CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006009
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 
Protein Synonyms/Alias
 Osmoregulatory trehalose synthesis protein A; Trehalose-6-phosphate synthase; UDP-glucose-glucosephosphate glucosyltransferase 
Gene Name
 otsA 
Gene Synonyms/Alias
 b1896; JW5312 
Created Date
 July 27, 2013 
Organism
 Escherichia coli (strain K12) 
NCBI Taxa ID
 83333 
Lysine Modification
Position
Peptide
Type
References
217KSHTAWGKAFRTEVYacetylation[1]
231YPIGIEPKEIAKQAAacetylation[1]
235IEPKEIAKQAAGPLPacetylation[1]
244AAGPLPPKLAQLKAEacetylation[1]
249PPKLAQLKAELKNVQacetylation[1]
253AQLKAELKNVQNIFSacetylation[1]
268VERLDYSKGLPERFLacetylation[1]
283AYEALLEKYPQHHGKacetylation[1]
324EAGRINGKYGQLGWTacetylation[1]
347FDRKLLMKIFRYSDVacetylation[1]
452ECFISDLKQIVPRSAacetylation[1]
472DKVATFPKLA*****acetylation[1]
Reference
 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618] 
Functional Description
 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. 
Sequence Annotation
 REGION 22 23 UDP-glucose binding.
 REGION 366 370 UDP-glucose binding.
 BINDING 10 10 Glucose-6-phosphate.
 BINDING 77 77 Glucose-6-phosphate.
 BINDING 131 131 Glucose-6-phosphate.
 BINDING 263 263 UDP-glucose.
 BINDING 268 268 UDP-glucose.
 BINDING 301 301 Glucose-6-phosphate.
 BINDING 340 340 UDP-glucose; via amide nitrogen and  
Keyword
 3D-structure; Complete proteome; Direct protein sequencing; Glycosyltransferase; Potassium; Reference proteome; Stress response; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 474 AA 
Protein Sequence
MSRLVVVSNR IAPPDEHAAS AGGLAVGILG ALKAAGGLWF GWSGETGNED QPLKKVKKGN 60
ITWASFNLSE QDLDEYYNQF SNAVLWPAFH YRLDLVQFQR PAWDGYLRVN ALLADKLLPL 120
LQDDDIIWIH DYHLLPFAHE LRKRGVNNRI GFFLHIPFPT PEIFNALPTY DTLLEQLCDY 180
DLLGFQTEND RLAFLDCLSN LTRVTTRSAK SHTAWGKAFR TEVYPIGIEP KEIAKQAAGP 240
LPPKLAQLKA ELKNVQNIFS VERLDYSKGL PERFLAYEAL LEKYPQHHGK IRYTQIAPTS 300
RGDVQAYQDI RHQLENEAGR INGKYGQLGW TPLYYLNQHF DRKLLMKIFR YSDVGLVTPL 360
RDGMNLVAKE YVAAQDPANP GVLVLSQFAG AANELTSALI VNPYDRDEVA AALDRALTMS 420
LAERISRHAE MLDVIVKNDI NHWQECFISD LKQIVPRSAE SQQRDKVATF PKLA 474 
Gene Ontology
 GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IDA:EcoCyc.
 GO:0006974; P:response to DNA damage stimulus; IEP:EcoliWiki.
 GO:0006970; P:response to osmotic stress; IMP:EcoCyc.
 GO:0005992; P:trehalose biosynthetic process; IMP:EcoCyc.
 GO:0070415; P:trehalose metabolism in response to cold stress; IEP:EcoCyc. 
Interpro
 IPR001830; Glyco_trans_20.
 IPR012766; Trehalose_OtsA. 
Pfam
 PF00982; Glyco_transf_20 
SMART
  
PROSITE
  
PRINTS