ID   OTSB_MYCPA              Reviewed;         391 AA.
AC   Q73U90;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=MAP_3478;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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; AE016958; AAS06028.1; -; Genomic_DNA.
DR   RefSeq; WP_010949975.1; NC_002944.2.
DR   AlphaFoldDB; Q73U90; -.
DR   SMR; Q73U90; -.
DR   STRING; 262316.MAP_3478; -.
DR   EnsemblBacteria; AAS06028; AAS06028; MAP_3478.
DR   KEGG; mpa:MAP_3478; -.
DR   PATRIC; fig|262316.17.peg.3699; -.
DR   eggNOG; COG0637; Bacteria.
DR   eggNOG; COG1877; Bacteria.
DR   HOGENOM; CLU_037265_4_1_11; -.
DR   OMA; HKLAKHP; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000000580; 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..391
FT                   /note="Trehalose-phosphate phosphatase"
FT                   /id="PRO_0000370705"
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;  40426 MW;  C5E87D14599CC028 CRC64;
     MGESGPVVID PRRHDAVLFG VGDALGSALA SQLGQIGVGT AAFAADGPAA AADRLRVRPG
     RCVVVAGDPA AVEAARTAGF ALVIGLAPVG RDGDGLRGAG ADAVVAELEQ ITVRTGDRRM
     SQLPDASQAL TGGADGLAGR HPAVFFDFDG TLSDIVDDPD AARPVAGATA ALTRLAARCP
     VAVLSGRDLA DVTKRVGVLG IWYAGSHGFE LTAPDGSHHQ NDDAAAAIPV LAQAAGRLRD
     ELGAIPGVVV EHKRFGVAVH YRNAARDRVG EVAAAVRAAG RHDALRVTTG REVIELRPDL
     DWDKGKTLHW VIEHLRRSGS GALTPVYLGD DITDEDAFDA VRGGPVQGVP ILVRHNDDGD
     RATAALFALD SPARAAEFTE RLADQLERGE G