RegulonDB RegulonDB 11.2: Gene Form
   

nuoL gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

nuoL nuoM nuoJ nuoK TSS_2539 TSS_2539 TSS_2538 TSS_2538 TSS_2537 TSS_2537 TSS_2536 TSS_2536 TSS_2535 TSS_2535 TSS_2534 TSS_2534 nuoNp1 nuoNp1

Gene      
Name: nuoL    Texpresso search in the literature
Synonym(s): ECK2272, EG12092, b2278
Genome position(nucleotides): 2393205 <-- 2395046
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 57.17
External database links:  
ASAP:
 ABE-0007532
CGSC:
 32646
ECHOBASE:
 EB2016
ECOLIHUB:
 nuoL
MIM:
 540000
MIM:
 256000
MIM:
 252010
MIM:
 535000
OU-MICROARRAY:
 b2278
STRING:
 511145.b2278
COLOMBOS: nuoL


Product      
Name: NADH:quinone oxidoreductase subunit L
Synonym(s): NADH:ubiquinone oxidoreductase, membrane subunit L, NuoL
Sequence: Get amino acid sequence Fasta Format
Cellular location: inner membrane
Molecular weight: 66.438
Isoelectric point: 8.404
Motif(s):
 
Type Positions Sequence Comment
7 -> 23 TIILPLIGFVLLAFSRG UniProt: Helical.
32 -> 52 IVGVGSVGLAALVTAFIGVDF UniProt: Helical.
39 -> 39 G UniProt: In Ref. 1; CAA48371..
47 -> 58 FIGVDFFANGEQ UniProt: In Ref. 1; CAA48371..
67 -> 117 WMSVGDFNIGFNLVLDGLSLTMLSVVTGVGFLIHMYASWYMRGEEGYSRFF

 
Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.3 - energy metabolism, carbon --> 1.3.6 - aerobic respiration
  1 - metabolism --> 1.3 - energy metabolism, carbon --> 1.3.7 - anaerobic respiration
  1 - metabolism --> 1.4 - energy production/transport --> 1.4.1 - electron donors
  4 - transport --> 4.3 - Primary Active Transporters --> 4.3.D - Oxidoreduction-driven Active Transporters
  6 - cell structure --> 6.1 - membrane
Gene Ontology Terms (GO)  
cellular_component GO:0016020 - membrane
GO:0005886 - plasma membrane
GO:0005887 - integral component of plasma membrane
GO:0016021 - integral component of membrane
GO:0030964 - NADH dehydrogenase complex
GO:0045271 - respiratory chain complex I
GO:0045272 - plasma membrane respiratory chain complex I
molecular_function GO:0003954 - NADH dehydrogenase activity
GO:0008137 - NADH dehydrogenase (ubiquinone) activity
GO:0048038 - quinone binding
biological_process GO:0015990 - electron transport coupled proton transport
GO:0042773 - ATP synthesis coupled electron transport
GO:0022904 - respiratory electron transport chain
Note(s): Note(s): ...[more].
Reference(s): [1] Gustavsson T., et al., 2010
[2] Kaila VR., et al., 2014
[3] Kriegel S., et al., 2015
[4] Sperling E., et al., 2016
External database links:  
ALPHAFOLD:
 P33607
DIP:
 DIP-10388N
ECOCYC:
 NUOL-MONOMER
ECOLIWIKI:
 b2278
INTERPRO:
 IPR018393
INTERPRO:
 IPR003945
INTERPRO:
 IPR001750
INTERPRO:
 IPR001516
PFAM:
 PF00361
PFAM:
 PF00662
PRIDE:
 P33607
PRINTS:
 PR01435
PRODB:
 PRO_000023439
REFSEQ:
 NP_416781
SMR:
 P33607
UNIPROT:
 P33607


Operon      
Name: nuoABCEFGHIJKLMN         
Operon arrangement:
Transcription unit        Promoter
nuoABCEFGHIJKLMN
nuoABCEFGHIJKLMN
nuoMN


Transcriptional Regulation      
Display Regulation             
Activated by: NarL, Fis
Repressed by: FNR, IHF, ArcA


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 nuoNp1 2391717 reverse nd [COMP-AINF] [5]
  promoter TSS_2534 2393605 reverse nd [RS-EPT-CBR] [6]
  promoter TSS_2535 2393635 reverse nd [RS-EPT-CBR] [6]
  promoter TSS_2536 2393749 reverse nd [RS-EPT-CBR] [6]
  promoter TSS_2537 2394474 reverse nd [RS-EPT-CBR] [6]
  promoter TSS_2538 2394595 reverse nd [RS-EPT-CBR] [6]
  promoter TSS_2539 2394680 reverse nd [RS-EPT-CBR] [6]


Evidence    

 [COMP-AINF] Inferred computationally without human oversight

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


Reference(s)    

 [1] Gustavsson T., Trane M., Moparthi VK., Miklovyte E., Moparthi L., Gorecki K., Leiding T., Arskold SP., Hagerhall C., 2010, A cytochrome c fusion protein domain for convenient detection, quantification, and enhanced production of membrane proteins in Escherichia coli--expression and characterization of cytochrome-tagged Complex I subunits., Protein Sci 19(8):1445-60

 [2] Kaila VR., Wikstrom M., Hummer G., 2014, Electrostatics, hydration, and proton transfer dynamics in the membrane domain of respiratory complex I., Proc Natl Acad Sci U S A 111(19):6988-93

 [3] Kriegel S., Srour B., Steimle S., Friedrich T., Hellwig P., 2015, Involvement of Acidic Amino Acid Residues in Zn(2+) Binding to Respiratory Complex I., Chembiochem 16(14):2080-5

 [4] Sperling E., Gorecki K., Drakenberg T., Hagerhall C., 2016, Functional Differentiation of Antiporter-Like Polypeptides in Complex I; a Site-Directed Mutagenesis Study of Residues Conserved in MrpA and NuoL but Not in MrpD, NuoM, and NuoN., PLoS One 11(7):e0158972

 [5] Huerta AM., Collado-Vides J., 2003, Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals., J Mol Biol 333(2):261-78

 [6] 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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