OTSA_SALTY
ID OTSA_SALTY Reviewed; 473 AA.
AC P0CL06; P0A1Q0; Q9L893;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 1.
DT 03-AUG-2022, entry version 53.
DE RecName: Full=Trehalose-6-phosphate synthase {ECO:0000250|UniProtKB:P31677};
DE Short=TPS {ECO:0000250|UniProtKB:P31677};
DE EC=2.4.1.15 {ECO:0000250|UniProtKB:P31677};
DE AltName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] {ECO:0000250|UniProtKB:P31677};
DE AltName: Full=Osmoregulatory trehalose synthesis protein A {ECO:0000250|UniProtKB:P31677};
DE Short=OtsA {ECO:0000250|UniProtKB:P31677};
DE AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase {ECO:0000250|UniProtKB:P31677};
GN Name=otsA {ECO:0000250|UniProtKB:P31677}; OrderedLocusNames=STM1928;
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: Probably involved in the osmoprotection via the biosynthesis
CC of trehalose. Catalyzes the transfer of glucose from UDP-alpha-D-
CC glucose (UDP-Glc) to D-glucose 6-phosphate (Glc-6-P) to form trehalose-
CC 6-phosphate. Acts with retention of the anomeric configuration of the
CC UDP-sugar donor. {ECO:0000250|UniProtKB:P31677}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-
CC trehalose 6-phosphate + H(+) + UDP; Xref=Rhea:RHEA:18889,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58429,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:61548; EC=2.4.1.15;
CC Evidence={ECO:0000250|UniProtKB:P31677};
CC -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC {ECO:0000250|UniProtKB:P31677}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P31677}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC {ECO:0000250|UniProtKB:P31677}.
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DR EMBL; AE006468; AAL20844.1; -; Genomic_DNA.
DR RefSeq; NP_460885.1; NC_003197.2.
DR RefSeq; WP_000089042.1; NC_003197.2.
DR AlphaFoldDB; P0CL06; -.
DR SMR; P0CL06; -.
DR STRING; 99287.STM1928; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR PaxDb; P0CL06; -.
DR EnsemblBacteria; AAL20844; AAL20844; STM1928.
DR GeneID; 1253449; -.
DR KEGG; stm:STM1928; -.
DR PATRIC; fig|99287.12.peg.2045; -.
DR HOGENOM; CLU_002351_7_1_6; -.
DR OMA; YYGFSNR; -.
DR PhylomeDB; P0CL06; -.
DR BioCyc; SENT99287:STM1928-MON; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IBA:GO_Central.
DR GO; GO:0005992; P:trehalose biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03788; GT20_TPS; 1.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR012766; Trehalose_OtsA.
DR PANTHER; PTHR10788; PTHR10788; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR TIGRFAMs; TIGR02400; trehalose_OtsA; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..473
FT /note="Trehalose-6-phosphate synthase"
FT /id="PRO_0000122493"
FT REGION 454..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 10
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 21..22
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 76
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 130
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 262
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 267
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 300
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 339
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 365..369
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT SITE 85
FT /note="Involved in alpha anomer selectivity"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT SITE 155
FT /note="Involved in alpha anomer selectivity"
FT /evidence="ECO:0000250|UniProtKB:P31677"
SQ SEQUENCE 473 AA; 53581 MW; E85B3F0AE58E144A CRC64;
MSRLVVVSNR IAPPDNKGGA GGLAVGVLGA LKAAGGLWFG WSGETGNEDE PLKKVTKGNI
TWASFNLSEQ DYEDYYCQFS NAVLWPAFHY RLDLVQFQRP AWEGYMRVNA LLADKLLPLI
KENDIIWVHD YHLLPFASEL RKRGVNNRIG FFLHIPFPTP EIFNALPPHD ELLEQLCDFD
LLGFQTENDR LAFLDSLSSQ TRVTTRSGKQ HIAWGKDFQT EVYPIGIEPD EIALQAAGPL
PPKLAQLKAE LKNVKNIFSV ERLDYSKGLP ERFLAYEALL ENYPQHRGKI RYTQIAPTSR
GEVQAYQDIR HQLETEAGRI NGKYGQLGWT PLYYLNQHFD RKLLMKIFRY SDVGLVTPLR
DGMNLVAKEF VAAQDPANPG VLVLSQFAGA ANELTSALIV NPYDRDDVAA ALNRALTMPL
AERISRHAEM LDVIVKNDIN RWQERFIHDL KEVTPRSPER QQQNNVATFP KLA
