Alpha,alpha-trehalose-phosphate synthase [UDP-forming]

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P31677 (OTSA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 111. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	474 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Stress response
Ligand	Potassium
Molecular function	Glycosyltransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	response to DNA damage stimulus Inferred from expression pattern PubMed 11967071. Source: EcoliWiki response to osmotic stress Inferred from mutant phenotype Ref.7. Source: EcoCyc trehalose biosynthetic process Inferred from mutant phenotype Ref.7 PubMed 8837441. Source: EcoCyc trehalose metabolism in response to cold stress Inferred from expression pattern Ref.9. Source: EcoCyc
Molecular_function	alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity Inferred from direct assay Ref.7. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 474

473

Alpha,alpha-trehalose-phosphate synthase [UDP-forming]

PRO_0000122489

Regions

Region

22 – 23

UDP-glucose binding

Region

366 – 370

UDP-glucose binding

Sites

Binding site

Glucose-6-phosphate

Binding site

Glucose-6-phosphate

Binding site

131

Glucose-6-phosphate

Binding site

263

UDP-glucose

Binding site

268

UDP-glucose

Binding site

301

Glucose-6-phosphate

Binding site

340

UDP-glucose; via amide nitrogen and carbonyl oxygen

Site

Involved in alpha anomer selectivity

Site

156

Involved in alpha anomer selectivity

Secondary structure

474

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P31677 [UniParc].

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

474

53,611

        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' referencesShow '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. 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 277:1453-1474(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.

PIR

I83402.

RefSeq

NP_416410.1. NC_000913.2.
YP_490157.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GZ5	X-ray	2.43	A/B/C/D	2-457	[»]
1UQT	X-ray	2.00	A/B	1-474	[»]
1UQU	X-ray	2.00	A/B	1-474	[»]
2WTX	X-ray	2.20	A/B/C/D	1-474	[»]

ProteinModelPortal

P31677.

SMR

P31677. Positions 2-458.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10417N.

STRING

511145.b1896.

Protein family/group databases

CAZy

GT20. Glycosyltransferase Family 20.

Proteomic databases

PaxDb

P31677.

PRIDE

P31677.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC74966; AAC74966; b1896.
BAA15717; BAA15717; BAA15717.

GeneID

12930479.
946405.

KEGG

ecj:Y75_p1871.
eco:b1896.

PATRIC

32119119. VBIEscCol129921_1977.

Organism-specific databases

EchoBASE

EB1701.

EcoGene

EG11751. otsA.

Phylogenomic databases

eggNOG

COG0380.

HOGENOM

HOG000191478.

K00697.

OMA

EYGRKEM.

ProtClustDB

PRK10117.

Enzyme and pathway databases

BioCyc

EcoCyc:TREHALOSE6PSYN-MONOMER.
ECOL316407:JW5312-MONOMER.
MetaCyc:TREHALOSE6PSYN-MONOMER.

UniPathway

UPA00299.

Gene expression databases

Genevestigator

P31677.

Family and domain databases

InterPro

IPR001830. Glyco_trans_20.
IPR012766. Trehalose_OtsA.
[Graphical view]

Pfam

PF00982. Glyco_transf_20. 1 hit.
[Graphical view]

TIGRFAMs

TIGR02400. trehalose_OtsA. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

P31677.

Entry information

Entry name

OTSA_ECOLI

Accession

Primary (citable) accession number: P31677

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 111 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents