A0A0I9S4L8 · A0A0I9S4L8_BACFG

  • 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

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.

167550100150200250300350400450500550600650
Type
IDPosition(s)Description
Binding site230-237ATP (UniProtKB | ChEBI)
Binding site453Zn2+ (UniProtKB | ChEBI); catalytic
Active site454
Binding site457Zn2+ (UniProtKB | ChEBI); catalytic
Binding site528Zn2+ (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
      EE52_0222875

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • DCMOUH0018B
  • Taxonomic lineage
    Bacteria > Bacteroidota > Bacteroidia > Bacteroidales > Bacteroidaceae > Bacteroides

Accessions

  • Primary accession
    A0A0I9S4L8

Subcellular Location

Cell membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane21-37Helical
Transmembrane132-153Helical

Keywords

Interaction

Subunit

Homohexamer.

Family & Domains

Features

Showing features for domain, coiled coil, region, compositional bias.

Type
IDPosition(s)Description
Domain222-362AAA+ ATPase
Coiled coil579-606
Region633-675Disordered
Compositional bias634-675Polar 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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    675
  • Mass (Da)
    75,064
  • Last updated
    2015-10-14 v1
  • Checksum
    63B193FAFFB6E06D
MDNNSKKTNNKVNMPKFNLNWMYMIIALMLLGLYFANGNSSVNKNISYDEFQQYVRDGYVSKVIGYDDNTVEIYIKPQYVGAVFKQDSTRVGRNPMITTEAPSRENLDNFLQKEKEETHFDGSVSYDKKKDYFSAILWNVLPIVFLIALWIFFMRRMGSGASGGAGGVFNVGKSKAQLFEKGGSIKVTFKDVAGLAEAKQEVEEIVEFLKEPQKYTDLGGKIPKGALLVGPPGTGKTLLAKAVAGEANVPFFSLAGSDFVEMFVGVGASRVRDLFKQAKEKAPCIVFIDEIDAVGRARGKNPAMGGNDERENTLNQLLTEMDGFGSNSGVIILAATNRVDVLDKALLRAGRFDRQIHVDLPDLNERKEVFGVHLRPIKIDDTVDVDLLARQTPGFSGADIANVCNEAALIAARHGKKFVGKQDFLDAVDRIIGGLEKKTKITTEAERRSIALHEAGHASISWLLEYANPLIKVTIVPRGRALGAAWYLPEERQITTKEQMLDEMCATLGGRAAEDLFIGRVSSGAANDLERVTKQAYGMIAYLGMSEKLPNLCYYNNDEYSFQRPYSEKTAELIDEEVKRMVNEQYERAKQILSEHKEQHNELAQLLIDKEVIFAEDVERIFGKRPWASRSEEIMAANSKQENTAHPTDGEDTDTPQATESQEDNAQQEPAASQN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias634-675Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JMZZ02000228
EMBL· GenBank· DDBJ
KFX72331.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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