Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P31677

- OTSA_ECOLI

UniProt

P31677 - OTSA_ECOLI

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

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

Gene

otsA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

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

Enzyme regulationi

Activated by potassium and other monovalent cations at 0.25 M. Partially inhibited at greater concentrations.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101Glucose-6-phosphate1 Publication
Binding sitei77 – 771Glucose-6-phosphate1 Publication
Sitei86 – 861Involved in alpha anomer selectivity
Binding sitei131 – 1311Glucose-6-phosphate1 Publication
Sitei156 – 1561Involved in alpha anomer selectivity
Binding sitei263 – 2631UDP-glucose1 Publication
Binding sitei268 – 2681UDP-glucose1 Publication
Binding sitei301 – 3011Glucose-6-phosphate1 Publication
Binding sitei340 – 3401UDP-glucose; via amide nitrogen and carbonyl oxygen1 Publication

GO - Molecular functioni

  1. alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity Source: EcoCyc

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: EcoliWiki
  2. response to osmotic stress Source: EcoCyc
  3. trehalose biosynthetic process Source: EcoCyc
  4. trehalose metabolism in response to cold stress Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Stress response

Keywords - Ligandi

Potassium

Enzyme and pathway databases

BioCyciEcoCyc:TREHALOSE6PSYN-MONOMER.
ECOL316407:JW5312-MONOMER.
MetaCyc:TREHALOSE6PSYN-MONOMER.
UniPathwayiUPA00299.

Protein family/group databases

CAZyiGT20. Glycosyltransferase Family 20.

Names & Taxonomyi

Protein namesi
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 namesi
Name:otsA
Ordered Locus Names:b1896, JW5312
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11751. otsA.

Pathology & Biotechi

Disruption phenotypei

Mutants are viable, but osmotically sensitive in minimal media and sensitive to cold shock.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed
Chaini2 – 474473Alpha,alpha-trehalose-phosphate synthase [UDP-forming]PRO_0000122489Add
BLAST

Proteomic databases

PaxDbiP31677.
PRIDEiP31677.

Expressioni

Inductioni

By cold-shock, osmotic-shock and during the transition to stationary phase. Expression is partially dependent on RpoS.4 Publications

Gene expression databases

GenevestigatoriP31677.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

DIPiDIP-10417N.
STRINGi511145.b1896.

Structurei

Secondary structure

1
474
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Helixi16 – 183Combined sources
Helixi23 – 3513Combined sources
Beta strandi37 – 4711Combined sources
Beta strandi54 – 585Combined sources
Beta strandi61 – 688Combined sources
Helixi70 – 767Combined sources
Turni77 – 793Combined sources
Helixi80 – 834Combined sources
Helixi85 – 895Combined sources
Helixi93 – 953Combined sources
Helixi100 – 11718Combined sources
Helixi118 – 1203Combined sources
Beta strandi126 – 1316Combined sources
Helixi132 – 1343Combined sources
Helixi137 – 1437Combined sources
Beta strandi150 – 1534Combined sources
Helixi161 – 1644Combined sources
Helixi170 – 1778Combined sources
Beta strandi180 – 1878Combined sources
Helixi188 – 20114Combined sources
Beta strandi204 – 2074Combined sources
Turni208 – 2103Combined sources
Beta strandi211 – 2144Combined sources
Beta strandi217 – 2237Combined sources
Helixi230 – 2389Combined sources
Helixi243 – 2519Combined sources
Turni252 – 2543Combined sources
Beta strandi256 – 2616Combined sources
Helixi266 – 2683Combined sources
Helixi270 – 28314Combined sources
Helixi285 – 2873Combined sources
Turni288 – 2903Combined sources
Beta strandi291 – 2966Combined sources
Helixi305 – 32521Combined sources
Beta strandi332 – 3365Combined sources
Helixi342 – 35110Combined sources
Beta strandi353 – 3575Combined sources
Beta strandi360 – 3634Combined sources
Helixi366 – 3749Combined sources
Beta strandi382 – 3865Combined sources
Helixi390 – 3934Combined sources
Beta strandi398 – 4014Combined sources
Helixi406 – 41712Combined sources
Helixi421 – 43717Combined sources
Helixi440 – 45314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GZ5X-ray2.43A/B/C/D2-457[»]
1UQTX-ray2.00A/B2-474[»]
1UQUX-ray2.00A/B2-474[»]
2WTXX-ray2.20A/B/C/D1-474[»]
ProteinModelPortaliP31677.
SMRiP31677. Positions 2-458.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31677.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni22 – 232UDP-glucose binding
Regioni366 – 3705UDP-glucose binding

Sequence similaritiesi

Belongs to the glycosyltransferase 20 family.Curated

Phylogenomic databases

eggNOGiCOG0380.
HOGENOMiHOG000191478.
InParanoidiP31677.
KOiK00697.
OMAiWGESFVK.
OrthoDBiEOG6CCH1M.
PhylomeDBiP31677.

