ID PP_LAMBD Reviewed; 221 AA. AC P03772; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 27-MAR-2024, entry version 140. DE RecName: Full=Serine/threonine-protein phosphatase; DE EC=3.1.3.16; OS Escherichia phage lambda (Bacteriophage lambda). OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Lambdavirus; Lambdavirus lambda. OX NCBI_TaxID=2681611; OH NCBI_TaxID=562; Escherichia coli. RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=6221115; DOI=10.1016/0022-2836(82)90546-0; RA Sanger F., Coulson A.R., Hong G.F., Hill D.F., Petersen G.B.; RT "Nucleotide sequence of bacteriophage lambda DNA."; RL J. Mol. Biol. 162:729-773(1982). RN [2] RP FUNCTION. RX PubMed=2548489; DOI=10.1042/bj2600931; RA Cohen P.T.W., Cohen P.; RT "Discovery of a protein phosphatase activity encoded in the genome of RT bacteriophage lambda. Probable identity with open reading frame 221."; RL Biochem. J. 260:931-934(1989). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS, AND RP COFACTOR. RX PubMed=11112522; DOI=10.1021/bi0021030; RA Voegtli W.C., White D.J., Reiter N.J., Rusnak F., Rosenzweig A.C.; RT "Structure of the bacteriophage lambda Ser/Thr protein phosphatase with RT sulfate ion bound in two coordination modes."; RL Biochemistry 39:15365-15374(2000). 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 Evidence={ECO:0000269|PubMed:11112522}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:11112522}; CC -!- INTERACTION: CC P03772; Q64702: Plk4; Xeno; NbExp=2; IntAct=EBI-4478820, EBI-2552433; CC -!- SIMILARITY: Belongs to the PPP phosphatase family. {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; J02459; AAA96594.1; -; Genomic_DNA. DR PIR; G43011; Q1BP1L. DR RefSeq; NP_040641.1; NC_001416.1. DR PDB; 1G5B; X-ray; 2.15 A; A/B/C=1-221. DR PDBsum; 1G5B; -. DR SMR; P03772; -. DR DIP; DIP-44028N; -. DR IntAct; P03772; 4. DR MINT; P03772; -. DR BindingDB; P03772; -. DR ChEMBL; CHEMBL3695; -. DR GeneID; 2703476; -. DR KEGG; vg:2703476; -. DR OrthoDB; 22132at10239; -. DR EvolutionaryTrace; P03772; -. DR PRO; PR:P03772; -. DR Proteomes; UP000001711; Genome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC. DR CDD; cd07424; MPP_PrpA_PrpB; 1. 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 3D-structure; Hydrolase; Manganese; Metal-binding; Protein phosphatase; KW Reference proteome. FT CHAIN 1..221 FT /note="Serine/threonine-protein phosphatase" FT /id="PRO_0000058912" FT ACT_SITE 76 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 20 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT BINDING 22 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT BINDING 49 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="1" FT BINDING 49 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT BINDING 75 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT BINDING 186 FT /ligand="Mn(2+)" FT /ligand_id="ChEBI:CHEBI:29035" FT /ligand_label="2" FT STRAND 3..8 FT /evidence="ECO:0007829|PDB:1G5B" FT HELIX 9..11 FT /evidence="ECO:0007829|PDB:1G5B" FT STRAND 15..18 FT /evidence="ECO:0007829|PDB:1G5B" FT HELIX 25..35 FT /evidence="ECO:0007829|PDB:1G5B" FT TURN 39..41 FT /evidence="ECO:0007829|PDB:1G5B" FT STRAND 43..46 FT /evidence="ECO:0007829|PDB:1G5B" FT STRAND 51..55 FT /evidence="ECO:0007829|PDB:1G5B" FT HELIX 57..61 FT /evidence="ECO:0007829|PDB:1G5B" FT HELIX 62..65 FT /evidence="ECO:0007829|PDB:1G5B" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:1G5B" FT HELIX 75..84 FT /evidence="ECO:0007829|PDB:1G5B" FT HELIX 91..94 FT /evidence="ECO:0007829|PDB:1G5B" FT TURN 95..97 FT /evidence="ECO:0007829|PDB:1G5B" FT HELIX 98..103 FT /evidence="ECO:0007829|PDB:1G5B" FT HELIX 106..119 FT /evidence="ECO:0007829|PDB:1G5B" FT STRAND 124..130 FT /evidence="ECO:0007829|PDB:1G5B" FT STRAND 133..137 FT /evidence="ECO:0007829|PDB:1G5B" FT STRAND 144..146 FT /evidence="ECO:0007829|PDB:1G5B" FT HELIX 155..160 FT /evidence="ECO:0007829|PDB:1G5B" FT HELIX 163..169 FT /evidence="ECO:0007829|PDB:1G5B" FT STRAND 179..184 FT /evidence="ECO:0007829|PDB:1G5B" FT STRAND 193..195 FT /evidence="ECO:0007829|PDB:1G5B" FT STRAND 198..200 FT /evidence="ECO:0007829|PDB:1G5B" FT HELIX 205..208 FT /evidence="ECO:0007829|PDB:1G5B" FT STRAND 213..217 FT /evidence="ECO:0007829|PDB:1G5B" SQ SEQUENCE 221 AA; 25219 MW; 5CE0E1A0F3BC5CB5 CRC64; MRYYEKIDGS KYRNIWVVGD LHGCYTNLMN KLDTIGFDNK KDLLISVGDL VDRGAENVEC LELITFPWFR AVRGNHEQMM IDGLSERGNV NHWLLNGGGW FFNLDYDKEI LAKALAHKAD ELPLIIELVS KDKKYVICHA DYPFDEYEFG KPVDHQQVIW NRERISNSQN GIVKEIKGAD TFIFGHTPAV KPLKFANQMY IDTGAVFCGN LTLIQVQGEG A //