RegulonDB RegulonDB 11.1: Gene Form
   

lpxC gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

ftsZ lpxC secM TSS_198 TSS_198 TSS_197 TSS_197 TSS_196 TSS_196 TSS_195 TSS_195 TSS_194 TSS_194 lpxCp2 lpxCp2 lpxCp1 lpxCp1 TSS_192 TSS_192 TSS_191 TSS_191 TSS_190 TSS_190 TSS_189 (cluster) TSS_189 (cluster)

Gene      
Name: lpxC    Texpresso search in the literature
Synonym(s): ECK0097, EG10265, asmB, b0096, envA
Genome position(nucleotides): 106557 --> 107474
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 51.09
External database links:  
ASAP:
 ABE-0000336
CGSC:
 815
ECHOBASE:
 EB0261
ECOLIHUB:
 lpxC
OU-MICROARRAY:
 b0096
STRING:
 511145.b0096
COLOMBOS: lpxC


Product      
Name: UDP-3-O-acyl-N-acetylglucosamine deacetylase
Synonym(s): AsmB, EnvA, LpxC
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 33.956
Isoelectric point: 5.639
Motif(s):
 
Type Positions Sequence Comment
4 -> 276 QRTLKRIVQATGVGLHTGKKVTLTLRPAPANTGVIYRRTDLNPPVDFPADAKSVRDTMLCTCLVNEHDVRISTVEHLNAALAGLGIDNIVIEVNAPEIPIMDGSAAPFVYLLLDAGIDELNCAKKFVRIKETVRVEDGDKWAEFKPYNGFSLDFTIDFNHPAIDSSNQRYAMNFSADAFMRQISRARTFGFMRDIEYLQSRGLCLGGSFDCAIVVDDYRVLNEDGLRFEDEFVRHKMLDAIGDLFMCGHNIIGAFTAYKSGHALNNKLLQAVL
19 -> 19 H UniProt: 200-fold decrease in activity..
50 -> 50 F UniProt: In ASMB2/3; reduced activity..
63 -> 63 C UniProt: Reduces level of inhibition by metal ions..
78 -> 78 E UniProt: 700-fold decrease in activity..

 
Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.6 - biosynthesis of macromolecules (cellular constituents) --> 1.6.3 - lipopolysaccharide --> 1.6.3.3 - lipid A
  6 - cell structure --> 6.3 - surface antigens (ECA, O antigen of LPS)
Gene Ontology Terms (GO)  
cellular_component GO:0005737 - cytoplasm
GO:0005829 - cytosol
molecular_function GO:0016787 - hydrolase activity
GO:0046872 - metal ion binding
GO:0008270 - zinc ion binding
GO:0019213 - deacetylase activity
GO:0005506 - iron ion binding
GO:0008759 - UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine deacetylase activity
GO:0103117 - UDP-3-O-acyl-N-acetylglucosamine deacetylase activity
biological_process GO:0006629 - lipid metabolic process
GO:0009245 - lipid A biosynthetic process
Note(s): Note(s): ...[more].
Reference(s): [1] Langklotz S., et al., 2011
[2] Westphal K., et al., 2012
External database links:  
ALPHAFOLD:
 P0A725
DIP:
 DIP-48045N
ECOCYC:
 UDPACYLGLCNACDEACETYL-MONOMER
ECOLIWIKI:
 b0096
INTERPRO:
 IPR015870
INTERPRO:
 IPR011334
INTERPRO:
 IPR004463
INTERPRO:
 IPR020568
MODBASE:
 P0A725
PANTHER:
 PTHR33694
PDB:
 4ISA
PDB:
 4MQY
PDB:
 4IS9
PDB:
 4MDT
PFAM:
 PF03331
PRIDE:
 P0A725
PRODB:
 PRO_000023122
REFSEQ:
 NP_414638
SMR:
 P0A725
UNIPROT:
 P0A725


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
rsmH-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
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_189 (cluster) 105669 forward nd [RS-EPT-CBR] [3]
  promoter TSS_190 105677 forward nd [RS-EPT-CBR] [3]
  promoter TSS_191 105795 reverse nd [RS-EPT-CBR] [3]
  promoter TSS_192 105816 forward nd [RS-EPT-CBR] [3]
  promoter TSS_194 106940 forward nd [RS-EPT-CBR] [3]
  promoter TSS_195 107603 forward nd [RS-EPT-CBR] [3]
  promoter TSS_196 107668 forward nd [RS-EPT-CBR] [3]
  promoter TSS_197 108025 forward nd [RS-EPT-CBR] [3]
  promoter TSS_198 108134 forward nd [RS-EPT-CBR] [3]


Evidence    

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


Reference(s)    

 [1] Langklotz S., Schakermann M., Narberhaus F., 2011, Control of lipopolysaccharide biosynthesis by FtsH-mediated proteolysis of LpxC is conserved in enterobacteria but not in all gram-negative bacteria., J Bacteriol 193(5):1090-7

 [2] Westphal K., Langklotz S., Thomanek N., Narberhaus F., 2012, A trapping approach reveals novel substrates and physiological functions of the essential protease FtsH in Escherichia coli., J Biol Chem 287(51):42962-71

 [3] 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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