Reviewed, UniProtKB/Swiss-Prot Q5LIJ7 (MURG_BACFN)

Names and origin

Protein names

Recommended name:
    UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase
    EC=2.4.1.227
Alternative name(s):
    Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase

Gene names

Name:	murG
Ordered Locus Names:	BF0254

Organism

Bacteroides fragilis (strain ATCC 25285 / NCTC 9343) [Complete proteome] [HAMAP]

Taxonomic identifier

272559 [NCBI]

Taxonomic lineage

Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides

Protein attributes

Sequence length	380 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II) By similarity.
Catalytic activity	UDP-N-acetylglucosamine + Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = UDP + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol. HAMAP MF_00033
Pathway	Cell wall biogenesis; peptidoglycan biosynthesis. HAMAP MF_00033
Subcellular location	Cell inner membrane; Peripheral membrane protein By similarity.
Sequence similarities	Belongs to the glycosyltransferase 28 family. MurG subfamily.

Ontologies

Keywords
Biological process	Cell cycle Cell division Cell shape Cell wall biogenesis/degradation Peptidoglycan synthesis
Cellular component	Cell inner membrane Cell membrane Membrane
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	UDP-N-acetylgalactosamine biosynthetic process Inferred from electronic annotation. Source: InterPro cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cell division Inferred from electronic annotation. Source: UniProtKB-KW cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW lipid glycosylation Inferred from electronic annotation. Source: HAMAP peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	Gram-negative-bacterium-type cell wall Inferred from electronic annotation. Source: InterPro extrinsic to membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: HAMAP
Molecular function	carbohydrate binding Inferred from electronic annotation. Source: InterPro undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 380	380	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase HAMAP MF_00033		PRO_0000225030

Sequences

	Sequence		Length	Mass (Da)
	Q5LIJ7-1 [UniParc]. Last modified March 7, 2006. Version 2. Checksum: C3FFCBCCF28616E4	FASTA	380	41,144
	10 20 30 40 50 60 MNKENNKEGQ GDALRVIISG GGTGGHIFPA VSIANAIKEL RPDAQILFVG AEGRMEMQRV 70 80 90 100 110 120 PDAGYQIIGL PVAGFDRKHL WKNVAVLLKL VRSQWKARNI IRQFRPQVAV GVGGYASGPT 130 140 150 160 170 180 LKMAGMMGVP TLIQEQNSYA GVTNKLLAQK ARRICVAYDG MEKFFPANKI IMTGNPVRQN 190 200 210 220 230 240 LLAEKPEREQ AIRSFGLNPE KKTILILGGS LGARTINNTL IAGLQLIRRT TDVQFIWQTG 250 260 270 280 290 300 KIYHQQVTEA VKAAGEIPNL FVTDFIKDMA AAYAAADLVI SRAGAGSISE FCLLNKPVIL 310 320 330 340 350 360 VPSPNVAEDH QTKNALALVN KQAAIYVKDA EAENKLLPVA LETIANAEKL SELSENIAHL 370 380 ALPDSAVVIA KEVIKLAQQS

References

[1]

"Extensive DNA inversions in the B. fragilis genome control variable gene expression." Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V., Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A., Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A. , Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J., Barrell B.G., Parkhill J. Science 307:1463-1465(2005) [PubMed: 15746427] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CR626927 Genomic DNA. Translation: CAH06029.1. Different initiation.
RefSeq	YP_209991.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5LIJ7.
Protein family/group databases
CAZy	GT28. Glycosyltransferase Family 28.
Genome annotation databases
GeneID	3286064.
GenomeReviews	Gene locus BF0254 in contig CR626927_GR.
KEGG	bfs:BF0254.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q5LIJ7.
Enzyme and pathway databases
BioCyc	BFRA272559:BF0254-MON.
Family and domain databases
HAMAP	MF_00033. [Tree]
InterPro	IPR006009. GlcNAc_MurG. IPR004276. Glyco_trans_28. IPR007235. Glyco_trans_28_C. [Graphical view]
Pfam	PF04101. Glyco_tran_28_C. 1 hit. PF03033. Glyco_transf_28. 1 hit. [Graphical view]
TIGRFAMs	TIGR01133. murG. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MURG_BACFN

Accession

Primary (citable) accession number: Q5LIJ7

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 7, 2006
Last sequence update:	March 7, 2006
Last modified:	October 13, 2009
This is version 39 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)