ID   OTSA_ECOK1              Reviewed;         474 AA.
AC   A1AC53;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   24-JAN-2024, entry version 83.
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=Ecok1_17490; ORFNames=APECO1_942;
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17293413; DOI=10.1128/jb.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P., Johnson S.J.,
RA   Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R., Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain O1:K1:H7
RT   shares strong similarities with human extraintestinal pathogenic E. coli
RT   genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABJ01243.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000468; ABJ01243.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_001332091.1; NZ_CADILS010000028.1.
DR   AlphaFoldDB; A1AC53; -.
DR   SMR; A1AC53; -.
DR   CAZy; GT20; Glycosyltransferase Family 20.
DR   KEGG; ecv:APECO1_942; -.
DR   HOGENOM; CLU_002351_7_1_6; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000008216; 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_0000348898"
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;  53542 MW;  985E5C0D63C6DE8E CRC64;
     MSRLVVVSNR IAPPDEHAAS AGGLAVGILG ALKAAGGLWF GWSGETGNED QPLKKVKKGN
     ITWASFNLSE QDLDEYYNKF SNAVLWPAFH YRLDLVQFQR PAWDGYLRVN ALLADKLLPL
     LQDDDIIWIH DYHLLPFAHE LRKRGVNNRI GFFLHIPFPT PEIFNALPTY DTLLEQLCEY
     DLLGFQTEND RLAFLDCLSN LTRVTTRSAK SHTACGKAFR 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
//