ID   Q1WUA9_LIGS1            Unreviewed;       247 AA.
AC   Q1WUA9;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 93.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=LSL_0616 {ECO:0000313|EMBL:ABD99426.1};
OS   Ligilactobacillus salivarius (strain UCC118) (Lactobacillus salivarius).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=362948 {ECO:0000313|EMBL:ABD99426.1, ECO:0000313|Proteomes:UP000006559};
RN   [1] {ECO:0000313|EMBL:ABD99426.1, ECO:0000313|Proteomes:UP000006559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCC118 {ECO:0000313|EMBL:ABD99426.1,
RC   ECO:0000313|Proteomes:UP000006559};
RX   PubMed=16617113; DOI=10.1073/pnas.0511060103;
RA   Claesson M.J., Li Y., Leahy S., Canchaya C., van Pijkeren J.P.,
RA   Cerdeno-Tarraga A.M., Parkhill J., Flynn S., O'Sullivan G.C., Collins J.K.,
RA   Higgins D., Shanahan F., Fitzgerald G.F., van Sinderen D., O'Toole P.W.;
RT   "Multireplicon genome architecture of Lactobacillus salivarius.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:6718-6723(2006).
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         Evidence={ECO:0000256|ARBA:ARBA00001512};
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         Evidence={ECO:0000256|ARBA:ARBA00001482};
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DR   EMBL; CP000233; ABD99426.1; -; Genomic_DNA.
DR   RefSeq; WP_003701707.1; NC_007929.1.
DR   RefSeq; YP_535509.1; NC_007929.1.
DR   AlphaFoldDB; Q1WUA9; -.
DR   STRING; 362948.LSL_0616; -.
DR   GeneID; 69723873; -.
DR   KEGG; lsl:LSL_0616; -.
DR   PATRIC; fig|362948.14.peg.695; -.
DR   HOGENOM; CLU_034545_4_1_9; -.
DR   OrthoDB; 9801841at2; -.
DR   Proteomes; UP000006559; Chromosome.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   NCBIfam; NF033484; Stp1_PP2C_phos; 1.
DR   PANTHER; PTHR47992:SF267; ALPHABET, ISOFORM E; 1.
DR   PANTHER; PTHR47992; PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF13672; PP2C_2; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ABD99426.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006559}.
FT   DOMAIN          2..241
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   247 AA;  27524 MW;  06A5F3FBCFCE6D8D CRC64;
     MEIAYLSDLG KMRKNNEDYV GKFVNKAGAV MVIVADGLGG HNGGEVASEM AVSHLGYYFS
     ETSFFSISQA STWLSKKVDE ENSLILKNSL HYKDLRGMGT TLVVAIIFEQ EFLLAHIGDS
     RGYILEKGNL TRVTEDHSLV NELIKEGELS PEEAEHHPKK NIITRSLGIS KNSELDEEFF
     QITKNSILML CTDGLTNMVE DTKLERLLNI SESLPDKCQR LVDEANRAGG NDNISVLLVS
     FDEEVKY
//