RegulonDB RegulonDB 10.10: Gene Form
   

ompX gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

opgE ompX yliM MicA CyaR ompXp2 ompXp2

Gene      
Name: ompX    Texpresso search in the literature
Synonym(s): ECK0803, EG12117, b0814, ompP, ybiG
Genome position(nucleotides): 850450 --> 850965 Genome Browser
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
51.36
External database links:  
ASAP:
ABE-0002784
ECHOBASE:
EB2056
ECOLIHUB:
ompX
OU-MICROARRAY:
b0814
STRING:
511145.b0814
COLOMBOS: ompX


Product      
Name: outer membrane protein X
Synonym(s): OmpP, OmpX, YbiG
Sequence: Get amino acid sequence Fasta Format
Cellular location: outer membrane
Molecular weight: 18.603
Isoelectric point: 7.322
Motif(s):
 
Type Positions Sequence
1 -> 23 MKKIACLSALAAVLAFTAGTSVA
60 -> 69 LGVIGSFTYT
24 -> 171 ATSTVTGGYAQSDAQGQMNKMGGFNLKYRYEEDNSPLGVIGSFTYTEKSRTASSGDYNKNQYYGITAGPAYRINDWASIYGVVGVGYGKFQTTEYPTYKHDTSDYGFSYGAGLQFNPMENVALDFSYEQSRIRSVDVGTWIAGVGYRF
161 -> 170 GTWIAGVGYR
9 -> 171 ALAAVLAFTAGTSVAATSTVTGGYAQSDAQGQMNKMGGFNLKYRYEEDNSPLGVIGSFTYTEKSRTASSGDYNKNQYYGITAGPAYRINDWASIYGVVGVGYGKFQTTEYPTYKHDTSDYGFSYGAGLQFNPMENVALDFSYEQSRIRSVDVGTWIAGVGYRF

 

Classification:
Multifun Terms (GenProtEC)  
  8 - extrachromosomal --> 8.1 - prophage genes and phage related functions
Gene Ontology Terms (GO)  
cellular_component GO:0044384 - host outer membrane
GO:0009279 - cell outer membrane
GO:0016020 - membrane
GO:0016021 - integral component of membrane
molecular_function GO:0005515 - protein binding
Note(s): Note(s): ...[more].
Reference(s): [1] Burmann BM., et al., 2013
[2] Chaturvedi D., et al., 2013
[3] Choutko A., et al., 2011
[4] Frey L., et al., 2018
[5] Hagn F., et al., 2015
[6] Mahalakshmi R., et al., 2008
[7] Rath P., et al., 2020
[8] Rath P., et al., 2019
[9] Shearer J., et al., 2019
[10] Vaiphei ST., et al., 2011
[11] Zhang Z., et al., 2021
External database links:  
DIP:
DIP-48016N
ECOCYC:
EG12117-MONOMER
ECOLIWIKI:
b0814
INTERPRO:
IPR000758
INTERPRO:
IPR011250
INTERPRO:
IPR027385
MINT:
P0A917
MODBASE:
P0A917
PDB:
2MNH
PDB:
2M07
PDB:
2M06
PDB:
1QJ9
PDB:
1QJ8
PDB:
1Q9G
PDB:
1Q9F
PDB:
1ORM
PFAM:
PF13505
PRIDE:
P0A917
PRINTS:
PR00316
PRODB:
PRO_000023460
PROSITE:
PS00695
PROSITE:
PS00694
REFSEQ:
NP_415335
SMR:
P0A917
UNIPROT:
P0A917


Operon      
Name: yliM-ompX         
Operon arrangement:
Transcription unit        Promoter
yliM-ompX
ompX


Transcriptional Regulation      
Display Regulation             
Repressed by: FNR


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


Reference(s)    

 [1] Burmann BM., Wang C., Hiller S., 2013, Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp., Nat Struct Mol Biol 20(11):1265-72

 [2] Chaturvedi D., Mahalakshmi R., 2013, Methionine mutations of outer membrane protein X influence structural stability and beta-barrel unfolding., PLoS One 8(11):e79351

 [3] Choutko A., Glattli A., Fernandez C., Hilty C., Wuthrich K., van Gunsteren WF., 2011, Membrane protein dynamics in different environments: simulation study of the outer membrane protein X in a lipid bilayer and in a micelle., Eur Biophys J 40(1):39-58

 [4] Frey L., Hiller S., Riek R., Bibow S., 2018, Lipid- and Cholesterol-Mediated Time-Scale-Specific Modulation of the Outer Membrane Protein X Dynamics in Lipid Bilayers., J Am Chem Soc 140(45):15402-15411

 [5] Hagn F., Wagner G., 2015, Structure refinement and membrane positioning of selectively labeled OmpX in phospholipid nanodiscs., J Biomol NMR 61(3-4):249-60

 [6] Mahalakshmi R., Marassi FM., 2008, Orientation of the Escherichia coli Outer Membrane Protein OmpX in Phospholipid Bilayer Membranes Determined by Solid-State NMR., Biochemistry

 [7] Rath P., Sharpe T., Hiller S., 2020, The electrostatic core of the outer membrane protein X from E. coli., Biochim Biophys Acta Biomembr 1862(1):183031

 [8] Rath P., Sharpe T., Kohl B., Hiller S., 2019, Two-State Folding of the Outer Membrane Protein X into a Lipid Bilayer Membrane., Angew Chem Int Ed Engl 58(9):2665-2669

 [9] Shearer J., Jefferies D., Khalid S., 2019, Outer Membrane Proteins OmpA, FhuA, OmpF, EstA, BtuB, and OmpX Have Unique Lipopolysaccharide Fingerprints., J Chem Theory Comput 15(4):2608-2619

 [10] Vaiphei ST., Tang Y., Montelione GT., Inouye M., 2011, The use of the condensed single protein production system for isotope-labeled outer membrane proteins, OmpA and OmpX in E. coli., Mol Biotechnol 47(3):205-10

 [11] Zhang Z., Ryoo D., Balusek C., Acharya A., Rydmark MO., Linke D., Gumbart JC., 2021, Inward-facing glycine residues create sharp turns in β-barrel membrane proteins., Biochim Biophys Acta Biomembr 1863(10):183662


RegulonDB