ID   A0Q111_CLONN            Unreviewed;       250 AA.
AC   A0Q111;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=NT01CX_2240 {ECO:0000313|EMBL:ABK60926.1};
OS   Clostridium novyi (strain NT).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=386415 {ECO:0000313|EMBL:ABK60926.1, ECO:0000313|Proteomes:UP000008220};
RN   [1] {ECO:0000313|EMBL:ABK60926.1, ECO:0000313|Proteomes:UP000008220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NT {ECO:0000313|EMBL:ABK60926.1,
RC   ECO:0000313|Proteomes:UP000008220};
RX   PubMed=17115055; DOI=10.1038/nbt1256;
RA   Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA   Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA   Zhou S.;
RT   "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT   NT.";
RL   Nat. Biotechnol. 24:1573-1580(2006).
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; CP000382; ABK60926.1; -; Genomic_DNA.
DR   RefSeq; WP_011722310.1; NC_008593.1.
DR   AlphaFoldDB; A0Q111; -.
DR   STRING; 386415.NT01CX_2240; -.
DR   KEGG; cno:NT01CX_2240; -.
DR   PATRIC; fig|386415.7.peg.1343; -.
DR   eggNOG; COG0631; Bacteria.
DR   HOGENOM; CLU_034545_4_1_9; -.
DR   Proteomes; UP000008220; 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:UP000008220}.
FT   DOMAIN          12..247
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   250 AA;  27824 MW;  C0A5044DDA17FBD4 CRC64;
     MNSSRIFTEK LCVGLLSDIG NVREINEDSI GKYENDEFAV YIVADGMGGH NAGDVASKIA
     VESCIEYIKR NRYLDDMERL LKESIKYANN NIYIKAENSE MLYGMGTTIT ACIVKQGKVV
     IANVGDSSCY IVTEENIEKI TKDHSLVQEL VDDGSITEEE AINHPNKNII TRALGTKKTV
     KIDTFSVDIS YNEKFVLCTD GLSNEVSKEE MYSIISQNTN QEACRLLVDL CKNKSGRDNI
     SVIIFGGMQK
//