ID   OTSA_ECO24              Reviewed;         474 AA.
AC   A7ZN22;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
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};
GN   OrderedLocusNames=EcE24377A_2128;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
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; CP000800; ABV19268.1; -; Genomic_DNA.
DR   RefSeq; WP_001295646.1; NC_009801.1.
DR   AlphaFoldDB; A7ZN22; -.
DR   SMR; A7ZN22; -.
DR   CAZy; GT20; Glycosyltransferase Family 20.
DR   GeneID; 75202700; -.
DR   KEGG; ecw:EcE24377A_2128; -.
DR   HOGENOM; CLU_002351_7_1_6; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000001122; Chromosome.
DR   GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd03788; GT20_TPS; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR001830; Glyco_trans_20.
DR   InterPro; IPR012766; Trehalose_OtsA.
DR   NCBIfam; TIGR02400; trehalose_OtsA; 1.
DR   PANTHER; PTHR10788:SF106; BCDNA.GH08860; 1.
DR   PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00982; Glyco_transf_20; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..474
FT                   /note="Trehalose-6-phosphate synthase"
FT                   /id="PRO_0000348897"
FT   BINDING         10
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         22..23
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         77
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         131
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         263
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         268
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         301
FT                   /ligand="D-glucose 6-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:61548"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         340
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   BINDING         366..370
FT                   /ligand="UDP-alpha-D-glucose"
FT                   /ligand_id="ChEBI:CHEBI:58885"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   SITE            86
FT                   /note="Involved in alpha anomer selectivity"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
FT   SITE            156
FT                   /note="Involved in alpha anomer selectivity"
FT                   /evidence="ECO:0000250|UniProtKB:P31677"
SQ   SEQUENCE   474 AA;  53611 MW;  63FFB6F938056F95 CRC64;
     MSRLVVVSNR IAPPDEHAAS AGGLAVGILG ALKAAGGLWF GWSGETGNED QPLKKVKKGN
     ITWASFNLSE QDLDEYYNQF SNAVLWPAFH YRLDLVQFQR PAWDGYLRVN ALLADKLLPL
     LQDDDIIWIH DYHLLPFAHE LRKRGVNNRI GFFLHIPFPT PEIFNALPTY DTLLEQLCDY
     DLLGFQTEND RLAFLDCLSN LTRVTTRSAK SHTAWGKAFR TEVYPIGIEP KEIAKQAAGP
     LPPKLAQLKA ELKNVQNIFS VERLDYSKGL PERFLAYEAL LEKYPQHHGK IRYTQIAPTS
     RGDVQAYQDI RHQLENEAGR INGKYGQLGW TPLYYLNQHF DRKLLMKIFR YSDVGLVTPL
     RDGMNLVAKE YVAAQDPANP GVLVLSQFAG AANELTSALI VNPYDRDEVA AALDRALTMS
     LAERISRHAE MLDVIVKNDI NHWQECFISD LKQIVPRSAE SQQRDKVATF PKLA
//