Q4J9K6 · FLAX_SULAC

Function

function

Component of the archaellum (PubMed:22081969, PubMed:23129770, PubMed:24103130, PubMed:26508112).
FlaX, FlaH and FlaI form the core cytoplasmic motor complex of the crenarchaeal archaellum (PubMed:24103130, PubMed:26508112).
FlaX forms a ring that may act as a membrane-bound cytoplasmic scaffold that guides the assembly of the archaellum motor complex (PubMed:24103130).
Is essential for archaellum assembly (PubMed:23129770).

Activity regulation

The presence of the flagellar core components FlaH, FlaI and FlaJ seems to be crucial for the stability of FlaX.

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 Componentarchaeal-type flagellum
Cellular Componentplasma membrane

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Archaeal flagellar motor scaffold protein FlaX

Gene names

    • Name
      flaX
    • Ordered locus names
      Saci_1177

Organism names

Accessions

  • Primary accession
    Q4J9K6

Proteomes

Subcellular Location

Archaeal flagellum
Cell membrane
; Single-pass membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-9Extracellular
Transmembrane10-30Helical
Topological domain31-250Cytoplasmic

Keywords

Phenotypes & Variants

Disruption phenotype

The deletion mutant lacks flagella and is non-motile.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004607321-250Archaeal flagellar motor scaffold protein FlaX

Expression

Induction

Part of the fla operon, which encodes the seven fla genes essential for crenarchaeal flagellum assembly and function (PubMed:22081969).
Expression is induced by tryptone starvation (PubMed:22081969).

Interaction

Subunit

The S.acidocaldarius archaellum assembly machinery and its filament consist of seven proteins (FlaB, FlaF, FlaG, FlaH, FlaI, FlaJ and FlaX) (PubMed:22081969).
FlaX assembles into ring-shaped oligomers (PubMed:23129770).
Interacts directly with FlaH and the motor ATPase FlaI (PubMed:23129770, PubMed:24103130, PubMed:26508112, PubMed:29605923).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q4J9K6Saci_1173 Q4J9L05EBI-8759763, EBI-8759747

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region.

TypeIDPosition(s)Description
Compositional bias42-68Polar residues
Region42-72Disordered

Domain

The C terminal region is involved in the oligomerization, but is also essential for interaction with FlaH and FlaI.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    250
  • Mass (Da)
    28,056
  • Last updated
    2005-08-02 v1
  • Checksum
    D5FBFCA640DF8E89
MAIQDLLQSSLFIILIGVGIPIAAFLEILFRVILPKTKRVQTQQSPQNISQEQRFPTQQKPANDETSKYSSDSIEKALKDVLGKMDKKENELLTNITNSFNEMKKLIENLNSAVEELALSVKASESDSSSPFNTIIQQEEEHVSREISTVSQLVGSNNPNNVNLTWFIKSCVLLEIMEYDEEKIKQLYELGYVSSDDMFTILRILSFIKNRKITAKELASIAANIAESYSSLTPEIKKYIMILEGGGVNG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias42-68Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000077
EMBL· GenBank· DDBJ
AAY80524.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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