ID   OTSB_MYCTA              Reviewed;         391 AA.
AC   A5U846;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=MRA_3412;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
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; CP000611; ABQ75196.1; -; Genomic_DNA.
DR   RefSeq; WP_003417892.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U846; -.
DR   SMR; A5U846; -.
DR   STRING; 419947.MRA_3412; -.
DR   EnsemblBacteria; ABQ75196; ABQ75196; MRA_3412.
DR   KEGG; mra:MRA_3412; -.
DR   eggNOG; COG0561; Bacteria.
DR   eggNOG; COG0637; Bacteria.
DR   HOGENOM; CLU_037265_4_1_11; -.
DR   OMA; HKLAKHP; -.
DR   OrthoDB; 1374424at2; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000001988; 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.
FT   CHAIN           1..391
FT                   /note="Trehalose-phosphate phosphatase"
FT                   /id="PRO_0000370707"
FT   ACT_SITE        147
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         147..149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         147
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         330
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   391 AA;  41720 MW;  87AAC490926F9187 CRC64;
     MRKLGPVTID PRRHDAVLFD TTLDATQELV RQLQEVGVGT GVFGSGLDVP IVAAGRLAVR
     PGRCVVVSAH SAGVTAARES GFALIIGVDR TGCRDALRRD GADTVVTDLS EVSVRTGDRR
     MSQLPDALQA LGLADGLVAR QPAVFFDFDG TLSDIVEDPD AAWLAPGALE ALQKLAARCP
     IAVLSGRDLA DVTQRVGLPG IWYAGSHGFE LTAPDGTHHQ NDAAAAAIPV LKQAAAELRQ
     QLGPFPGVVV EHKRFGVAVH YRNAARDRVG EVAAAVRTAE QRHALRVTTG REVIELRPDV
     DWDKGKTLLW VLDHLPHSGS APLVPIYLGD DITDEDAFDV VGPHGVPIVV RHTDDGDRAT
     AALFALDSPA RVAEFTDRLA RQLREAPLRA T