ID   OTSB_MYCMM              Reviewed;         390 AA.
AC   B2HDP8;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=MMAR_1156;
OS   Mycobacterium marinum (strain ATCC BAA-535 / M).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=216594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-535 / M;
RX   PubMed=18403782; DOI=10.1101/gr.075069.107;
RA   Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
RA   Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C.,
RA   Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K.,
RA   Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
RA   Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L., Brosch R.,
RA   Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
RT   "Insights from the complete genome sequence of Mycobacterium marinum on the
RT   evolution of Mycobacterium tuberculosis.";
RL   Genome Res. 18:729-741(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; CP000854; ACC39614.1; -; Genomic_DNA.
DR   RefSeq; WP_012393039.1; NC_010612.1.
DR   AlphaFoldDB; B2HDP8; -.
DR   SMR; B2HDP8; -.
DR   STRING; 216594.MMAR_1156; -.
DR   EnsemblBacteria; ACC39614; ACC39614; MMAR_1156.
DR   GeneID; 64259899; -.
DR   KEGG; mmi:MMAR_1156; -.
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; UP000001190; 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..390
FT                   /note="Trehalose-phosphate phosphatase"
FT                   /id="PRO_0000370704"
FT   ACT_SITE        150
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         150..152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         152
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         333
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   390 AA;  41049 MW;  726AABDE7F87F30D CRC64;
     MSVTIDPRRH DAVLFDTALN STQALVRQLQ QARVGTATFA SGGGGHDAAI QALTESADRV
     GARPGRCVVI TADAASVAAA RDSGFALVIG VDQAGHRDAL PDHGADTVLA DLDEVRVRAG
     DRHMSELPDA LQALGRPDGL TVPRPAVFFD FDGTLSEIVD DPDAATPTAG AVAALQQLAA
     QCPVAILSGR DLADVSQRVG LPGIWYAGSH GFELTAPDGT HHQNEAAAAA IPVLEQAAAQ
     LRDRLGSIPG VMVEHKRFGV ATHYRNAARD RVGEIAAVVR AAGQRDGLRV TTGREVIELR
     PDIDWDKGKT LRWVIDHLPD QRAAPLVPIY LGDDITDEDA FDAVGPNGVA IMVRHNEDGD
     RATAALFALE SPARVAEFTG RLASQLSTLG