A0A517PMS3 · A0A517PMS3_9PLAN

  • Protein
    ATP-dependent zinc metalloprotease FtsH
  • Gene
    ftsH_1
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

166450100150200250300350400450500550600650
TypeIDPosition(s)Description
Binding site239-246ATP (UniProtKB | ChEBI)
Binding site460Zn2+ (UniProtKB | ChEBI); catalytic
Active site461
Binding site464Zn2+ (UniProtKB | ChEBI); catalytic
Binding site536Zn2+ (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 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_1
    • Synonyms
      ftsH
    • ORF names
      HG66A1_24750

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • HG66A1
  • Taxonomic lineage
    Bacteria > Planctomycetota > Planctomycetia > Planctomycetales > Planctomycetaceae > Gimesia

Accessions

  • Primary accession
    A0A517PMS3

Proteomes

Subcellular Location

Cell membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane32-50Helical
Transmembrane144-166Helical

Keywords

Interaction

Subunit

Homohexamer.

Family & Domains

Features

Showing features for region, domain, compositional bias.

TypeIDPosition(s)Description
Region1-31Disordered
Domain231-370AAA+ ATPase
Region644-664Disordered
Compositional bias645-664Polar 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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    664
  • Mass (Da)
    73,132
  • Last updated
    2019-10-16 v1
  • Checksum
    4B60F52E6C1EA011
MASPQENPQRTPPPGKDPQKPSSKETQGAPSTGPWLIILLILVIGSLMMMKSSPENTGSKVDYSFFIDELNRGNVDSVEFHGDILTGKWKVRPKNPDDKEKKGEKLAEEFNTVLPSHPVEDRDLVPELIKQNVTFKAESTSVGIGTYILPWLIGPLLIIGFFWFMLRRSADPMGSGMLGNFTKSPAKRFRPSEEQTTFDDVAAMEQAKAELQEVVEFLKTPAKFQRLGAQIPKGVLLMGSPGTGKTLLARATAGEAGVPFYSINGSEFIQMFVGVGASRVRDLFRNAKENAPCIIFVDEIDAVGRIRGAGLGGGHDEREQTLNQMLSEMDGFQQNEAVIVIAATNRPDVLDPALLRPGRFDRHITVDRPTKEGRAAILKVHSRKIPLSDDVDLEKIAAGTIGFSGADLKNLVNEAALSATRLNKDQVDKEDFDNARDRVLMGPPREEILSEKEREMTAYHEAGHALLAWLLPEIDPVHKVTVIPRGRALGVTQLLPDEERYNMGEKQLHSQLAFMLGGRAAEGLVFGEHTAGAADDIKRATQITRKMVGQWGMSGVIGPVAFRHSDENPFLGKEMKSQGECSEETAHVIDQEMQRFLNAAEERAVKILTENREKLDLLAKALVEQEAIDSNDIKRLIGVSVREQANLDNAKQAGTDTENEQPPE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias645-664Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP036266
EMBL· GenBank· DDBJ
QDT20686.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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