Q5PB22 (MURG_ANAMM) 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:	AM471

Organism

Anaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]

Taxonomic identifier

234826 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Anaplasma

Protein attributes

Sequence length	356 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.
Sequence caution	The sequence AAV86508.1 differs from that shown. Reason: Erroneous initiation.

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 – 356	356	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase HAMAP MF_00033		PRO_0000315063

Sequences

	Sequence		Length	Mass (Da)
	Q5PB22 [UniParc]. Last modified January 15, 2008. Version 2. Checksum: 93A718B36B7F2246	FASTA	356	38,262
	10 20 30 40 50 60 MKKVVLAAGG TGGHIVPAAL LCQVLADRGY RCVLYTDQYF LQYTARFPGI KGYVLLPLCK 70 80 90 100 110 120 RSGGAVRLLK FCALLAYSCV LSYIKLRSLK PDLVIGFGAY ASFPVLLSAW LMSVDAVLHE 130 140 150 160 170 180 QNSVMGRVNR VFAGYARVIA CGLPLRTVGN KLAHKVAHVG VPTDVKKAVK RPLAGDSINL 190 200 210 220 230 240 VILGGSQGLC TFGKTFALAI AELPTNIRGR VFVTQQCGKG QLEVITELYA RHGIKHKLSG 250 260 270 280 290 300 FFTDMQNIIG EADLIISRAG ATTIAEVMAA GRPAIYVPYE RSSCSHQLYN AQLIESLGAG 310 320 330 340 350 LCIEERTLDV SSARDALTNL LGDRNKLQEM SCNAAKHAMP DADAQFCAIV DGLLKG

References

[1]

"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins." Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr. Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: St. Maries.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000030 Genomic DNA. Translation: AAV86508.1. Different initiation.
RefSeq	YP_153763.1. NC_004842.2.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q5PB22.
Protein family/group databases
CAZy	GT28. Glycosyltransferase Family 28.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3171244.
GenomeReviews	Gene locus AM471 in contig CP000030_GR.
KEGG	ama:AM471.
PATRIC	20946955. VBIAnaMar46146_0403.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0707.
HOGENOM	HBG617076.
OMA	EDHQTKN.
ProtClustDB	CLSK740297.
Enzyme and pathway databases
BioCyc	AMAR234826:AM471-MONOMER.
Family and domain databases
HAMAP	MF_00033. MurG. [Tree]
InterPro	IPR006009. GlcNAc_MurG. IPR004276. Glyco_trans_28. IPR007235. Glyco_trans_28_C. [Graphical view]
KO	K02563.
PANTHER	PTHR21015:SF22. PTHR21015:SF22. 1 hit.
Pfam	PF04101. Glyco_tran_28_C. 1 hit. PF03033. Glyco_transf_28. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MURG_ANAMM

Accession

Primary (citable) accession number: Q5PB22

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	January 15, 2008
Last modified:	January 25, 2012
This is version 47 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program