RegulonDB RegulonDB 10.8: Gene Form
   

murG gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

murC murD ftsW murG ddlB TSS_173 (cluster) TSS_173 (cluster) TSS_172 TSS_172 TSS_171 TSS_171 TSS_170 TSS_170 TSS_169 TSS_169

Gene      
Name: murG    Texpresso search in the literature
Synonym(s): ECK0091, EG10623, b0090
Genome position(nucleotides): 99644 --> 100711 Genome Browser
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
56.09
External database links:  
ASAP:
ABE-0000322
CGSC:
473
ECHOBASE:
EB0618
OU-MICROARRAY:
b0090
PortEco:
murG
STRING:
511145.b0090
COLOMBOS: murG


Product      
Name: N-acetylglucosaminyl transferase
Synonym(s): MurG
Sequence: Get amino acid sequence Fasta Format
Cellular location: inner membrane
Molecular weight: 37.815
Isoelectric point: 10.321
Motif(s):
 
Type Positions Sequence
2 -> 355 SGQGKRLMVMAGGTGGHVFPGLAVAHHLMAQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGIKALIAAPLRIFNAWRQARAIMKAYKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVMQAFPGAFPNAEVVGNPVRTDVLALPLPQQRLAGREGPVRVLVVGGSQGARILNQTMPQVAAKLGDSVTIWHQSGKGSQQSVEQAYAEAGQPQHKVTEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHKDRQQYWNALPLEKAGAAKIIEQPQLSVDAVANTLAGWSRETLLTMAERARAASIPDATERVANEVSRVARA
9 -> 145 MVMAGGTGGHVFPGLAVAHHLMAQGWQVRWLGTADRMEADLVPKHGIEIDFIRISGLRGKGIKALIAAPLRIFNAWRQARAIMKAYKPDVVLGMGGYVSGPGGLAAWSLGIPVVLHEQNGIAGLTNKWLAKIATKVM
185 -> 344 VLVVGGSQGARILNQTMPQVAAKLGDSVTIWHQSGKGSQQSVEQAYAEAGQPQHKVTEFIDDMAAAYAWADVVVCRSGALTVSEIAAAGLPALFVPFQHKDRQQYWNALPLEKAGAAKIIEQPQLSVDAVANTLAGWSRETLLTMAERARAASIPDATER

 

Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.6 - biosynthesis of macromolecules (cellular constituents) --> 1.6.7 - murein (peptidoglycan)
  6 - cell structure --> 6.1 - membrane
  6 - cell structure --> 6.2 - murein
Gene Ontology Terms (GO)  
cellular_component GO:0016020 - membrane
GO:0005886 - plasma membrane
molecular_function GO:0005515 - protein binding
GO:0016757 - transferase activity, transferring glycosyl groups
GO:0016758 - transferase activity, transferring hexosyl groups
GO:0016740 - transferase activity
GO:0050511 - undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase activity
GO:0051991 - 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
biological_process GO:0051301 - cell division
GO:0005975 - carbohydrate metabolic process
GO:0007049 - cell cycle
GO:0009252 - peptidoglycan biosynthetic process
GO:0008360 - regulation of cell shape
GO:0030259 - lipid glycosylation
GO:0071555 - cell wall organization
Note(s): Note(s): ...[more].
Reference(s): [1] Barbosa MD., et al., 2002
[2] Branstrom AA., et al., 2000
[3] Chandrakala B., et al., 2001
[4] Chen L., et al., 2002
[5] Crouvoisier M., et al., 2007
[6] Crouvoisier M., et al., 1999
[7] Cudic P., et al., 2001
[8] Hu Y., et al., 2004
[9] Hyland SA., et al., 2003
[10] Ikeda M., et al., 1990
[11] Liu H., et al., 2003
[12] Mengin-Lecreulx D., et al., 1998
[13] Mengin-Lecreulx D., et al., 1989
[14] Mengin-Lecreulx D., et al., 1990
[15] Ravishankar S., et al., 2005
[16] Salmond GP., et al., 1980
[17] Wrabl JO., et al., 2001
[18] Zawadzke LE., et al., 2003
[19] van den Brink-van der Laan E., et al., 2003
External database links:  
CAZY:
GT28
DIP:
DIP-10282N
ECOCYC:
NACGLCTRANS-MONOMER
ECOLIWIKI:
b0090
INTERPRO:
IPR007235
INTERPRO:
IPR006009
INTERPRO:
IPR004276
MINT:
MINT-1233082
MODBASE:
P17443
PANTHER:
PTHR21015:SF22
PDB:
1NLM
PDB:
1F0K
PFAM:
PF04101
PFAM:
PF03033
PRIDE:
P17443
PRODB:
PRO_000023318
REFSEQ:
NP_414632
SMR:
P17443
UNIPROT:
P17443


Operon      
Name: mraZ-rsmH-ftsLI-murEF-mraY-murD-ftsW-murGC-ddlB-ftsQAZ-lpxC         
Operon arrangement:
Transcription unit        Promoter
mraZW-ftsLI-murEF-mraY-murD-ftsW-murGC-ddlB-ftsQAZ-lpxC
mraW-ftsLI-murEF-mraY-murD-ftsW-murGC-ddlB-ftsQAZ-lpxC
ftsLI-murEF-mraY-murD-ftsW-murGC-ddlB-ftsQAZ-lpxC
ftsLI-murEF-mraY-murD-ftsW-murGC-ddlB-ftsQAZ-lpxC
ftsQ
ftsQAZ
ftsAZ
ftsZ
ftsZ
ftsZ
lpxC
lpxC


Transcriptional Regulation      
Display Regulation             
Repressed by: MraZ, LexA, PdhR


