ID   Q6HEV2_BACHK            Unreviewed;       250 AA.
AC   Q6HEV2;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE            EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN   OrderedLocusNames=BT9727_3604 {ECO:0000313|EMBL:AAT61110.1};
OS   Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=281309 {ECO:0000313|EMBL:AAT61110.1, ECO:0000313|Proteomes:UP000001301};
RN   [1] {ECO:0000313|EMBL:AAT61110.1, ECO:0000313|Proteomes:UP000001301}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27 {ECO:0000313|EMBL:AAT61110.1,
RC   ECO:0000313|Proteomes:UP000001301};
RX   PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Brown N.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA   Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA   Green L.D., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA   Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T.,
RA   Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E.,
RA   Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA   Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(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; AE017355; AAT61110.1; -; Genomic_DNA.
DR   RefSeq; WP_000648699.1; NC_005957.1.
DR   RefSeq; YP_037924.1; NC_005957.1.
DR   AlphaFoldDB; Q6HEV2; -.
DR   GeneID; 45023692; -.
DR   KEGG; btk:BT9727_3604; -.
DR   PATRIC; fig|281309.8.peg.3842; -.
DR   HOGENOM; CLU_034545_4_1_9; -.
DR   Proteomes; UP000001301; 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   Hydrolase {ECO:0000313|EMBL:AAT61110.1}.
FT   DOMAIN          2..242
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
SQ   SEQUENCE   250 AA;  27815 MW;  A2B87A98E307A09A CRC64;
     MKAVFLSDKG KVRQHNEDSA GVFHNLDGNI LAVVADGMGG HRAGDVASSM TIQLFHDYWK
     QTHNMNEPKK VEEWLHTSVG IINERIYEYS KQHVECNGMG TTLIIAICTP SFVTIGHIGD
     SRCYMVSEGE ISLVTEDHSL VNELVRHGEI SKEDAEYHPK KNVLLRALGT EERVGLDVKT
     LVLEEDDQLL LCSDGLSNKV SIADMQQILQ LNEQLETKGQ RLIQLANDRG GEDNITLVLI
     DYAGSTNESR
//