B0V9F5 (MURG_ACIBY) Reviewed, UniProtKB/Swiss-Prot

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:	ABAYE0148

Organism

Acinetobacter baumannii (strain AYE) [Complete proteome] [HAMAP]

Taxonomic identifier

509173 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter › Acinetobacter calcoaceticus/baumannii complex

Protein attributes

Sequence length	365 AA.
Sequence status	Complete.
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. HAMAP MF_00033
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 HAMAP MF_00033.
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 cellular cell wall organization Inferred from electronic annotation. Source: UniProtKB-KW lipid glycosylation Inferred from electronic annotation. Source: InterPro peptidoglycan biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol 4-beta-N-acetylglucosaminlytransferase activity Inferred from electronic annotation. Source: EC carbohydrate binding Inferred from electronic annotation. Source: InterPro undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 365	365	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase HAMAP MF_00033		PRO_1000090399

Sequences

	Sequence		Length	Mass (Da)
	B0V9F5 [UniParc]. Last modified April 8, 2008. Version 1. Checksum: B6088B90834407E8	FASTA	365	39,350
	10 20 30 40 50 60 MTDSQQSKPK HVMMMAAGTG GHVFPALAVA KQLQQQGCQV SWLATPTGME NRLLKDQNIP 70 80 90 100 110 120 IYQIDIQGVR GNGVIRKLAA PFKILKATFS AMRYMKQLKV DAVAGFGGYV AGPGGLAARL 130 140 150 160 170 180 LGIPVLIHEQ NAVAGFTNAQ LSRVAKVVCE AFPNTFPASE KVVTTGNPVR REITDILSPK 190 200 210 220 230 240 WRYDEREQAG KPLNILIVGG SLGAKALNER LPPALKQLEV PLNIFHQCGQ QQVEATQALY 250 260 270 280 290 300 ADAPANLTVQ VLPFIEDMAK AYSEADLIIC RAGALTVTEV ATAGVAAVFV PLPIAVDDHQ 310 320 330 340 350 360 TANAKFLADV GAAKICQQST MTPEVLNQLF TTLMNRQLLT EMAVKARQHA QPNATQHVVD LIQKM

References

[1]

"Comparative analysis of Acinetobacters: three genomes for three lifestyles." Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E., Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J., Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C., Weissenbach J., Cruveiller S. PLoS ONE 3:E1805-E1805(2008) [PubMed: 18350144] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AYE.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU459141 Genomic DNA. Translation: CAM85134.1.
RefSeq	YP_001712141.1. NC_010410.1.
3D structure databases
ProteinModelPortal	B0V9F5.
ModBase	Search...
Protein-protein interaction databases
STRING	B0V9F5.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6003307.
GenomeReviews	Gene locus ABAYE0148 in contig CU459141_GR.
PATRIC	20723765. VBIAciBau69881_0244.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG617076.
OMA	EDHQTKN.
ProtClustDB	PRK00726.
Family and domain databases
HAMAP	MF_00033. MurG. [Tree]
InterPro	IPR006009. GlcNAc_MurG. IPR004276. Glyco_trans_28. IPR007235. Glyco_trans_28_C. [Graphical view]
PANTHER	PTHR21015:SF22. PTHR21015:SF22. 1 hit.
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_ACIBY

Accession

Primary (citable) accession number: B0V9F5

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 24, 2009
Last sequence update:	April 8, 2008
Last modified:	January 25, 2012
This is version 33 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program