OTSB_SALTY
ID OTSB_SALTY Reviewed; 267 AA.
AC P0CL50; Q9L894;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Trehalose-phosphate phosphatase;
DE Short=TPP;
DE EC=3.1.3.12;
DE AltName: Full=Trehalose 6-phosphate phosphatase;
DE AltName: Full=Trehalose-phosphatase;
GN Name=otsB; OrderedLocusNames=STM1929;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(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; AE006468; AAL20845.1; -; Genomic_DNA.
DR RefSeq; NP_460886.1; NC_003197.2.
DR RefSeq; WP_000830111.1; NC_003197.2.
DR AlphaFoldDB; P0CL50; -.
DR SMR; P0CL50; -.
DR STRING; 99287.STM1929; -.
DR PaxDb; P0CL50; -.
DR EnsemblBacteria; AAL20845; AAL20845; STM1929.
DR GeneID; 1253450; -.
DR KEGG; stm:STM1929; -.
DR PATRIC; fig|99287.12.peg.2046; -.
DR HOGENOM; CLU_037265_2_0_6; -.
DR OMA; YGAERWD; -.
DR PhylomeDB; P0CL50; -.
DR BioCyc; SENT99287:STM1929-MON; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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; -; 1.
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; 1.
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..267
FT /note="Trehalose-phosphate phosphatase"
FT /id="PRO_0000058102"
FT ACT_SITE 20
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 20..22
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 20
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 22
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 267 AA; 29245 MW; 3F83A1DE81429A21 CRC64;
MAEPLTVSPE LTANYAYFFD LDGTLAEIKP HPDQVVVPHK ILQLLDRLAA HNAGALALIS
GRSMTELDAL AKPFRFPLAG VHGAERRDIN GKTHIVRLPE AVVREVEALL RSTLVALPGT
ELESKGMAFA LHYRQAPEHE AALLALAQHV TQHWPQLALQ PGKCVVEIKP KGTNKGEAIA
AFMQEAPFAG RIPVFVGDDL TDEAGFGVVN HAGGISVKVG VGATQAAWRL ESVPDVWRWL
EQINYPQQEQ QVMNNRRDGY ESFSRSI
