OTSA_ECOHS
ID OTSA_ECOHS Reviewed; 474 AA.
AC A8A1A0;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=EcHS_A1993;
OS Escherichia coli O9:H4 (strain HS).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=331112;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000802; ABV06304.1; -; Genomic_DNA.
DR RefSeq; WP_012135897.1; NC_009800.1.
DR AlphaFoldDB; A8A1A0; -.
DR SMR; A8A1A0; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR KEGG; ecx:EcHS_A1993; -.
DR HOGENOM; CLU_002351_7_1_6; -.
DR OMA; YYGFSNR; -.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000001123; 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 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; Transferase.
FT CHAIN 1..474
FT /note="Trehalose-6-phosphate synthase"
FT /id="PRO_0000348901"
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; 53639 MW; BD24A47FBC18E613 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 PERFLAYEVL LEKYPQHHGK IRYTQIAPTS
RGDVQAYQDI RHQLENEAGR INGKYGQLGW TPLYYLNQHF DRKLLMKIFR YSDVGLVTPL
RDGMNLVAKE YVAAQDPANP GVLVLSQFAG AANELTSALI VNPYDRDEVA AALDRALTMS
LAERISRHAE MLDVIVKNDI NHWQECFISD LKQIVPRSAE SQQRDKVATF PKLA
