDB; Q8ZNY9; -.
DR BioCyc; SENT99287:STM1853-MON; -.
DR Proteomes; UP000001014; 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 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..216
FT /note="Serine/threonine-protein phosphatase 1"
FT /id="PRO_0000058909"
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 185
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 216 AA; 25037 MW; C2A62B823F4AAAD5 CRC64;
MMRPEEIYQR IEAKNWRHVW VVGDIHGCFS MLMKRLRECR FDPQQDLLVS VGDLIDRGPD
SLGCLALLRE SWMTAVRGNH EQMALDARAS SQSTLWLMNG GDWFTRLTAE HAAQAEALFI
LCQRLPWILE VRCRHSTHVI AHADYPASTY QWQKKVDLHQ VLWSRERLIN KRGGISGADH
FWFGHTPLRR RMDFANVHYI DTGAVFGGQL TLARIQ
