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msbA ATP-binding lipopolysaccharide transport protein [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945530, updated on 23-Nov-2023

Summary

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Gene symbol
msbA
Gene description
ATP-binding lipopolysaccharide transport protein
Primary source
ASAP:ABE-0003113
Locus tag
b0914
See related
ECOCYC:EG10613
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK0905
Summary
MsbA PDB structures 1JSQ, 1PF4 and 1Z2R, and any conclusions derived from these structures, have been retracted due to a software data inversion error (Chang, 2006). [More information is available at EcoGene: EG10613]. Lipid A serves as a hydrophobic membrane anchor for the lipopolysaccharide, which is a major component of the outer leaflet of the outer membranes of Gram-negative bacteria. [More information is available at EcoCyc: EG10613].
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Genomic context

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Sequence:
NC_000913.3 (966621..968369)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene integration host factor subunit beta Neighboring gene metallo-beta-lactamase superfamily inner membrane protein YcaI Neighboring gene tetraacyldisaccharide 4'-kinase Neighboring gene interstrand DNA crosslink repair glycosylase Neighboring gene PF03966 family protein YcaR Neighboring gene 3-deoxy-manno-octulosonate cytidylyltransferase

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. The ABC transporter MsbA adopts the wide inward-open conformation in E. coli cells. Galazzo L, et al. Sci Adv, 2022 Oct 14. PMID 36223470, Free PMC Article
  2. Conformational States of ABC Transporter MsbA in a Lipid Environment Investigated by Small-Angle Scattering Using Stealth Carrier Nanodiscs. Josts I, et al. Structure, 2018 Aug 7. PMID 29937358
  3. The effect of drug binding on specific sites in transmembrane helices 4 and 6 of the ABC exporter MsbA studied by DNP-enhanced solid-state NMR. Spadaccini R, et al. Biochim Biophys Acta Biomembr, 2018 Apr. PMID 29069570
  4. Coupled ATPase-adenylate kinase activity in ABC transporters. Kaur H, et al. Nat Commun, 2016 Dec 22. PMID 28004795, Free PMC Article
  5. Allosteric transitions of ATP-binding cassette transporter MsbA studied by the adaptive anisotropic network model. Xie XL, et al. Proteins, 2015 Sep. PMID 26148303

See all (77) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. The ABC transporter MsbA adopts the wide inward-open conformation in E. coli cells.
    Title: The ABC transporter MsbA adopts the wide inward-open conformation in E. coli cells.
  2. The conformational states of the ABC transporter MsbA in a lipid environment investigated by small-angle scattering using stealth carrier nanodiscs have been reported.
    Title: Conformational States of ABC Transporter MsbA in a Lipid Environment Investigated by Small-Angle Scattering Using Stealth Carrier Nanodiscs.
  3. The ABC exporter MsbA can couple ATP hydrolysis to an adenylate kinase activity, where ADP is converted into AMP and ATP. Single-point mutations reveal that both ATPase and adenylate kinase mechanisms are associated with the same conserved motifs of the nucleotide-binding domain.
    Title: Coupled ATPase-adenylate kinase activity in ABC transporters.
  4. Data show that the conformational space of lipid ABC transporter MsbA changes upon vanadate trapping.
    Title: The effect of drug binding on specific sites in transmembrane helices 4 and 6 of the ABC exporter MsbA studied by DNP-enhanced solid-state NMR.
  5. Data show that the twisting motion of ATP-binding cassette transporter MsbA plays an important role for the rearrangement of transmembrane helices and the opening of transmembrane domains on the periplasmic side.
    Title: Allosteric transitions of ATP-binding cassette transporter MsbA studied by the adaptive anisotropic network model.
  6. Data indicate that E208A mutation interrupts the inward- to outward-facing conformational switch in ATP-binding cassette transport protein MsbA.
    Title: Molecular disruption of the power stroke in the ATP-binding cassette transport protein MsbA.
  7. Data show that the isolated MsbA nucleotide-binding domain hydrolyzed ATP with V(max) = 45 nmol mg(-1) min(-1), similar to the full-length transporter.
    Title: Time-resolved Fourier transform infrared spectroscopy of the nucleotide-binding domain from the ATP-binding Cassette transporter MsbA: ATP hydrolysis is the rate-limiting step in the catalytic cycle.
  8. Catalytic activity of MsbA reconstituted in nanodisc particles is modulated by remote interactions with the bilayer
    Title: Catalytic activity of MsbA reconstituted in nanodisc particles is modulated by remote interactions with the bilayer.
  9. analysis of the E506Q and H537A dysfunctional mutants in the E. coli ABC transporter MsbA
    Title: Characterization of the E506Q and H537A dysfunctional mutants in the E. coli ABC transporter MsbA.
  10. investigation of catalytic mechanism using mutants: L511P prevents effective ATP hydrolysis; D512G hydrolyzes ATP at rate 3-fold faster than wild type; both mutants bind ATP at near-wild-type levels but are unable to maintain cell viability
    Title: Effects of the L511P and D512G mutations on the Escherichia coli ABC transporter MsbA.
Submit: New GeneRIF Correction See all GeneRIFs (20)

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables ABC-type transporter activity IEA
Inferred from Electronic Annotation
more info
  
enables ABC-type xenobiotic transporter activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables ATP binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables ATP binding ISM
Inferred from Sequence Model
more info
 PubMed 
enables ATP hydrolysis activity IEA
Inferred from Electronic Annotation
more info
  
enables ATPase-coupled lipid transmembrane transporter activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables ATPase-coupled lipid transmembrane transporter activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables ATPase-coupled lipid transmembrane transporter activity IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables lipid binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables lipopolysaccharide floppase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables nucleotide binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
acts_upstream_of_or_within lipid translocation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in lipid transport IEA
Inferred from Electronic Annotation
more info
  
involved_in lipid transport IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within lipopolysaccharide transport IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in lipopolysaccharide transport IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in transmembrane transport IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in transmembrane transport IEA
Inferred from Electronic Annotation
more info
  
involved_in xenobiotic transport IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
part_of ATP-binding cassette (ABC) transporter complex IDA
Inferred from Direct Assay
more info
 PubMed 
part_of ATP-binding cassette (ABC) transporter complex RCA
inferred from Reviewed Computational Analysis
more info
 PubMed 
part_of MsbA transporter complex IPI
Inferred from Physical Interaction
more info
 PubMed 
located_in membrane HDA PubMed 
located_in membrane IEA
Inferred from Electronic Annotation
more info
  
located_in plasma membrane IDA
Inferred from Direct Assay
more info
 PubMed 
located_in plasma membrane IEA
Inferred from Electronic Annotation
more info
  
located_in plasma membrane ISM
Inferred from Sequence Model
more info
 PubMed 

General protein information

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Preferred Names
ATP-binding lipopolysaccharide transport protein
NP_415434.1

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    966621..968369
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415434.1 ATP-binding lipopolysaccharide transport protein [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415434.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A376RMT3, A0A827Y4A4
    Conserved Domains (1) summary
    PRK11176
    Location:1 → 582
    PRK11176; lipid A ABC transporter ATP-binding protein/permease MsbA
Nucleotide Protein
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