A0A109QY89 · A0A109QY89_9MICO

  • 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.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

167150100150200250300350400450500550600650
Type
IDPosition(s)Description
Binding site204-211ATP (UniProtKB | ChEBI)
Binding site426Zn2+ (UniProtKB | ChEBI); catalytic
Active site427
Binding site430Zn2+ (UniProtKB | ChEBI); catalytic
Binding site502Zn2+ (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
      AWU67_00390

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • ERGS5:02
  • Taxonomic lineage
    Bacteria > Bacillati > Actinomycetota > Actinomycetes > Micrococcales > Microbacteriaceae > Microterricola

Accessions

  • Primary accession
    A0A109QY89

Proteomes

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Membrane

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane12-33Helical
Transmembrane111-133Helical

Keywords

Interaction

Subunit

Homohexamer.

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain196-335AAA+ ATPase
Region617-671Disordered
Compositional bias618-628Basic and acidic residues
Compositional bias636-652Polar 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
    671
  • Mass (Da)
    73,009
  • Last updated
    2016-04-13 v1
  • MD5 Checksum
    544DBEB64BFCB27C980533B4ACB695E6
MNVKKLLRGPLLYIVLAVVAVWIGSSLITMSGFRQVSTQEGLAFLKDGKVASAKIVDGEQRVDLTLTTADPKLGDQVQFYYVAPRGPEVVDAVTTANPPKGFDDEVPQPNWLLSLLGILLPVLLIGLFFWWMLSSMQGGGNKVMQFGKSKAKLVTKESPKVTFEDVAGADEAIEELEEIKDFLKDPARFQAVGARIPKGVLLYGPPGTGKTLLARAVAGEAGVPFYSISGSDFVEMFVGVGASRVRDLFQQAKENSPAIIFVDEIDAVGRHRGAGMGGGHDEREQTLNQLLVEMDGFDPKANVILIAATNRPDILDPALLRPGRFDRQIGVDAPDMLGRKKILEVHGKGKPLAKGVDLEVVARKTPGFTGADLANVLNEAALLTARSHAQLIDNRALDEAIDRVMAGPQRRTRVMRDKEKLITAYHEGGHAVAAAAMNYTDPVTKITILPRGRALGYTMVMPLEDKYSVTRNELLDQLTYAMGGRVAEEMVFHDPTTGASNDIEKATSTARKMVTEYGMSTDVGAVKLGQSSGEVFLGRDMGHQRDYSERIAEQVDNEVRALIEQAHDEAWQVLNDNRDILDRLAAELLEKETLDHNQIAEIFADVRKLPERPQWLSSDKRPISERPPIDFPVLTSPVNPGITSGSVESSEAGTEAPPERGPSANPRPATA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias618-628Basic and acidic residues
Compositional bias636-652Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP014145
EMBL· GenBank· DDBJ
AMB57570.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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