ID A0A2N0UPH6_9FIRM Unreviewed; 241 AA. AC A0A2N0UPH6; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 02-OCT-2024, entry version 19. DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081}; DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081}; GN Name=stp {ECO:0000313|EMBL:PKD28891.1}; GN ORFNames=RB5AMG_00229 {ECO:0000313|EMBL:PKD31356.1}, RBL236_01505 GN {ECO:0000313|EMBL:PKD28891.1}, RO624_01380 GN {ECO:0000313|EMBL:MDT4340771.1}; OS Ruminococcus bromii. OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae; OC Ruminococcus. OX NCBI_TaxID=40518 {ECO:0000313|EMBL:PKD28891.1, ECO:0000313|Proteomes:UP000233570}; RN [1] {ECO:0000313|Proteomes:UP000233562, ECO:0000313|Proteomes:UP000233570} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5AMG {ECO:0000313|EMBL:PKD31356.1, RC ECO:0000313|Proteomes:UP000233562}, and L2-36 RC {ECO:0000313|EMBL:PKD28891.1, ECO:0000313|Proteomes:UP000233570}; RX PubMed=29159997; RA Mukhopadhya I., Morais S., Laverde-Gomez J., Sheridan P.O., Walker A.W., RA Kelly W., Klieve A.V., Ouwerkerk D., Duncan S.H., Louis P., Koropatkin N., RA Cockburn D., Kibler R., Cooper P.J., Sandoval C., Crost E., Juge N., RA Bayer E.A., Flint H.J.; RT "Sporulation capability and amylosome conservation among diverse human RT colonic and rumen isolates of the keystone starch-degrader Ruminococcus RT bromii."; RL Environ. Microbiol. 0:0-0(2017). RN [2] {ECO:0000313|EMBL:MDT4340771.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=225S_6FAANB {ECO:0000313|EMBL:MDT4340771.1}; RA Wilde J., Boyes R., Robinson A.V., Daisley B.A., Allen-Vercoe E.; RT "Reintroducing virulent viruses to syntetic microbiomes."; RL Submitted (APR-2023) to the EMBL/GenBank/DDBJ databases. 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:PKD28891.1}. 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; JAVSNA010000001; MDT4340771.1; -; Genomic_DNA. DR EMBL; NPHY01000018; PKD28891.1; -; Genomic_DNA. DR EMBL; NNBY01000025; PKD31356.1; -; Genomic_DNA. DR Proteomes; UP000233562; Unassembled WGS sequence. DR Proteomes; UP000233570; Unassembled WGS sequence. DR Proteomes; UP001262132; Unassembled WGS sequence. 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:PKD28891.1}. FT DOMAIN 2..241 FT /note="PPM-type phosphatase" FT /evidence="ECO:0000259|PROSITE:PS51746" SQ SEQUENCE 241 AA; 26376 MW; 43A31D87868B169B CRC64; MEVFSKSDIG LVRNQNQDDC RFGVISPSCV WAVVCDGMGG ANGGNIASAT AVDYISTKIT DLYKDDMTKE QIGELMAEIV VNANMKVFEM SMKDPELTGM GTTCEFVFVK DTTVHVVHVG DSRTYAIRGG KIKQLTEDHS VVQEMVRRGE LTYEQAQNHP NKNFITRALG IKPSVRLDYI EANFIYGDVL LICTDGLSNC VTTGDMVKIC HENRGEGLIT KLVDKAKDGG GSDNITATVI Y //