Q6HNU4 (UGTP_BACHK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Processive diacylglycerol glucosyltransferase
EC=2.4.1.-

Alternative name(s):
Beta-gentiobiosyldiacylglycerol synthase
DGlcDAG synthase
Diglucosyldiacylglycerol synthase
Glc2-DAG synthase
Monoglucosyldiacylglycerol synthase
Short name=MGlcDAG synthase
Triglucosyldiacylglycerol synthase
Short name=TGlcDAG synthase
UDP glucosyltransferase
UDP-glucose:1,2-diacylglycerol-3-beta-D-glucosyltransferase

Gene names

Name:	ugtP
Ordered Locus Names:	BT9727_0426

Organism

Bacillus thuringiensis subsp. konkukian (strain 97-27) [Complete proteome] [HAMAP]

Taxonomic identifier

281309 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	388 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Is a processive glucosyltransferase involved in the synthesis of both bilayer- and non-bilayer-forming membrane glycolipids. Is able to successively transfer up to three glucosyl residues to diacylglycerol (DAG), thereby catalyzing the formation of mono-, di- and triglucosyldiacylglycerol. Diglucosyldiacylglycerol (Glc2-DAG) is the predominant glycolipid found in Bacillales and is also used as a membrane anchor for lipoteichoic acid (LTA) By similarity. HAMAP MF_01280
Catalytic activity	UDP-glucose + 1,2-diacylglycerol = UDP + 1,2-diacyl-3-(O-beta-D-glucopyranosyl)-sn-glycerol. HAMAP MF_01280 UDP-glucose + 1,2-diacyl-3-(O-beta-D-glucopyranosyl)-sn-glycerol = UDP + 1,2-diacyl-3-(O-beta-D-glucopyranosyl(1->6)-O-beta-D-glucopyranosyl)-sn-glycerol. HAMAP MF_01280 UDP-glucose + 1,2-diacyl-3-(O-beta-D-glucopyranosyl(1->6)-O-beta-D-glucopyranosyl)-sn-glycerol = UDP + 1,2-diacyl-3-(O-beta-D-glucopyranosyl(1->6)-O-beta-D-glucopyranosyl(1->6)-O-beta-D-glucopyranosyl)-sn-glycerol.
Pathway	Glycolipid metabolism; diglucosyl-diacylglycerol biosynthesis. HAMAP MF_01280
Sequence similarities	Belongs to the glycosyltransferase 28 family. UgtP subfamily.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	glycolipid biosynthetic process Inferred from electronic annotation. Source: InterPro lipid glycosylation Inferred from electronic annotation. Source: InterPro
Molecular function	carbohydrate binding Inferred from electronic annotation. Source: InterPro glucosyltransferase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 388	388	Processive diacylglycerol glucosyltransferase HAMAP MF_01280		PRO_0000308451

Sequences

	Sequence		Length	Mass (Da)
	Q6HNU4 [UniParc]. Last modified July 19, 2004. Version 1. Checksum: 258505FF5A850662	FASTA	388	43,761
	10 20 30 40 50 60 MIKNPKVLIL TAHYGNGHVQ VAKTLEQTFR QKGIKDVIVC DLFGESHPVI TDITKYLYLK 70 80 90 100 110 120 SYTIGKELYR LFYYGVEKIY DKKIASWYAN FGRKRLKLLL QAEKPDIVIN TFPIIAVPEL 130 140 150 160 170 180 KKQTGISIPV YNVLTDFCVH KIWIHREVDR YFVATDHVKK VMVDIGVPAE QIVETGIPIR 190 200 210 220 230 240 SSFELKINPD IIYNKYQLCK NKKILLIVAG AHGVLGSVKE LCQSFMSVPD LQVVVVCGKN 250 260 270 280 290 300 EALKQDLVGV QETNPDALKV FGYVENIDEL FRVTSCMITK PGGITLSEAA ALQVPVILYK 310 320 330 340 350 360 PVPGQENENA MYFERKGAAV VIRDDSEVFA KTEALLQDDM KLLQMKEAMK SIYRPEPADH 370 380 IVDTILAENH VEPNHIPIKS PALAQSFT

References

[1]

"Pathogenomic sequence analysis of Bacillus cereus and Bacillus thuringiensis isolates closely related to Bacillus anthracis." Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., Hill K.K., Hitchcock P. , Jackson P.J., Keim P., Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Brettin T.S., Gilna P. J. Bacteriol. 188:3382-3390(2006) [PubMed: 16621833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 97-27.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017355 Genomic DNA. Translation: AAT62328.1.
RefSeq	YP_034776.1. NC_005957.1.
3D structure databases
ProteinModelPortal	Q6HNU4.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000074341; EBBACP00000072427; EBBACG00000074332.
GeneID	2854580.
GenomeReviews	Gene locus BT9727_0426 in contig AE017355_GR.
KEGG	btk:BT9727_0426.
PATRIC	18981357. VBIBacThu119411_0452.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000001193.
HOGENOM	HBG535586.
OMA	EPAGHIV.
ProtClustDB	PRK13609.
Enzyme and pathway databases
BioCyc	BTHU281309:BT9727_0426-MONOMER.
Family and domain databases
HAMAP	MF_01280. Diacylglyc_glucosyltr. [Tree]
InterPro	IPR009695. Diacylglyc_glucosyltr_N. IPR007235. Glyco_trans_28_C. IPR023589. Pro_diacylglycrl_glcsylTrfase. [Graphical view]
KO	K03429.
Pfam	PF04101. Glyco_tran_28_C. 1 hit. PF06925. MGDG_synth. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

UGTP_BACHK

Accession

Primary (citable) accession number: Q6HNU4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 2007
Last sequence update:	July 19, 2004
Last modified:	January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program