ID   A0A2N0UPH6_9FIRM        Unreviewed;       241 AA.
AC   A0A2N0UPH6;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   29-MAY-2024, entry version 17.
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};
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).
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}.
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DR   EMBL; NPHY01000018; PKD28891.1; -; Genomic_DNA.
DR   EMBL; NNBY01000025; PKD31356.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N0UPH6; -.
DR   Proteomes; UP000233562; Unassembled WGS sequence.
DR   Proteomes; UP000233570; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IEA:TreeGrafter.
DR   GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; IEA:TreeGrafter.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:TreeGrafter.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:TreeGrafter.
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
//