Reviewed, UniProtKB/Swiss-Prot P31677 (OTSA_ECOLI)

Names and origin

Protein names

Recommended name:
    Alpha,alpha-trehalose-phosphate synthase [UDP-forming]
    EC=2.4.1.15
Alternative name(s):
    Trehalose-6-phosphate synthase
    UDP-glucose-glucosephosphate glucosyltransferase
    Osmoregulatory trehalose synthesis protein A

Gene names

Name:	otsA
Ordered Locus Names:	b1896, JW5312

Organism

Escherichia coli (strain K12) [Complete 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
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.6
Pathway	Glycan biosynthesis; trehalose biosynthesis.
Subunit structure	Homotetramer. Ref.8
Induction	By cold-shock and osmotic-shock. Ref.6 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
Gene Ontology (GO)
Biological process	response to stress Inferred from electronic annotation. Source: UniProtKB-KW trehalose biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity Inferred from electronic annotation. Source: EC potassium ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 474

473

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

PRO_0000122489

Regions

Region

22 – 23

2

UDP-glucose binding

Region

366 – 370

5

UDP-glucose binding

Sites

Binding site

10

1

Glucose-6-phosphate

Binding site

77

1

Glucose-6-phosphate

Binding site

131

1

Glucose-6-phosphate

Binding site

263

1

UDP-glucose

Binding site

268

1

UDP-glucose

Binding site

301

1

Glucose-6-phosphate

Binding site

340

1

UDP-glucose; via amide nitrogen and carbonyl oxygen

Site

86

1

Involved in alpha anomer selectivity

Site

156

1

Involved in alpha anomer selectivity

Secondary structure

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474

Helix Strand Turn

Details...

Beta strand

4 – 7

4

Helix

16 – 18

3

Helix

23 – 35

13

Beta strand

37 – 47

11

Beta strand

54 – 58

5

Beta strand

61 – 68

8

Helix

70 – 76

7

Turn

77 – 79

3

Helix

80 – 83

4

Helix

85 – 89

5

Helix

93 – 95

3

Helix

100 – 117

18

Helix

118 – 120

3

Beta strand

126 – 131

6

Helix

132 – 134

3

Helix

137 – 143

7

Beta strand

150 – 153

4

Helix

161 – 164

4

Helix

170 – 177

8

Beta strand

180 – 187

8

Helix

188 – 201

14

Beta strand

204 – 208

5

Beta strand

211 – 214

4

Beta strand

217 – 223

7

Helix

230 – 238

9

Helix

243 – 251

9

Turn

252 – 254

3

Beta strand

255 – 261

7

Helix

266 – 268

3

Helix

270 – 283

14

Helix

285 – 287

3

Turn

288 – 290

3

Beta strand

291 – 296

6

Helix

305 – 325

21

Beta strand

332 – 336

5

Helix

342 – 351

10

Beta strand

353 – 357

5

Beta strand

360 – 363

4

Helix

366 – 374

9

Beta strand

382 – 386

5

Helix

390 – 393

4

Beta strand

398 – 401

4

Helix

406 – 417

12

Helix

421 – 437

17

Helix

440 – 452

13

Sequences

	Sequence		Length	Mass (Da)
	P31677-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 63FFB6F938056F95	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

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: 8045430] [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. , 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: 9097040] [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: 9278503] [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: 16738553] [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]	"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: 3131312] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, INDUCTION.
[7]	"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: 12105274] [Abstract] Cited for: FUNCTION, INDUCTION. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[8]	"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: 12498887] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) OF 1-457 IN COMPLEX WITH UDP AND GLUCOSE-6-PHOSPHATE, SUBUNIT.
[9]	"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: 14570926] [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

EMBLGenBankDDBJ

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

AP_002515.1.
NP_416410.1.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein family/group databases

CAZy

GT20. Glycosyltransferase Family 20.

Genome annotation databases

GeneID

946405.

GenomeReviews

Gene locus JW5312 in contig AP009048_GR.
Gene locus b1896 in contig U00096_GR.

KEGG

ecj:JW5312.
eco:b1896.

Organism-specific databases

EchoBASE

EB1701.

EcoGene

EG11751. otsA.

CMR

Search...

Phylogenomic databases

HOGENOM

P31677.

OMA

P31677. MAGYFRV.

Enzyme and pathway databases

BioCyc

EcoCyc:TREHALOSE6PSYN-MON.
MetaCyc:TREHALOSE6PSYN-MON.

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...

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:	June 16, 2009
This is version 75 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)