ID   Q895P7_CLOTE            Unreviewed;       269 AA.
AC   Q895P7;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=CTC_01224 {ECO:0000313|EMBL:AAO35793.1};
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO35793.1, ECO:0000313|Proteomes:UP000001412};
RN   [1] {ECO:0000313|EMBL:AAO35793.1, ECO:0000313|Proteomes:UP000001412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Massachusetts / E88 {ECO:0000313|Proteomes:UP000001412};
RX   PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA   Brueggemann H., Baumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I.,
RA   Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.;
RT   "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT   disease.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO35793.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q895P7; -.
DR   STRING; 212717.CTC_01224; -.
DR   KEGG; ctc:CTC_01224; -.
DR   HOGENOM; CLU_034545_4_2_9; -.
DR   Proteomes; UP000001412; 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:AAO35793.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001412}.
FT   DOMAIN          22..258
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   269 AA;  30127 MW;  DF40D45F3B87125F CRC64;
     MQPVDSFEED MLKIIVKRCK SMVGMITDVG NFRKINEDYV GYYIDETKEI YIVADGMGGH
     NAGEVASELA VNTVIEYLNN MEDTEDIDWQ LTKAIKKANE NIFKLACTKK EYEGMGTTIT
     AAFIKKEKIV VANVGDSSCY IIDKDDKILK VTKDHSLVQQ LIDNGSITEE EALIHPNKNV
     ITRALGTSDL VIVDTFLLDL KEIKKAILCT DGLTNDITPK EMYDIIITNN NENACRILLE
     SCKEKGGKDN ISVIVFEGEC SDDRHIARK
//