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P31677 (OTSA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha,alpha-trehalose-phosphate synthase [UDP-forming]

EC=2.4.1.15
Alternative name(s):
Osmoregulatory trehalose synthesis protein A
Trehalose-6-phosphate synthase
UDP-glucose-glucosephosphate glucosyltransferase
Gene names
Name:otsA
Ordered Locus Names:b1896, JW5312
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of glucose from UDP-glucose to glucose-6-phosphate to form alpha,alpha-1,1 trehalose-6-phosphate. Acts with retention of the anomeric configuration of the UDP-sugar donor. Essential for viability of the cells at low temperatures and at elevated osmotic strength. Ref.6 Ref.7 Ref.9

Catalytic activity

UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate.

Enzyme regulation

Activated by potassium and other monovalent cations at 0.25 M. Partially inhibited at greater concentrations. Ref.7

Pathway

Glycan biosynthesis; trehalose biosynthesis.

Subunit structure

Homotetramer. Ref.10

Induction

By cold-shock, osmotic-shock and during the transition to stationary phase. Expression is partially dependent on RpoS. Ref.6 Ref.7 Ref.8 Ref.9

Disruption phenotype

Mutants are viable, but osmotically sensitive in minimal media and sensitive to cold shock. Ref.7

Sequence similarities

Belongs to the glycosyltransferase 20 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 474473Alpha,alpha-trehalose-phosphate synthase [UDP-forming]
PRO_0000122489

Regions

Region22 – 232UDP-glucose binding
Region366 – 3705UDP-glucose binding

Sites

Binding site101Glucose-6-phosphate
Binding site771Glucose-6-phosphate
Binding site1311Glucose-6-phosphate
Binding site2631UDP-glucose
Binding site2681UDP-glucose
Binding site3011Glucose-6-phosphate
Binding site3401UDP-glucose; via amide nitrogen and carbonyl oxygen
Site861Involved in alpha anomer selectivity
Site1561Involved in alpha anomer selectivity

Secondary structure

................................................................................... 474
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31677 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 63FFB6F938056F95

FASTA47453,611
        10         20         30         40         50         60 
MSRLVVVSNR IAPPDEHAAS AGGLAVGILG ALKAAGGLWF GWSGETGNED QPLKKVKKGN 

        70         80         90        100        110        120 
ITWASFNLSE QDLDEYYNQF SNAVLWPAFH YRLDLVQFQR PAWDGYLRVN ALLADKLLPL 

       130        140        150        160        170        180 
LQDDDIIWIH DYHLLPFAHE LRKRGVNNRI GFFLHIPFPT PEIFNALPTY DTLLEQLCDY 

       190        200        210        220        230        240 
DLLGFQTEND RLAFLDCLSN LTRVTTRSAK SHTAWGKAFR TEVYPIGIEP KEIAKQAAGP 

       250        260        270        280        290        300 
LPPKLAQLKA ELKNVQNIFS VERLDYSKGL PERFLAYEAL LEKYPQHHGK IRYTQIAPTS 

       310        320        330        340        350        360 
RGDVQAYQDI RHQLENEAGR INGKYGQLGW TPLYYLNQHF DRKLLMKIFR YSDVGLVTPL 

       370        380        390        400        410        420 
RDGMNLVAKE YVAAQDPANP GVLVLSQFAG AANELTSALI VNPYDRDEVA AALDRALTMS 

