RegulonDB RegulonDB 10.10: Gene Form
   

lolB gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

hemA prs ispE lolB FNR PurR anti-anti-terminator anti-terminator TSS_1544 (cluster) TSS_1544 (cluster) TSS_1543 (cluster) TSS_1543 (cluster) hemAp1 hemAp1 TSS_1542 TSS_1542 hemAp2 hemAp2 lolBp lolBp TSS_1541 (cluster) TSS_1541 (cluster) prsp prsp TSS_1540 TSS_1540 TSS_1539 TSS_1539 TSS_1538 TSS_1538

Gene      
Name: lolB    Texpresso search in the literature
Synonym(s): ECK1197, EG11293, b1209, hemM, ychC
Genome position(nucleotides): 1262877 <-- 1263500 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 51.44
External database links:  
ASAP:
 ABE-0004059
CGSC:
 31940
ECHOBASE:
 EB1270
ECOLIHUB:
 lolB
OU-MICROARRAY:
 b1209
STRING:
 511145.b1209
COLOMBOS: lolB


Product      
Name: outer membrane lipoprotein LolB
Synonym(s): HemM, LolB, YchC
Sequence: Get amino acid sequence Fasta Format
Cellular location: outer membrane,periplasmic space
Molecular weight: 23.551
Isoelectric point: 9.18
Motif(s):
 
Type Positions Sequence
41 -> 42 QH
138 -> 138 W
1 -> 21 MPLPDFRLIRLLPLAALVLTA
176 -> 207 YDTKTQPAMPANMELTDGGQRIKLKMDNWIVK
12 -> 12 L

 
Classification:
Multifun Terms (GenProtEC)  
Gene Ontology Terms (GO)  
cellular_component GO:0009279 - cell outer membrane
GO:0016020 - membrane
GO:0030288 - outer membrane-bounded periplasmic space
GO:0036406 - anchored component of periplasmic side of cell outer membrane
molecular_function GO:0005515 - protein binding
biological_process GO:0042157 - lipoprotein metabolic process
GO:0015031 - protein transport
GO:0044874 - lipoprotein localization to outer membrane
Note(s): Note(s): ...[more].
Evidence: [APPH] Assay of protein purified to homogeneity
[IMP] Inferred from mutant phenotype
Reference(s): [1] Hayashi Y., et al., 2014
[2] Matsuyama S., et al., 1997
[3] Nakada S., et al., 2007
[4] Pedebos C., et al., 2021
[5] Rao S., et al., 2020
[6] Svanberg Frisinger F., et al., 2021
[7] Tsukahara J., et al., 2009
[8] Wada R., et al., 2004
[9] Yokota N., et al., 1999
External database links:  
DIP:
 DIP-35933N
ECOCYC:
 EG11293-MONOMER
ECOLIWIKI:
 b1209
INTERPRO:
 IPR004565
INTERPRO:
 IPR029046
MINT:
 P61320
MODBASE:
 P61320
PDB:
 1IWN
PDB:
 1IWM
PFAM:
 PF03550
PRIDE:
 P61320
PRODB:
 PRO_000023104
PROSITE:
 PS51257
REFSEQ:
 NP_415727
SMR:
 P61320
UNIPROT:
 P61320


Operon      
Name: lolB-ispE-prs         
Operon arrangement:
Transcription unit        Promoter
prs
lolB-ispE-prs


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_1538 1260982 reverse nd [RS-EPT-CBR] [10]
  promoter TSS_1539 1261162 reverse nd [RS-EPT-CBR] [10]
  promoter TSS_1540 1261821 reverse nd [RS-EPT-CBR] [10]
  promoter TSS_1541 (cluster) 1263536 reverse nd [RS-EPT-CBR] [10]
  promoter TSS_1542 1263675 forward nd [RS-EPT-CBR] [10]
  promoter TSS_1543 (cluster) 1264894 forward nd [RS-EPT-CBR] [10]
  promoter TSS_1544 (cluster) 1264899 forward nd [RS-EPT-CBR] [10]


Evidence    

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


Reference(s)    

 [1] Hayashi Y., Tsurumizu R., Tsukahara J., Takeda K., Narita S., Mori M., Miki K., Tokuda H., 2014, Roles of the protruding loop of factor B essential for the localization of lipoproteins (LolB) in the anchoring of bacterial triacylated proteins to the outer membrane., J Biol Chem 289(15):10530-9

 [2] Matsuyama S., Yokota N., Tokuda H., 1997, A novel outer membrane lipoprotein, LolB (HemM), involved in the LolA (p20)-dependent localization of lipoproteins to the outer membrane of Escherichia coli., EMBO J 16(23):6947-55

 [3] Nakada S., Sakakura M., Takahashi H., Tokuda H., Shimada I., 2007, Backbone resonance assignment for the outer membrane lipoprotein receptor LolB from Escherichia coli., Biomol NMR Assign 1(1):121-3

 [4] Pedebos C., Smith IPS., Boags A., Khalid S., 2021, The hitchhiker's guide to the periplasm: Unexpected molecular interactions of polymyxin B1 in E. coli., Structure 29(5):444-456.e2

 [5] Rao S., Bates GT., Matthews CR., Newport TD., Vickery ON., Stansfeld PJ., 2020, Characterizing Membrane Association and Periplasmic Transfer of Bacterial Lipoproteins through Molecular Dynamics Simulations., Structure 28(4):475-487.e3

 [6] Svanberg Frisinger F., Jana B., Donadio S., Guardabassi L., 2021, In Silico Prediction and Prioritization of Novel Selective Antimicrobial Drug Targets in Escherichia coli., Antibiotics (Basel) 10(6)

 [7] Tsukahara J., Narita S., Tokuda H., 2009, Real time analysis of lipoprotein transfer from LolA to LolB by means of surface plasmon resonance., FEBS Lett 583(18):2987-90

 [8] Wada R., Matsuyama S., Tokuda H., 2004, Targeted mutagenesis of five conserved tryptophan residues of LolB involved in membrane localization of Escherichia coli lipoproteins., Biochem Biophys Res Commun 323(3):1069-74

 [9] Yokota N., Kuroda T., Matsuyama S., Tokuda H., 1999, Characterization of the LolA-LolB system as the general lipoprotein localization mechanism of Escherichia coli., J Biol Chem 274(43):30995-9

 [10] 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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