O67238 (MURG_AQUAE) 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:	aq_1177

Organism

Aquifex aeolicus (strain VF5)

Taxonomic identifier

224324 [NCBI]

Taxonomic lineage

Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex

Protein attributes

Sequence length	344 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 Reference 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 – 344	344	UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase HAMAP MF_00033		PRO_0000109137

Sequences

	Sequence		Length	Mass (Da)
	O67238 [UniParc]. Last modified August 1, 1998. Version 1. Checksum: 5A4B3322B4AC650C	FASTA	344	39,325
	10 20 30 40 50 60 MIAVSGGGTG GHFFPALAFT NYVLKKEKVK FIGSKRGIEY ELKDLIKTEK LFLDVEPLRE 70 80 90 100 110 120 RNFYQKLKAI WKFLKAQEEI NEFLKEDYRA LIFGGYASLP LGINTVLRRK ELFIHEQNSI 130 140 150 160 170 180 PSKTNKILSK KAKKVLITFN YTKRFFPEGV RVGLPIRKEL KKKLPKKEVK KRFGLEPDKI 190 200 210 220 230 240 TVLIFGGSQG ALFLNELARD LKSVLPKEFQ VILLTGKIHY EKFKNLEGEK FRVMPFSLDM 250 260 270 280 290 300 GLIYSASDVA ISRAGAGTIN ELSHFGVPSV FVPYPYAVDD HQFYNAKEIE KLGGGLVLRQ 310 320 330 340 EEAKPDKVLS ALKEIVKNLE RYSENIKKFF AEGAEERMYE ELLG

References

[1]

"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus." Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V. Nature 392:353-358(1998) [PubMed: 9537320] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: VF5.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000657 Genomic DNA. Translation: AAC07193.1.
PIR	C70401.
RefSeq	NP_213802.1. NC_000918.1.
3D structure databases
ProteinModelPortal	O67238.
ModBase	Search...
Protein family/group databases
CAZy	GT28. Glycosyltransferase Family 28.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1192584.
GenomeReviews	Gene locus aq_1177 in contig AE000657_GR.
KEGG	aae:aq_1177.
NMPDR	fig|224324.1.peg.817.
PATRIC	20959590. VBIAquAeo85532_0915.
Phylogenomic databases
HOGENOM	HBG617076.
OMA	QITHTIS.
PhylomeDB	O67238.
ProtClustDB	PRK00726.
Enzyme and pathway databases
BioCyc	AAEO224324:AQ_1177-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.
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_AQUAE

Accession

Primary (citable) accession number: O67238

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	August 1, 1998
Last modified:	January 25, 2012
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program