Reviewed, UniProtKB/Swiss-Prot Q0SM88 (MURG_BORAP)

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:	BAPKO_0815

Organism

Borrelia afzelii (strain PKo) [Complete proteome] [HAMAP]

Taxonomic identifier

390236 [NCBI]

Taxonomic lineage

Bacteria › Spirochaetes › Spirochaetales › Spirochaetaceae › Borrelia › Borrelia burgdorferi group

Protein attributes

Sequence length	363 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 – 363	363	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase HAMAP MF_00033		PRO_1000002620

Sequences

	Sequence		Length	Mass (Da)
	Q0SM88-1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 461AD2B8ABB390BC	FASTA	363	41,172
	10 20 30 40 50 60 MSNKKIIFFT GGGTGGHIFP GISIIQKLKE LDNEIEFFWI GKKNSIEEKL IKEQNNIKFI 70 80 90 100 110 120 SIPCGKLRRY FSFQNFTDFF KVIFGIIKSF YILKKYKPQI VYATGGFVST PTIIASSLLK 130 140 150 160 170 180 IKRITHEMDL DPGLATKINS KFANKIYISF KESEKYFKNH KNIIHTGSPI RKEFLTPNPK 190 200 210 220 230 240 IIKQLTQNTN KPIVSILGGS LGANALNNLA LCIKKDAEIY FIHQSGKNLN DLREDNYIRR 250 260 270 280 290 300 QFFNAEEMAS IVKFSNIIIS RAGAGAIKEF ANACTCTILI PFKKGSRGDQ IKNAKLLKTQ 310 320 330 340 350 360 NACIYIDEDE ILNANILKII KETLKDKEKI NTLKANIKKF NNKNSSALIA QLLIKDIKET KSK

References

[1]

"Comparative genome analysis: selection pressure on the Borrelia vls cassettes is essential for infectivity." Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J., Wilske B., Platzer M. BMC Genomics 7:211-211(2006) [PubMed: 16914037] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000395 Genomic DNA. Translation: ABH02040.1.
RefSeq	YP_710216.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q0SM88.
Protein family/group databases
CAZy	GT28. Glycosyltransferase Family 28.
Genome annotation databases
GeneID	4227881.
GenomeReviews	Gene locus BAPKO_0815 in contig CP000395_GR.
KEGG	baf:BAPKO_0815.
NMPDR	fig|390236.5.peg.820.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q0SM88.
OMA	HESDMTP.
Enzyme and pathway databases
BioCyc	BAFZ390236:BAPKO_0815-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_BORAP

Accession

Primary (citable) accession number: Q0SM88

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	November 3, 2009
This is version 31 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)