ID Q74IN1_LACJO Unreviewed; 250 AA. AC Q74IN1; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 112. DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081}; DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081}; GN OrderedLocusNames=LJ_1538 {ECO:0000313|EMBL:AAS09306.1}; OS Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533). OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; OC Lactobacillus. OX NCBI_TaxID=257314 {ECO:0000313|EMBL:AAS09306.1, ECO:0000313|Proteomes:UP000000581}; RN [1] {ECO:0000313|EMBL:AAS09306.1, ECO:0000313|Proteomes:UP000000581} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CNCM I-1225 / La1 / NCC 533 RC {ECO:0000313|Proteomes:UP000000581}; RX PubMed=14983040; DOI=10.1073/pnas.0307327101; RA Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C., RA Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R., RA Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.; RT "The genome sequence of the probiotic intestinal bacterium Lactobacillus RT johnsonii NCC 533."; RL Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004). 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}; 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; AE017198; AAS09306.1; -; Genomic_DNA. DR RefSeq; WP_004895348.1; NC_005362.1. DR AlphaFoldDB; Q74IN1; -. DR KEGG; ljo:LJ_1538; -. DR eggNOG; COG0631; Bacteria. DR HOGENOM; CLU_034545_4_1_9; -. DR Proteomes; UP000000581; Chromosome. DR GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro. 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; FT DOMAIN 3..243 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|PROSITE:PS51746" SQ SEQUENCE 250 AA; 27577 MW; 24801EDA25C73132 CRC64; MIKTAFASSI GRVRETNQDF VKVFKNQNNI IMGIVCDGMG GHQGGDVAST MAVSHLGHNF EKTDFTDPDL AQKWLTVQLR LENETILNTA DRFSDLNGMG TTIVLAIAFT EKILIAHLGD SRCYLYGGNE FKQITEDHSL VHELVKMGQI TEQQARNHPQ KNIITETLGV SSTVNPEFDI LEVHAGDIFL LCTDGLTNSL TDPQIQQILA TKNLSLKERC NKLINEANRL GGGDNITVCL LAYVEKDGDK //