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A0A4Y8P7D1 · A0A4Y8P7D1_9BACT

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

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.

163950100150200250300350400450500550600
Type
IDPosition(s)Description
Binding site220-227ATP (UniProtKB | ChEBI)
Binding site442Zn2+ (UniProtKB | ChEBI); catalytic
Active site443
Binding site446Zn2+ (UniProtKB | ChEBI); catalytic
Binding site519Zn2+ (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
      A7Q10_02180

Organism names

  • Taxonomic identifier
  • Strain
    • Phi
  • Taxonomic lineage
    Bacteria > Verrucomicrobiota > Methylacidiphilae > Methylacidiphilales > Methylacidiphilaceae > Methylacidiphilum (ex Ratnadevi et al. 2023)

Accessions

  • Primary accession
    A0A4Y8P7D1

Proteomes

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Membrane

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane21-39Helical
Transmembrane132-160Helical

Keywords

Interaction

Subunit

Homohexamer.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain212-351AAA+ ATPase

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
    639
  • Mass (Da)
    70,872
  • Last updated
    2019-09-18 v1
  • MD5 Checksum
    D209856670785DD3D6BD399CAEDF2965
MKLSTTKRNLPPQKNNEPPFPYVRFLIQIGIALFLVWIWQESLHKATVSTIPYSEFLNKLNQKEIIECKITPDEIYGKMLISKPEEKGKPPKIGLFSTVRVDDPDLVKRLQAAGVVYGSVKPSLLSQILFSWVVPILIFFLVWFVLARFVGGGGAGYSLLNIGKSRARLLVDESTGVTFADVAGCDEAKYELQEVVDFLKNPSRYRALGAKIPKGVLLVGPPGTGKTLLAKAVAGEAKVPFFSISGSEFVEMFVGVGAARVRDLFGQAKSKAPCIVFIDELDAIGRQRGVRIQIGSDEHEQTLNQLLVEMDGFDPNEGIIVLAATNRPEILDRALLRPGRFDRQVVVDLPDANGREAILRVHARGKPLSANIDFKEIAQATMGFSGADLANLLNEAALLAARRKSSSIEQIDLLEAMEKVIAGPERKSRILSEKERERVAYHEVGHALTAYYCEHAEPVRKISIVPRGKSALGYTLQLPTIQKYLMTKSELLDRICVAMGGRAAEELIYGDITTGAENDLEVATTIARQMVCLYGMGEKSGLAHYVPPQPLLGGLDNSYLKECSNETARIIDLEIEKILEENYQRALSLLRHHHAELKEVTKHLLEKETLNADEFKRILDQLKEKEQRKEAPSYSSSTL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LXQC01000187
EMBL· GenBank· DDBJ
TFE66167.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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