ID   Y1129_BACHK             Reviewed;         172 AA.
AC   Q6HLV6;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Putative phosphoesterase BT9727_1129 {ECO:0000255|HAMAP-Rule:MF_01444};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01444};
GN   OrderedLocusNames=BT9727_1129;
OS   Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=281309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=97-27;
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., Bruce D.,
RA   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   Hill K.K., Hitchcock P., Jackson P.J., Keim P., Kewalramani A.R.,
RA   Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M.,
RA   Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B.,
RA   Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R.,
RA   Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   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   -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. YjcG family.
CC       {ECO:0000255|HAMAP-Rule:MF_01444}.
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DR   EMBL; AE017355; AAT62699.1; -; Genomic_DNA.
DR   RefSeq; WP_000765876.1; NC_005957.1.
DR   RefSeq; YP_035465.1; NC_005957.1.
DR   AlphaFoldDB; Q6HLV6; -.
DR   SMR; Q6HLV6; -.
DR   EnsemblBacteria; AAT62699; AAT62699; BT9727_1129.
DR   GeneID; 64200086; -.
DR   KEGG; btk:BT9727_1129; -.
DR   PATRIC; fig|281309.8.peg.1188; -.
DR   HOGENOM; CLU_132020_0_0_9; -.
DR   OMA; RELQFPY; -.
DR   Proteomes; UP000001301; Chromosome.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01444; 2H_phosphoesterase_YjcG; 1.
DR   InterPro; IPR009097; Cyclic_Pdiesterase.
DR   InterPro; IPR022932; YjcG.
DR   SUPFAM; SSF55144; SSF55144; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..172
FT                   /note="Putative phosphoesterase BT9727_1129"
FT                   /id="PRO_0000299333"
FT   MOTIF           34..37
FT                   /note="HXTX 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01444"
FT   MOTIF           115..118
FT                   /note="HXTX 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01444"
FT   ACT_SITE        34
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01444"
FT   ACT_SITE        115
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01444"
SQ   SEQUENCE   172 AA;  19878 MW;  972A3914A31F4817 CRC64;
     MKLGIVIFPS KMIQDKANGL RKRYDPHYAL VPPHITLKTP FETQDEQLES IVNELHTIAS
     KTNPFTLHVG KVGSFAPVNN VIYFKVEKTP ELTFLNEEMH SGFFTQEREY AFVPHLTIGQ
     GLSDAEHADV LGRLRMKDFY YEQPIDRFHL LYQLENGTWT VHETFRLGKG NN