A0A4Q9B3A8 · A0A4Q9B3A8_9DEIN

  • Protein
    ATP-dependent zinc metalloprotease FtsH
  • Gene
    ftsH
  • 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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.
The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

162450100150200250300350400450500550600
Type
IDPosition(s)Description
Binding site195-202ATP (UniProtKB | ChEBI)
Binding site417Zn2+ (UniProtKB | ChEBI); catalytic
Active site418
Binding site421Zn2+ (UniProtKB | ChEBI); catalytic
Binding site492Zn2+ (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
    • ORF names
      ETP66_07260

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CFH 72773T
  • Taxonomic lineage
    Bacteria > Deinococcota > Deinococci > Thermales > Thermaceae > Thermus

Accessions

  • Primary accession
    A0A4Q9B3A8

Proteomes

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Membrane

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane106-123Helical

Keywords

Interaction

Subunit

Homohexamer.

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain187-326AAA+ ATPase
Region589-624Disordered
Compositional bias595-612Basic and acidic 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
    624
  • Mass (Da)
    68,344
  • Last updated
    2019-07-31 v1
  • Checksum
    D258B0C5DB6CE0A5
MSRLPHLLVLVLAVFLLVWAFSLAGTPGGSGGAVNYTTFLEDLQAGRVKEVVVRAGDTRIQGTLTDGSTFTTFAASPPDNETLESWTKRGVSVRVEPPANPNPLGFLWPLLLVGLLVGALFYFSRAGRAGPSDGAFSFTKSRAKVLTEAPKVTFKDVAGAEEAKEELREIVEFLKNPARFHEMGARIPKGVLLVGPPGVGKTHIARAVAGEARVPFITASGSDFVEMFVGVGAARVRDLFETAKRHAPCIVFIDEIDAVGRRRGGGVGGGNDEREQTLNQLLVEMDGFEKDSTVIVMAATNRPDVLDPALLRPGRFDRQVAIDAPDVKGREQILRIHARGKPLAEDVDLALLAKRTPGFVGADLENLLNEAALLAAREGRKKITMKDLEEAADRVMMGPAKKSLVLTSRDRRITAYHEAGHALAAHYLEHVEGVHKVTIVPRGRALGFMMPRREDMLHWSRKRLLDQIAVALAGRAAEELVFEDVTTGAENDFRQATELARRMITEWGMHPEFGPVAYALREDTYLGGYDVRQYSEATAKRIDEAVRCLIEEQYGRVKTLLQERREVLERVAETLLEVETLTAEEFQRVVEGLPPEPAKPEEREEKEAPRVVPKVKPGGALGGA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias595-612Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SIJL01000008
EMBL· GenBank· DDBJ
TBH20152.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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