ID   OTSB_MYCLE              Reviewed;         429 AA.
AC   Q49734; O08220;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Trehalose-phosphate phosphatase;
DE            Short=TPP;
DE            EC=3.1.3.12;
DE   AltName: Full=Trehalose-6-phosphate phosphatase;
GN   Name=otsB; OrderedLocusNames=ML0414; ORFNames=MLCL383.17c;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8446027; DOI=10.1111/j.1365-2958.1993.tb01111.x;
RA   Eiglmeier K., Honore N., Woods S.A., Caudron B., Cole S.T.;
RT   "Use of an ordered cosmid library to deduce the genomic organization of
RT   Mycobacterium leprae.";
RL   Mol. Microbiol. 7:197-206(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- FUNCTION: Removes the phosphate from trehalose 6-phosphate to produce
CC       free trehalose. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-
CC         trehalose + phosphate; Xref=Rhea:RHEA:23420, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16551, ChEBI:CHEBI:43474, ChEBI:CHEBI:58429; EC=3.1.3.12;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC   -!- SIMILARITY: Belongs to the trehalose phosphatase family. {ECO:0000305}.
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DR   EMBL; Z97179; CAB09930.1; -; Genomic_DNA.
DR   EMBL; U00015; AAC43238.1; -; Genomic_DNA.
DR   EMBL; AL583918; CAC29922.1; -; Genomic_DNA.
DR   PIR; S72829; S72829.
DR   RefSeq; NP_301392.1; NC_002677.1.
DR   RefSeq; WP_010907716.1; NC_002677.1.
DR   AlphaFoldDB; Q49734; -.
DR   SMR; Q49734; -.
DR   STRING; 272631.ML0414; -.
DR   EnsemblBacteria; CAC29922; CAC29922; CAC29922.
DR   KEGG; mle:ML0414; -.
DR   PATRIC; fig|272631.5.peg.704; -.
DR   Leproma; ML0414; -.
DR   eggNOG; COG0637; Bacteria.
DR   eggNOG; COG1877; Bacteria.
DR   HOGENOM; CLU_037265_4_1_11; -.
DR   OMA; HKLAKHP; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004805; F:trehalose-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1000; -; 2.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR044651; OTSB-like.
DR   InterPro; IPR003337; Trehalose_PPase.
DR   PANTHER; PTHR43768; PTHR43768; 1.
DR   Pfam; PF02358; Trehalose_PPase; 1.
DR   SUPFAM; SSF56784; SSF56784; 2.
DR   TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR   TIGRFAMs; TIGR00685; T6PP; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..429
FT                   /note="Trehalose-phosphate phosphatase"
FT                   /id="PRO_0000370703"
FT   ACT_SITE        181
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         181..183
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         368
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   429 AA;  45888 MW;  53F45D2A56516FA3 CRC64;
     MPVTIDPRRH SAALFDLDAV VTDTPLDSTV TLVRQLQGIG VGTAVFSTNR NSQGVLTATG
     LDHLFPVHVD GLASGKVTIL VAAANRLMAQ PGRCVVVAVD AAGITAARYG GFALVLGLVI
     GEDQTGHRDT LRNSGADTVV ADLGEVIVRT GDRRMSELPD ALQTLGLTDD LTARQPAVFF
     DFDGTLSDIV DDPDSARPVP GATEALQKLA THCPVAILSG RDLADVIKRI GVPGIWYSGS
     HGFESTAPDG THHQNDAAEA TIPILEQAAT QLRDQLGPIP GVMVEHKRFG VAVHYRNVAR
     DRVNEVAVAV RTAGQRNALR VTTGREVIEL RPDIDWDKGK TLHWVIDRLH HAGTQVGSAS
     LMPICLGDDI TDEDAFDAVR HTDVGGIPIV VRHTEDGNRA TAALFTLDSP MHVSEFTERL
     ARQLSDTQR