ID A5D1B3_PELTS Unreviewed; 237 AA. AC A5D1B3; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 27-MAR-2024, entry version 77. DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081}; DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081}; GN Name=PTC1 {ECO:0000313|EMBL:BAF59965.1}; GN OrderedLocusNames=PTH_1784 {ECO:0000313|EMBL:BAF59965.1}; OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae; OC Pelotomaculum. OX NCBI_TaxID=370438 {ECO:0000313|EMBL:BAF59965.1, ECO:0000313|Proteomes:UP000006556}; RN [1] {ECO:0000313|Proteomes:UP000006556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13744 / JCM 10971 / SI {ECO:0000313|Proteomes:UP000006556}; RX PubMed=18218977; DOI=10.1101/gr.7136508; RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.; RT "The genome of Pelotomaculum thermopropionicum reveals niche-associated RT evolution in anaerobic microbiota."; RL Genome Res. 18:442-448(2008). 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; AP009389; BAF59965.1; -; Genomic_DNA. DR AlphaFoldDB; A5D1B3; -. DR STRING; 370438.PTH_1784; -. DR KEGG; pth:PTH_1784; -. DR eggNOG; COG0631; Bacteria. DR HOGENOM; CLU_034545_4_1_9; -. DR Proteomes; UP000006556; 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; KW Reference proteome {ECO:0000313|Proteomes:UP000006556}. FT DOMAIN 2..237 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|PROSITE:PS51746" SQ SEQUENCE 237 AA; 25604 MW; 785ABD071BA0ACFC CRC64; MRWAQVTDTG PVRAANEDSL IVSPEIGLFA VADGMGGHQA GEVASSMALV LMERELKKRL GNGERPENAL IDSVKEANRS IYELALRNPR LAGMGTTVTA CLRCLNEILV AQVGDSRAYL LRDGLIVRLT EDHSLVQELV KNGGITEEQA LSHPHRNVLT RALGTSPFLE VDLKRVGIKP GDLLLLCTDG LSGYLRAEEI MSTVFTSPGL EAAVQTLLLK AFQYGGTDNV TIILVEL //