ID   OTSA_KLEP7              Reviewed;         474 AA.
AC   A6TB47;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=KPN78578_23570; ORFNames=KPN_02392;
OS   Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=272620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700721 / MGH 78578;
RG   The Klebsiella pneumonia Genome Sequencing Project;
RA   McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA   Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL   Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR77818.1; -; Genomic_DNA.
DR   RefSeq; WP_004175414.1; NC_009648.1.
DR   AlphaFoldDB; A6TB47; -.
DR   SMR; A6TB47; -.
DR   STRING; 272620.KPN_02392; -.
DR   CAZy; GT20; Glycosyltransferase Family 20.
DR   jPOST; A6TB47; -.
DR   PaxDb; 272620-KPN_02392; -.
DR   EnsemblBacteria; ABR77818; ABR77818; KPN_02392.
DR   KEGG; kpn:KPN_02392; -.
DR   HOGENOM; CLU_002351_7_1_6; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000000265; 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; Transferase.
FT   CHAIN           1..474
FT                   /note="Trehalose-6-phosphate synthase"
FT                   /id="PRO_0000348902"
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;  53813 MW;  B022E7320D3BBD79 CRC64;
     MSRLVVVSNR IALPDDKKSS AGGLAVGILG ALRAAGGLWF GWSGEIGDDQ QPLKQVSRGN
     ISWASFNLNE RDHDEYYNQF SNAVLWPAFH YRLDLVSFQR EAWEGYLRVN AMLADKLLPL
     IEPDDTLWIH DYHLLPFASE LRKRGVNNRI GFFLHIPFPT PEIFNALPPH AELLEQLCDY
     DLLGFQTESD RTAFLDSIAM QTRLSDLGDK RYQAWGKAFS TEVYPIGIDP DEITRNAKGP
     LPPKLAQLKN ELKNVKNIFS VERLDYSKGL PERFLAYETL LEKYPQHHGK IRYTQIAPTS
     RGDVQAYQDI RHQLETAAGR INGQFGQLGW TPLYYLNQHF DRKLLMKVFR YSDVGLVTPL
     RDGMNLVAKE YVAAQDPDNP GVLVLSQFAG AAQELTSALI VNPYDRDEVA AALDRALSMP
     LAERIARHSA MLDVIRENDI HNWQARFVED LQHISPRSEE SRLRGKIATF PKLA
//