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Q66CI3 · MSBA_YERPS

Function

function

Involved in lipopolysaccharide (LPS) biosynthesis. Translocates lipid A-core from the inner to the outer leaflet of the inner membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.

Catalytic activity

  • ATP + H2O + lipid A-core oligosaccharideSide 1 = ADP + phosphate + lipid A-core oligosaccharideSide 2.
    EC:7.5.2.6 (UniProtKB | ENZYME | Rhea)

Features

Showing features for binding site.

158250100150200250300350400450500550
TypeIDPosition(s)Description
Binding site376-383ATP (UniProtKB | ChEBI)

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentplasma membrane
Molecular FunctionABC-type transporter activity
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATPase-coupled lipid transmembrane transporter activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent lipid A-core flippase
  • EC number
  • Alternative names
    • Lipid A export ATP-binding/permease protein MsbA

Gene names

    • Name
      msbA
    • Ordered locus names
      YPTB1420

Organism names

Accessions

  • Primary accession
    Q66CI3

Proteomes

Subcellular Location

Cell inner membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane25-45Helical
Transmembrane69-89Helical
Transmembrane137-159Helical
Transmembrane253-273Helical
Transmembrane275-295Helical

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000926111-582ATP-dependent lipid A-core flippase

Interaction

Subunit

Homodimer.

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain28-310ABC transmembrane type-1
Domain342-578ABC transporter

Domain

In MsbA the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    582
  • Mass (Da)
    64,462
  • Last updated
    2004-10-11 v1
  • MD5 Checksum
    0F0910E0DF9785CC95DC053B9E0B534F
MMNDKDLSTWQTFRRLWPTISPYKAGLIVAAIALILNAASDTFMLSLLKPLLDDGFGNSNSSILKWMPLAVIGLMVVRGVTGFVSSYCISWVSGKVVMHIRRRLFSHMMGMPVSFFDQQSTGTLLSRITYDSEQVAASSSSALVTVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVSISIRLVSKRFRNISKNMQNTMGEVTTSAEQMLKGHKEVLIFGGQKVETERFDAVSNRMRQQGMKLVSASSISDPIIQLIASFALALVLYAASFPSVMETLTAGTITVVFSAMIALMRPLKSLTNVNTQFQRGMAACQTLFSILDMEQEKDEGKLEVERAKGDIEFRHVTFYYPGKDTPALNDINIHLEAGKTVALVGRSGSGKSTIANLLTRFYDVSEGSILLDGHDLRDYRLGALRNQVALVSQNVHLFNDTVANNIAYARNEQYSRAEIEEAARMAYAMDFINKMEHGLDTVIGENGIMLSGGQRQRIAIARALLRNCPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIVVIEDGRIVERGVHAELLVQQGVYAQLNRMQFGQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BX936398
EMBL· GenBank· DDBJ
CAH20660.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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