PP_LAMBD
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 03-AUG-2022, entry version 135.
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 Caudovirales; Siphoviridae; Lambdavirus.
OX NCBI_TaxID=10710;
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 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 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 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
