Reviewed, UniProtKB/Swiss-Prot P17443 (MURG_ECOLI)

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:	b0090, JW0088

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	355 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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). 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. Ref.7
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	3D-structure Complete proteome Direct protein sequencing
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 plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
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

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 355

354

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

PRO_0000109170

Secondary structure

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355

Helix Strand Turn

Details...

Beta strand

7 – 11

5

Helix

16 – 30

15

Turn

31 – 33

3

Beta strand

35 – 40

6

Helix

46 – 49

4

Helix

50 – 53

4

Beta strand

56 – 59

4

Helix

70 – 74

5

Helix

77 – 94

18

Beta strand

97 – 101

5

Helix

107 – 116

10

Beta strand

121 – 125

5

Beta strand

127 – 129

3

Helix

132 – 137

6

Turn

138 – 140

3

Beta strand

142 – 148

7

Beta strand

151 – 154

4

Helix

164 – 167

4

Helix

172 – 176

5

Beta strand

181 – 188

8

Turn

190 – 192

3

Helix

195 – 208

14

Helix

209 – 211

3

Beta strand

212 – 217

6

Helix

223 – 232

10

Beta strand

238 – 242

5

Helix

247 – 253

7

Beta strand

255 – 259

5

Helix

263 – 272

10

Beta strand

276 – 278

3

Helix

287 – 297

11

Beta strand

300 – 303

4

Helix

306 – 308

3

Helix

311 – 319

9

Helix

323 – 335

13

Helix

341 – 353

13

Sequences

	Sequence		Length	Mass (Da)
	P17443-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: DE347361A7B9293A	FASTA	355	37,815
	10 20 30 40 50 60 MSGQGKRLMV MAGGTGGHVF PGLAVAHHLM AQGWQVRWLG TADRMEADLV PKHGIEIDFI 70 80 90 100 110 120 RISGLRGKGI KALIAAPLRI FNAWRQARAI MKAYKPDVVL GMGGYVSGPG GLAAWSLGIP 130 140 150 160 170 180 VVLHEQNGIA GLTNKWLAKI ATKVMQAFPG AFPNAEVVGN PVRTDVLALP LPQQRLAGRE 190 200 210 220 230 240 GPVRVLVVGG SQGARILNQT MPQVAAKLGD SVTIWHQSGK GSQQSVEQAY AEAGQPQHKV 250 260 270 280 290 300 TEFIDDMAAA YAWADVVVCR SGALTVSEIA AAGLPALFVP FQHKDRQQYW NALPLEKAGA 310 320 330 340 350 AKIIEQPQLS VDAVANTLAG WSRETLLTMA ERARAASIPD ATERVANEVS RVARA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence involving murG and murC in the mra gene cluster region of Escherichia coli." Ikeda M., Wachi M., Jung H.K., Ishino F., Matsuhashi M. Nucleic Acids Res. 18:4014-4014(1990) [PubMed: 2197603] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region." Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A. Nucleic Acids Res. 20:3305-3308(1992) [PubMed: 1630901] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Nucleotide sequence of the cell-envelope murG gene of Escherichia coli." Mengin-Lecreulx D., Texier L., van Heijenoort J. Nucleic Acids Res. 18:2810-2810(1990) [PubMed: 2187180] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 9-355. Strain: K12.
[6]	"The murG gene of Escherichia coli codes for the UDP-N-acetylglucosamine: N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase involved in the membrane steps of peptidoglycan synthesis." Mengin-Lecreulx D., Texier L., Rousseau M., van Heijenoort J. J. Bacteriol. 173:4625-4636(1991) [PubMed: 1649817] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-18, CHARACTERIZATION.
[7]	"The final step of peptidoglycan subunit assembly in Escherichia coli occurs in the cytoplasm." Bupp K., van Heijenoort J. J. Bacteriol. 175:1841-1843(1993) [PubMed: 8449890] [Abstract] Cited for: SUBCELLULAR LOCATION.
[8]	"The 1.9 A crystal structure of Escherichia coli MurG, a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis." Ha S., Walker D., Shi Y., Walker S. Protein Sci. 9:1045-1052(2000) [PubMed: 10892798] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X52644 Genomic DNA. Translation: CAA36867.1.
X52540 Genomic DNA. Translation: CAA36776.1.
X55034 Genomic DNA. Translation: CAA38867.1.
U00096 Genomic DNA. Translation: AAC73201.1.
AP009048 Genomic DNA. Translation: BAB96658.1.

PIR

BVECMG. JQ0544.

RefSeq

AP_000753.1.
NP_414632.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F0K	X-ray	1.90	A/B	1-355	[»]
1NLM	X-ray	2.50	A/B	2-354	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:10282N.

Protein family/group databases

CAZy

GT28. Glycosyltransferase Family 28.

Genome annotation databases

GeneID

946321.

GenomeReviews

Gene locus JW0088 in contig AP009048_GR.
Gene locus b0090 in contig U00096_GR.

KEGG

ecj:JW0088.
eco:b0090.

Organism-specific databases

EchoBASE

EB0618.

EcoGene

EG10623. murG.

CMR

Search...

Phylogenomic databases

HOGENOM

P17443.

OMA

P17443. YVCGPVV.

Enzyme and pathway databases

BioCyc

EcoCyc:NACGLCTRANS-MON.
MetaCyc:NACGLCTRANS-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_ECOLI

Accession

Primary (citable) accession number: P17443

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 106 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)