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter TSS_169 97532 forward nd [RS-EPT-CBR] [20]
  promoter TSS_170 97539 forward nd [RS-EPT-CBR] [20]
  promoter TSS_171 97550 forward nd [RS-EPT-CBR] [20]
  promoter TSS_172 100621 forward nd [RS-EPT-CBR] [20]
  promoter TSS_173 (cluster) 102049 forward For this promoter, there
Read more >
[RS-EPT-CBR] [20]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates



Reference(s)    

 [1] Barbosa MD., Ross HO., Hillman MC., Meade RP., Kurilla MG., Pompliano DL., 2002, A multitarget assay for inhibitors of membrane-associated steps of peptidoglycan biosynthesis., Anal Biochem 306(1):17-22

 [2] Branstrom AA., Midha S., Longley CB., Han K., Baizman ER., Axelrod HR., 2000, Assay for identification of inhibitors for bacterial MraY translocase or MurG transferase., Anal Biochem 280(2):315-9

 [3] Chandrakala B., Elias BC., Mehra U., Umapathy NS., Dwarakanath P., Balganesh TS., deSousa SM., 2001, Novel scintillation proximity assay for measuring membrane-associated steps of peptidoglycan biosynthesis in Escherichia coli., Antimicrob Agents Chemother 45(3):768-75

 [4] Chen L., Men H., Ha S., Ye XY., Brunner L., Hu Y., Walker S., 2002, Intrinsic lipid preferences and kinetic mechanism of Escherichia coli MurG., Biochemistry 41(21):6824-33

 [5] Crouvoisier M., Auger G., Blanot D., Mengin-Lecreulx D., 2007, Role of the amino acid invariants in the active site of MurG as evaluated by site-directed mutagenesis., Biochimie 89(12):1498-508

 [6] Crouvoisier M., Mengin-Lecreulx D., van Heijenoort J., 1999, UDP-N-acetylglucosamine:N-acetylmuramoyl-(pentapeptide) pyrophosphoryl undecaprenol N-acetylglucosamine transferase from Escherichia coli: overproduction, solubilization, and purification., FEBS Lett 449(2-3):289-92

 [7] Cudic P., Behenna DC., Yu MK., Kruger RG., Szewczuk LM., McCafferty DG., 2001, Synthesis of P(1)-Citronellyl-P(2)-alpha-D-pyranosyl pyrophosphates as potential substrates for the E. coli undecaprenyl-pyrophosphoryl-N-acetylglucoseaminyl transferase MurG., Bioorg Med Chem Lett 11(24):3107-10

 [8] Hu Y., Helm JS., Chen L., Ginsberg C., Gross B., Kraybill B., Tiyanont K., Fang X., Wu T., Walker S., 2004, Identification of selective inhibitors for the glycosyltransferase MurG via high-throughput screening., Chem Biol 11(5):703-11

 [9] Hyland SA., Anderson MS., 2003, A high-throughput solid-phase extraction assay capable of measuring diverse polyprenyl phosphate: sugar-1-phosphate transferases as exemplified by the WecA, MraY, and MurG proteins., Anal Biochem 317(2):156-65

 [10] Ikeda M., Wachi M., Jung HK., Ishino F., Matsuhashi M., 1990, Nucleotide sequence involving murG and murC in the mra gene cluster region of Escherichia coli., Nucleic Acids Res 18(13):4014

 [11] Liu H., Ritter TK., Sadamoto R., Sears PS., Wu M., Wong CH., 2003, Acceptor specificity and inhibition of the bacterial cell-wall glycosyltransferase MurG., Chembiochem 4(7):603-9

 [12] Mengin-Lecreulx D., Ayala J., Bouhss A., van Heijenoort J., Parquet C., Hara H., 1998, Contribution of the Pmra promoter to expression of genes in the Escherichia coli mra cluster of cell envelope biosynthesis and cell division genes., J Bacteriol 180(17):4406-12

 [13] Mengin-Lecreulx D., Parquet C., Desviat LR., Pla J., Flouret B., Ayala JA., van Heijenoort J., 1989, Organization of the murE-murG region of Escherichia coli: identification of the murD gene encoding the D-glutamic-acid-adding enzyme., J Bacteriol 171(11):6126-34

 [14] Mengin-Lecreulx D., Texier L., van Heijenoort J., 1990, Nucleotide sequence of the cell-envelope murG gene of Escherichia coli., Nucleic Acids Res 18(9):2810

 [15] Ravishankar S., Kumar VP., Chandrakala B., Jha RK., Solapure SM., de Sousa SM., 2005, Scintillation proximity assay for inhibitors of Escherichia coli MurG and, optionally, MraY., Antimicrob Agents Chemother 49(4):1410-8

 [16] Salmond GP., Lutkenhaus JF., Donachie WD., 1980, Identification of new genes in a cell envelope-cell division gene cluster of Escherichia coli: cell envelope gene murG., J Bacteriol 144(1):438-40

 [17] Wrabl JO., Grishin NV., 2001, Homology between O-linked GlcNAc transferases and proteins of the glycogen phosphorylase superfamily., J Mol Biol 314(3):365-74

 [18] Zawadzke LE., Wu P., Cook L., Fan L., Casperson M., Kishnani M., Calambur D., Hofstead SJ., Padmanabha R., 2003, Targeting the MraY and MurG bacterial enzymes for antimicrobial therapeutic intervention., Anal Biochem 314(2):243-52

 [19] van den Brink-van der Laan E., Boots JW., Spelbrink RE., Kool GM., Breukink E., Killian JA., de Kruijff B., 2003, Membrane interaction of the glycosyltransferase MurG: a special role for cardiolipin., J Bacteriol 185(13):3773-9

 [20] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.


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