       430        440        450        460        470 
LAERISRHAE MLDVIVKNDI NHWQECFISD LKQIVPRSAE SQQRDKVATF PKLA 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the otsBA operon for osmoregulatory trehalose synthesis in Escherichia coli and homology of the OtsA and OtsB proteins to the yeast trehalose-6-phosphate synthase/phosphatase complex."
Kaasen I., McDougall J., Stroem A.R.
Gene 145:9-15(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: K12 / CSH7.
[2]"A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map."
Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S. expand/collapse author list , Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:379-392(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]Estep P., O'Keeffe T., Robison K., Church G.M.
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 430-474.
Strain: K12 / EMG2.
[6]"Molecular cloning and physical mapping of the otsBA genes, which encode the osmoregulatory trehalose pathway of Escherichia coli: evidence that transcription is activated by katF (AppR)."
Kaasen I., Falkenberg P., Styrvold O.B., Strom A.R.
J. Bacteriol. 174:889-898(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A TREHALOSE-6-PHOSPHATE SYNTHASE, INDUCTION.
[7]"Biochemical and genetic characterization of osmoregulatory trehalose synthesis in Escherichia coli."
Giaever H.M., Styrvold O.B., Kaasen I., Stroem A.R.
J. Bacteriol. 170:2841-2849(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A TREHALOSE-6-PHOSPHATE SYNTHASE, ENZYME REGULATION, DISRUPTION PHENOTYPE, INDUCTION, NOMENCLATURE.
[8]"Trehalose synthesis genes are controlled by the putative sigma factor encoded by rpoS and are involved in stationary-phase thermotolerance in Escherichia coli."
Hengge-Aronis R., Klein W., Lange R., Rimmele M., Boos W.
J. Bacteriol. 173:7918-7924(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[9]"Trehalose synthesis is induced upon exposure of Escherichia coli to cold and is essential for viability at low temperatures."
Kandror O., DeLeon A., Goldberg A.L.
Proc. Natl. Acad. Sci. U.S.A. 99:9727-9732(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A TREHALOSE-6-PHOSPHATE SYNTHASE, INDUCTION.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[10]"Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA."
Gibson R.P., Turkenburg J.P., Charnock S.J., Lloyd R., Davies G.J.
Chem. Biol. 9:1337-1346(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) OF 1-457 IN COMPLEX WITH UDP AND GLUCOSE-6-PHOSPHATE, SUBUNIT.
[11]"The donor subsite of trehalose-6-phosphate synthase: binary complexes with UDP-glucose and UDP-2-deoxy-2-fluoro-glucose at 2 A resolution."
Gibson R.P., Tarling C.A., Roberts S., Withers S.G., Davies G.J.
J. Biol. Chem. 279:1950-1955(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEXES WITH UDP-GLUCOSE AND SUBSTRATE ANALOG.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X69160 Genomic DNA. Translation: CAA48913.1.
U00096 Genomic DNA. Translation: AAC74966.1.
AP009048 Genomic DNA. Translation: BAA15717.2.
U27211 Genomic DNA. Translation: AAA68604.1.
PIRI83402.
RefSeqNP_416410.1. NC_000913.3.
YP_490157.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GZ5X-ray2.43A/B/C/D2-457[»]
1UQTX-ray2.00A/B1-474[»]
1UQUX-ray2.00A/B1-474[»]
2WTXX-ray2.20A/B/C/D1-474[»]
ProteinModelPortalP31677.
SMRP31677. Positions 2-458.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10417N.
STRING511145.b1896.

Protein family/group databases

CAZyGT20. Glycosyltransferase Family 20.

Proteomic databases

PaxDbP31677.
PRIDEP31677.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74966; AAC74966; b1896.
BAA15717; BAA15717; BAA15717.
GeneID12930479.
946405.
KEGGecj:Y75_p1871.
eco:b1896.
PATRIC32119119. VBIEscCol129921_1977.

Organism-specific databases

EchoBASEEB1701.
EcoGeneEG11751. otsA.

Phylogenomic databases

eggNOGCOG0380.
HOGENOMHOG000191478.
KOK00697.
OMAIEFMPIH.
OrthoDBEOG6CCH1M.
PhylomeDBP31677.
ProtClustDBPRK10117.

Enzyme and pathway databases

BioCycEcoCyc:TREHALOSE6PSYN-MONOMER.
ECOL316407:JW5312-MONOMER.
MetaCyc:TREHALOSE6PSYN-MONOMER.
UniPathwayUPA00299.

Gene expression databases

GenevestigatorP31677.

Family and domain databases

InterProIPR001830. Glyco_trans_20.
IPR012766. Trehalose_OtsA.
[Graphical view]
PfamPF00982. Glyco_transf_20. 1 hit.
[Graphical view]
TIGRFAMsTIGR02400. trehalose_OtsA. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP31677.
PROP31677.

Entry information

Entry nameOTSA_ECOLI
AccessionPrimary (citable) accession number: P31677
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene