Reviewed, UniProtKB/Swiss-Prot Q1LSW5 (MURG_BAUCH)

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:	BCI_0519

Organism

Baumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]

Taxonomic identifier

374463 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Candidatus Baumannia

Protein attributes

Sequence length	358 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 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 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: HAMAP peptidoglycan biosynthetic process Inferred from electronic annotation. Source: HAMAP regulation of cell shape Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	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 – 358	358	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase HAMAP MF_00033		PRO_0000315071

Sequences

	Sequence		Length	Mass (Da)
	Q1LSW5-1 [UniParc]. Last modified May 30, 2006. Version 1. Checksum: AEC06BA29F2E53D2	FASTA	358	39,869
	10 20 30 40 50 60 MIRKRLIIVA GGTGGHIFPG LAIANNMITQ GWDVRWLGTK NRIEADLVPK HGITTYFLSI 70 80 90 100 110 120 YGYGLHGKKQ KILAIVSILQ AVLQSYYIMR KWRPDIVLGM GGYISGPCGL AAWMCKIPLV 130 140 150 160 170 180 IHEQNRVTGL TNYYLSKFAK KVLQAFPSVF PNANVVGNPI RKEILAVIEP SLRLCNRTGP 190 200 210 220 230 240 IRILVIGGSQ GSKIINQILP VVAAQLAGKY VFWHQVGKGA LKEVQQVYTS MLKNQLNYKL 250 260 270 280 290 300 VEFIDDIAIA YAWADVVICR SGALTISEIA AVGLPAIFVP FMHKDRHQYW NALPLEQLGA 310 320 330 340 350 AKILEQPNFT AEKVSQILMS WDRSKLFTMA QRARTIAMVD STERVTSELI ELANNTKH

References

[1]

"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters." Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A. PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000238 Genomic DNA. Translation: ABF13989.1.
RefSeq	YP_588949.1.
3D structure databases
SMR	Q1LSW5. Positions 4-354.
ModBase	Search...
Protein-protein interaction databases
STRING	Q1LSW5.
Protein family/group databases
CAZy	GT28. Glycosyltransferase Family 28.
Genome annotation databases
GeneID	4056736.
GenomeReviews	Gene locus BCI_0519 in contig CP000238_GR.
KEGG	bci:BCI_0519.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0707.
HOGENOM	HBG617076.
OMA	GGTGGHM.
PhylomeDB	Q1LSW5.
Family and domain databases
HAMAP	MF_00033. MurG. [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_BAUCH

Accession

Primary (citable) accession number: Q1LSW5

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	May 30, 2006
Last modified:	February 9, 2010
This is version 35 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)