Family and domain databases

InterProiIPR001830. Glyco_trans_20.
IPR012766. Trehalose_OtsA.
[Graphical view]
PfamiPF00982. Glyco_transf_20. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02400. trehalose_OtsA. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P31677-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSRLVVVSNR IAPPDEHAAS AGGLAVGILG ALKAAGGLWF GWSGETGNED
60 70 80 90 100
QPLKKVKKGN ITWASFNLSE QDLDEYYNQF SNAVLWPAFH YRLDLVQFQR
110 120 130 140 150
PAWDGYLRVN ALLADKLLPL LQDDDIIWIH DYHLLPFAHE LRKRGVNNRI
160 170 180 190 200
GFFLHIPFPT PEIFNALPTY DTLLEQLCDY DLLGFQTEND RLAFLDCLSN
210 220 230 240 250
LTRVTTRSAK SHTAWGKAFR TEVYPIGIEP KEIAKQAAGP LPPKLAQLKA
260 270 280 290 300
ELKNVQNIFS VERLDYSKGL PERFLAYEAL LEKYPQHHGK IRYTQIAPTS
310 320 330 340 350
RGDVQAYQDI RHQLENEAGR INGKYGQLGW TPLYYLNQHF DRKLLMKIFR
360 370 380 390 400
YSDVGLVTPL RDGMNLVAKE YVAAQDPANP GVLVLSQFAG AANELTSALI
410 420 430 440 450
VNPYDRDEVA AALDRALTMS LAERISRHAE MLDVIVKNDI NHWQECFISD
460 470
LKQIVPRSAE SQQRDKVATF PKLA
Length:474
Mass (Da):53,611
Last modified:January 23, 2007 - v3
Checksum:i63FFB6F938056F95
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69160 Genomic DNA. Translation: CAA48913.1.
U00096 Genomic DNA. Translation: AAC74966.1.
AP009048 Genomic DNA. Translation: BAA15717.2.
U27211 Genomic DNA. Translation: AAA68604.1.
PIRiI83402.
RefSeqiNP_416410.1. NC_000913.3.
YP_490157.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC74966; AAC74966; b1896.
BAA15717; BAA15717; BAA15717.
GeneIDi12930479.
946405.
KEGGiecj:Y75_p1871.
eco:b1896.
PATRICi32119119. VBIEscCol129921_1977.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X69160 Genomic DNA. Translation: CAA48913.1 .
U00096 Genomic DNA. Translation: AAC74966.1 .
AP009048 Genomic DNA. Translation: BAA15717.2 .
U27211 Genomic DNA. Translation: AAA68604.1 .
PIRi I83402.
RefSeqi NP_416410.1. NC_000913.3.
YP_490157.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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 2-474 [» ]
1UQU X-ray 2.00 A/B 2-474 [» ]
2WTX X-ray 2.20 A/B/C/D 1-474 [» ]
ProteinModelPortali P31677.
SMRi P31677. Positions 2-458.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10417N.
STRINGi 511145.b1896.

Protein family/group databases

CAZyi GT20. Glycosyltransferase Family 20.

Proteomic databases

PaxDbi P31677.
PRIDEi P31677.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC74966 ; AAC74966 ; b1896 .
BAA15717 ; BAA15717 ; BAA15717 .
GeneIDi 12930479.
946405.
KEGGi ecj:Y75_p1871.
eco:b1896.
PATRICi 32119119. VBIEscCol129921_1977.

Organism-specific databases

EchoBASEi EB1701.
EcoGenei EG11751. otsA.

Phylogenomic databases

eggNOGi COG0380.
HOGENOMi HOG000191478.
InParanoidi P31677.
KOi K00697.
OMAi WGESFVK.
OrthoDBi EOG6CCH1M.
PhylomeDBi P31677.

Enzyme and pathway databases

UniPathwayi UPA00299 .
BioCyci EcoCyc:TREHALOSE6PSYN-MONOMER.
ECOL316407:JW5312-MONOMER.
MetaCyc:TREHALOSE6PSYN-MONOMER.

Miscellaneous databases

EvolutionaryTracei P31677.
PROi P31677.

Gene expression databases

Genevestigatori P31677.

Family and domain databases

InterProi IPR001830. Glyco_trans_20.
IPR012766. Trehalose_OtsA.
[Graphical view ]
Pfami PF00982. Glyco_transf_20. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR02400. trehalose_OtsA. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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.

Entry informationi

Entry nameiOTSA_ECOLI
AccessioniPrimary (citable) accession number: P31677
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 121 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3