Reviewed, UniProtKB/Swiss-Prot Q7VUQ3 (MURG_BORPE)

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:	BP3023

Organism

Bordetella pertussis [Complete proteome] [HAMAP]

Taxonomic identifier

520 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	357 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 – 357	357	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase HAMAP MF_00033		PRO_0000109149

Sequences

	Sequence		Length	Mass (Da)
	Q7VUQ3-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 2730305ECA9CB893	FASTA	357	37,907
	10 20 30 40 50 60 MSAPTILIMA GGTGGHIMPG LAVAEVLRER GWRVLWLGNP DKMEGRLVPP RGIELVPLRF 70 80 90 100 110 120 QGVRGRGAAA LLKLPFLLAR ACAQAWRRLA DIRPDVVLGM GGYVAFPGGV MAALRRTPLV 130 140 150 160 170 180 VHEQNAVAGT ANRWLARLAR RVLSGFPGVL PRGEALGNPV RADLCALPEP AERYAGRSGA 190 200 210 220 230 240 LRVLVVGGSL GAHALNTTVP QALALLPEQA RPQVVHQAGE QHLPALQQAY AQAGVQADCR 250 260 270 280 290 300 AFIDDMADAM AQADLLICRA GAMTVSEVAA AGVAALFVPF PHAIDDHQTA NARFLSDAQA 310 320 330 340 350 AWLQPQASLT PQWLAQWLGQ RTRQELQAVA GRARTHALPR AAAHIADVCE QAARRAS

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tohama I / ATCC BAA-589 / NCTC 13251.

Cross-references

Sequence databases
EMBLGenBankDDBJ	BX640420 Genomic DNA. Translation: CAE43294.1.
RefSeq	NP_881598.1.
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GT28. Glycosyltransferase Family 28.
Genome annotation databases
GeneID	2665871.
GenomeReviews	Gene locus BP3023 in contig BX470248_GR.
KEGG	bpe:BP3023.
NMPDR	fig|257313.1.peg.2671.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7VUQ3.
OMA	YVCGPVV.
Enzyme and pathway databases
BioCyc	BPER257313:BP3023-MON.
BRENDA	2.4.1.227. 21511.
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_BORPE

Accession

Primary (citable) accession number: Q7VUQ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 2003
Last sequence update:	October 1, 2003
Last modified:	November 3, 2009
This is version 44 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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