Q8NXC3 (UGTP_STAAW) 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:	MW0898

Organism

Staphylococcus aureus (strain MW2) [Complete proteome] [HAMAP]

Taxonomic identifier

196620 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	391 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 – 391	391	Processive diacylglycerol glucosyltransferase HAMAP MF_01280		PRO_0000308459

Sequences

	Sequence		Length	Mass (Da)
	Q8NXC3 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: A1D6E96C91B7E99D	FASTA	391	44,548
	10 20 30 40 50 60 MVTQNKKILI ITGSFGNGHM QVTQSIVNQL NDMNLDHLSV IEHDLFMEAH PILTSICKKW 70 80 90 100 110 120 YINSFKYFRN MYKGFYYSRP DKLDKCFYKY YGLNKLINLL IKEKPDLILL TFPTPVMSVL 130 140 150 160 170 180 TEQFNINIPV ATVMTDYRLH KNWITPYSTR YYVATKETKQ DFIDVGIDPS TVKVTGIPID 190 200 210 220 230 240 NKFETPINQK QWLIDNNLDP DKQTILMSAG AFGVSKGFDT MITDILAKSA NAQVVMICGK 250 260 270 280 290 300 SKELKRSLTA KFKSNENVLI LGYTKHMNEW MASSQLMITK PGGITITEGF ARCIPMIFLN 310 320 330 340 350 360 PAPGQELENA LYFEEKGFGK IADTPEEAIK IVASLTNGNE QLTNMISTME QDKIKYATQT 370 380 390 ICRDLLDLIG HSSQPQEIYG KVPLYARFFV K

References

[1]

"Genome and virulence determinants of high virulence community-acquired MRSA." Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K. Lancet 359:1819-1827(2002) [PubMed: 12044378] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MW2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000033 Genomic DNA. Translation: BAB94763.1.
RefSeq	NP_645715.1. NC_003923.1.
3D structure databases
ProteinModelPortal	Q8NXC3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8NXC3.
Protein family/group databases
CAZy	GT28. Glycosyltransferase Family 28.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBSTAT00000025338; EBSTAP00000024377; EBSTAG00000025337.
GeneID	1003010.
GenomeReviews	Gene locus MW0898 in contig BA000033_GR.
KEGG	sam:MW0898.
PATRIC	19568365. VBIStaAur44266_0944.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0707.
GeneTree	EBGT00050000024210.
HOGENOM	HBG535586.
OMA	EPAGHIV.
ProtClustDB	PRK13608.
Enzyme and pathway databases
BioCyc	SAUR196620:MW0898-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_STAAW

Accession

Primary (citable) accession number: Q8NXC3

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 23, 2007
Last sequence update:	October 1, 2002
Last modified:	January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program