Q8XCE7 (OTSA_ECO57) Reviewed, UniProtKB/Swiss-Prot

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:	Z2949, ECs2604

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

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

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 By similarity.
Catalytic activity	UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate.
Pathway	Glycan biosynthesis; trehalose biosynthesis.
Subunit structure	Homotetramer By similarity.
Sequence similarities	Belongs to the glycosyltransferase 20 family.

Ontologies

Keywords
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological_process	trehalose biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 474	473	Alpha,alpha-trehalose-phosphate synthase [UDP-forming]		PRO_0000122490
Regions
	Region	22 – 23	2	UDP-glucose binding By similarity
	Region	366 – 370	5	UDP-glucose binding By similarity
Sites
	Binding site	10	1	Glucose-6-phosphate By similarity
	Binding site	77	1	Glucose-6-phosphate By similarity
	Binding site	131	1	Glucose-6-phosphate By similarity
	Binding site	263	1	UDP-glucose By similarity
	Binding site	268	1	UDP-glucose By similarity
	Binding site	301	1	Glucose-6-phosphate By similarity
	Binding site	340	1	UDP-glucose; via amide nitrogen and carbonyl oxygen By similarity
	Site	86	1	Involved in alpha anomer selectivity By similarity
	Site	156	1	Involved in alpha anomer selectivity By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8XCE7 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 63FFA9F628056F82	FASTA	474	53,667
	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 VALDRALTMS 430 440 450 460 470 LAERISRHAE MLDVIVKNDI NHWQECFISD LKQIVPRSAE SQQRDKVATF PKLV

References

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG56885.1. BA000007 Genomic DNA. Translation: BAB36027.1.
PIR	A85803. D90954.
RefSeq	NP_288332.1. NC_002655.2. NP_310631.1. NC_002695.1.
3D structure databases
ProteinModelPortal	Q8XCE7.
SMR	Q8XCE7. Positions 2-457.
ModBase	Search...
Protein-protein interaction databases
STRING	155864.Z2949.
Protein family/group databases
CAZy	GT20. Glycosyltransferase Family 20.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAG56885; AAG56885; Z2949. BAB36027; BAB36027; BAB36027.
GeneID	912524. 961867.
KEGG	ece:Z2949. ecs:ECs2604.
PATRIC	18354586. VBIEscCol44059_2504.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0380.
HOGENOM	HOG000191478.
KO	K00697.
OMA	EYGRKEM.
ProtClustDB	PRK10117.
Enzyme and pathway databases
BioCyc	ECOL386585:GJFA-2578-MONOMER.
UniPathway	UPA00299.
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_ECO57

Accession

Primary (citable) accession number: Q8XCE7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 63 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program