A0A0Q6DW80 · A0A0Q6DW80_9HYPH

  • 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.

164250100150200250300350400450500550600
Type
IDPosition(s)Description
Binding site198-205ATP (UniProtKB | ChEBI)
Binding site420Zn2+ (UniProtKB | ChEBI); catalytic
Active site421
Binding site424Zn2+ (UniProtKB | ChEBI); catalytic
Binding site498Zn2+ (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
      ASG54_20305

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Leaf460
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Aurantimonadaceae > Aureimonas

Accessions

  • Primary accession
    A0A0Q6DW80

Proteomes

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Membrane

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane105-125Helical

Keywords

Interaction

Subunit

Homohexamer.

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain190-329AAA+ ATPase
Region604-642Disordered
Compositional bias618-642Polar 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
    642
  • Mass (Da)
    69,854
  • Last updated
    2016-01-20 v1
  • MD5 Checksum
    06BA6F1F129914CC59593F2FA5D12637
MNQNFRNFALWAIIALLLIALFQLFSSGTQGAASREIPYSQFLSDVDSGRVRAVTIQGPRITGNYSDGSNGFQTYSPGDPNVVSRLEGKGVTITASPPSDNSNPIWSMLLSFGPILLILGVWIFLMRQMQGGAGGKAMGFGKSKAKLLTEAHGRVTFGDVAGVDEAKQDLEEIVEFLREPQKFQRLGGKIPRGVLLVGPPGTGKTLLARSVAGEANVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKNSPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDRQVMVPNPDVGGREKILKVHVRNVPLAPNVDLKTIARGTPGFSGADLANLVNEAALMAARRSKRLVTMLEFEDAKDKVMMGAERRSMAMTEDEKALTAYHEAGHALVGIHEPFNDPLHKVTIIPRGRALGVTMNLPERDRYGMRKNEMEARLVMIFGGRAAEEIIYGLDNVTTGASNDIQQATNMARAMVMEYGMSDKLGRLRYRQNQEEIFLGHSVSQQQNMSEDTARLIDSEVRGIVEVAENKARKILNERIDELHIVAKGLLEYETLSGDEVRDLIAGKTLARDMGDDTPPSRGSAVPKTGSIKPSGSQEGGLEPQPSV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias618-642Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LMQY01000037
EMBL· GenBank· DDBJ
KQT70949.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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