A0AAC9FC13 · A0AAC9FC13_9ACTN

Function

function

Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

1749100200300400500600700
Type
IDPosition(s)Description
Binding site208-215ATP (UniProtKB | ChEBI)
Binding site430Zn2+ (UniProtKB | ChEBI); catalytic
Active site431
Binding site434Zn2+ (UniProtKB | ChEBI); catalytic
Binding site506Zn2+ (UniProtKB | ChEBI); catalytic

GO annotations

AspectTerm
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent peptidase activity
Molecular Functionmetalloendopeptidase activity
Molecular Functionzinc ion binding
Biological Processcell division
Biological Processprotein catabolic process
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent zinc metalloprotease FtsH
  • EC number

Gene names

    • Name
      ftsH
    • ORF names
      AXH35_07295

Organism names

  • Taxonomic identifier
  • Strain
    • ATCC 55737
  • Taxonomic lineage
    Bacteria > Actinomycetota > Actinomycetes > Propionibacteriales > Propionibacteriaceae > Acidipropionibacterium

Accessions

  • Primary accession
    A0AAC9FC13

Proteomes

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Membrane

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane116-134Helical

Keywords

Interaction

Subunit

Homohexamer.

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain200-339AAA+ ATPase
Region615-749Disordered
Compositional bias707-729Polar residues

Sequence similarities

Belongs to the AAA ATPase family.
In the C-terminal section; belongs to the peptidase M41 family.
In the central section; belongs to the AAA ATPase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    749
  • Mass (Da)
    79,727
  • Last updated
    2024-05-29 v1
  • Checksum
    F75F44C9D7406B69
MKNASRIFRGPLLWILLAIIAIITVLNLTSSMAGAKDIPTSQAVSMINGNDKLKEVVLTDGDQTIQITNAKGEQFRSHWVGDQSDKIIDRLNQRVENKTITTWRGENPGPSVWKSLLVNMLPFVIMIVVFLWFFNAAQGGMGGRGGVMNFGKSKANVGTKDTPKTTFKDVAGVQEAIDELQEIREFLSEPAKFQRVGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQAKEAAPAIIFIDEIDAVGRHRGAGMGGGHDEREQTLNQLLVEMDGFDVHGGVILIAATNRPDVLDPALLRPGRFDRQIAVEAPDMEGRVKILQVHAEGKPMADNVDLASIARRTPGMTGADLANVLNEAALLTARNNLPVIGNGELDEAIDRVIAGPQKKTRIMDDHERLVTAYHEGGHALVAAAMPGTDPVQKITILPRGRALGYTMVMPDSDKYSQTRGELLDQMAYMMGGRAAEELIFHDPSTGASNDIEKATKVARAMVTQYGLSAKIGTVQLGSGDSEPFLGMTAGQDRDYSEQTASVVDGEVRVLLENAHQEAFDCLVANRPVLDELVRQLFAKETLSKAEVADVFQALQKWPSRGSFTGSDKRIPSTVPPITPPPVPSAADPKGAISTGTATSTAAPAADPAAGNQQADGSAPAWHAPSDWAPPSWNPSQGPEQHEAGPRTDPGQAPGQQDSAQQGPGESGSDGRSSDGGSAGDDGSDGQNPWAPRQ

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias707-729Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP014352
EMBL· GenBank· DDBJ
AMS05293.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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