PRP2_SALTY
ID PRP2_SALTY Reviewed; 218 AA.
AC Q8ZMH3; Q79S89;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Serine/threonine-protein phosphatase 2;
DE EC=3.1.3.16;
GN Name=pphB; Synonyms=prpB; OrderedLocusNames=STM2907;
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].
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 activity but with less efficiency.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5-8.5.;
CC Temperature dependence:
CC Optimum temperature is 30-37 degrees Celsius.;
CC -!- MISCELLANEOUS: Neither magnesium nor calcium stimulates activity.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. PP-1 subfamily.
CC {ECO:0000305}.
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DR EMBL; AY049951; AAL09832.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21787.1; -; Genomic_DNA.
DR RefSeq; NP_461828.1; NC_003197.2.
DR RefSeq; WP_000420452.1; NC_003197.2.
DR AlphaFoldDB; Q8ZMH3; -.
DR SMR; Q8ZMH3; -.
DR STRING; 99287.STM2907; -.
DR PaxDb; Q8ZMH3; -.
DR EnsemblBacteria; AAL21787; AAL21787; STM2907.
DR GeneID; 1254430; -.
DR KEGG; stm:STM2907; -.
DR PATRIC; fig|99287.12.peg.3061; -.
DR HOGENOM; CLU_023125_1_1_6; -.
DR OMA; NTSWFIS; -.
DR PhylomeDB; Q8ZMH3; -.
DR BioCyc; SENT99287:STM2907-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 Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 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_0000058911"
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"
SQ SEQUENCE 218 AA; 25025 MW; 723B98837426E350 CRC64;
MELIRYADIN SDLYRHIWVV GDIHGCYSLL LTRLAQLNFS PDTDLLISTG DNIDRGKENL
ETLRLLNTPW FISVVGNHEA MALDAFETQD GNFWYVNGGY WYDSVTEKDR QEATELLLTF
KQRPHIIEVE TSSKKYVIAH ADYPDDSYDY GKQVDIDSVL WSRDRLLGSL QGNIHPIRGA
DTFIFGHMIV DYTTTFANQI YIDTGSFCSG NLSFFKIK
