Skip Header

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

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

Gene

otsA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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: trehalose biosynthesis

This protein is involved in the pathway trehalose biosynthesis, which is part of Glycan biosynthesis.
View all proteins of this organism that are known to be involved in the pathway trehalose biosynthesis and in Glycan biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei10Glucose-6-phosphate1 Publication1
Binding sitei77Glucose-6-phosphate1 Publication1
Sitei86Involved in alpha anomer selectivity1
Binding sitei131Glucose-6-phosphate1 Publication1
Sitei156Involved in alpha anomer selectivity1
Binding sitei263UDP-glucose1 Publication1
Binding sitei268UDP-glucose1 Publication1
Binding sitei301Glucose-6-phosphate1 Publication1
Binding sitei340UDP-glucose; via amide nitrogen and carbonyl oxygen1 Publication1

GO - Molecular functioni

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • response to osmotic stress Source: EcoCyc
  • trehalose biosynthetic process Source: EcoCyc
  • 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11751. otsA.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

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)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00001224892 – 474Alpha,alpha-trehalose-phosphate synthase [UDP-forming]Add BLAST473

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

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

BioGridi4259473. 8 interactors.
DIPiDIP-10417N.
STRINGi511145.b1896.

Structurei

Secondary structure

1474
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 10Combined sources7
Helixi16 – 18Combined sources3
Helixi23 – 35Combined sources13
Beta strandi37 – 47Combined sources11
Beta strandi54 – 58Combined sources5
Beta strandi61 – 68Combined sources8
Helixi70 – 76Combined sources7
Turni77 – 79Combined sources3
Helixi80 – 83Combined sources4
Helixi85 – 89Combined sources5
Helixi93 – 95Combined sources3
Helixi100 – 117Combined sources18
Helixi118 – 120Combined sources3
Beta strandi126 – 131Combined sources6
Helixi132 – 134Combined sources3
Helixi137 – 143Combined sources7
Beta strandi150 – 153Combined sources4
Helixi161 – 164Combined sources4
Helixi170 – 177Combined sources8
Beta strandi180 – 187Combined sources8
Helixi188 – 201Combined sources14
Beta strandi204 – 207Combined sources4
Turni208 – 210Combined sources3
Beta strandi211 – 214Combined sources4
Beta strandi217 – 223Combined sources7
Helixi230 – 238Combined sources9
Helixi243 – 251Combined sources9
Turni252 – 254Combined sources3
Beta strandi256 – 261Combined sources6
Helixi266 – 268Combined sources3
Helixi270 – 283Combined sources14
Helixi285 – 287Combined sources3
Turni288 – 290Combined sources3
Beta strandi291 – 296Combined sources6
Helixi305 – 325Combined sources21
Beta strandi332 – 336Combined sources5
Helixi342 – 351Combined sources10
Beta strandi353 – 357Combined sources5
Beta strandi360 – 363Combined sources4
Helixi366 – 374Combined sources9
Beta strandi382 – 386Combined sources5
Helixi390 – 393Combined sources4
Beta strandi398 – 401Combined sources4
Helixi406 – 417Combined sources12
Helixi421 – 437Combined sources17
Helixi440 – 453Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31677.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni22 – 23UDP-glucose binding2
Regioni366 – 370UDP-glucose binding5

Sequence similaritiesi

Belongs to the glycosyltransferase 20 family.Curated

Phylogenomic databases

eggNOGiENOG4105C1K. Bacteria.
COG0380. LUCA.
HOGENOMiHOG000191478.
InParanoidiP31677.
KOiK00697.
OMAiIEFMPIH.
PhylomeDBiP31677.

Family and domain databases

CDDicd03788. GT1_TPS. 1 hit.
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.
WP_001295646.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74966; AAC74966; b1896.
BAA15717; BAA15717; BAA15717.
GeneIDi946405.
KEGGiecj:JW5312.
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.
PIRiI83402.
RefSeqiNP_416410.1. NC_000913.3.
WP_001295646.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259473. 8 interactors.
DIPiDIP-10417N.
STRINGi511145.b1896.

Protein family/group databases

CAZyiGT20. Glycosyltransferase Family 20.

Proteomic databases

PaxDbiP31677.
PRIDEiP31677.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74966; AAC74966; b1896.
BAA15717; BAA15717; BAA15717.
GeneIDi946405.
KEGGiecj:JW5312.
eco:b1896.
PATRICi32119119. VBIEscCol129921_1977.

Organism-specific databases

EchoBASEiEB1701.
EcoGeneiEG11751. otsA.

Phylogenomic databases

eggNOGiENOG4105C1K. Bacteria.
COG0380. LUCA.
HOGENOMiHOG000191478.
InParanoidiP31677.
KOiK00697.
OMAiIEFMPIH.
PhylomeDBiP31677.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP31677.
PROiP31677.

Family and domain databases

CDDicd03788. GT1_TPS. 1 hit.
InterProiIPR001830. Glyco_trans_20.
IPR012766. Trehalose_OtsA.
[Graphical view]
PfamiPF00982. Glyco_transf_20. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02400. trehalose_OtsA. 1 hit.
ProtoNetiSearch...

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 2, 2016
This is version 133 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.