A0A7C9HS77 · A0A7C9HS77_9BACT

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

168950100150200250300350400450500550600650
Type
IDPosition(s)Description
Binding site235-242ATP (UniProtKB | ChEBI)
Binding site458Zn2+ (UniProtKB | ChEBI); catalytic
Active site459
Binding site462Zn2+ (UniProtKB | ChEBI); catalytic
Binding site533Zn2+ (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
      hflB
    • Synonyms
      ftsH
    • ORF names
      F0475_04740

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • A2879
  • Taxonomic lineage
    Bacteria > Bacteroidota > Bacteroidia > Bacteroidales > Prevotellaceae > Prevotella

Accessions

  • Primary accession
    A0A7C9HS77

Proteomes

Subcellular Location

Cell membrane
; Multi-pass membrane protein

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane21-43Helical
Transmembrane138-159Helical

Keywords

Interaction

Subunit

Homohexamer.

Family & Domains

Features

Showing features for domain, compositional bias, region.

Type
IDPosition(s)Description
Domain227-367AAA+ ATPase
Compositional bias640-659Basic and acidic residues
Region640-689Disordered
Compositional bias665-689Polar 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
    689
  • Mass (Da)
    76,142
  • Last updated
    2021-02-10 v1
  • Checksum
    ACA29CD35FBDF761
MDNSSPNNNPNMPKMPKFNMNWLYVLVIIALGVVFFAGGNSFLSSSAGVDRDYTTFKQYIAKGYGTKVVINKSDNTLRMYVSPDHIRDIFKQGTQQVGKSPYVNVEIGSVDKVETFLDQAVAQKKIASYSYENKSGNGFMDILISIAPWVFFFGIWYFLIRRMGGGAGGGGGVFSVGKSKAKLYEKANEMGITFKDVAGQTGAKQEVQEIVEFLKNPKKYTDLGGKIPKGALLIGPPGTGKTLLAKAVAGEAGVPFFSMSGSDFVEMFVGVGASRVRDVFRQAKEKSPCIIFIDEIDAVGRARSKNPAMGGNDERENTLNALLTEMDGFGTNSGVIVLAATNRVDMLDKALLRAGRFDRQIHVDLPDLPERKDIFLVHMRNLKLDKNLDIDLLARQTPGFSGADIANVCNEAALIAARHDSKEVAKQDFLDAVDRIIGGLEKKTKVMTTAEKRTIALHEAGHATISWFCEHSNPLVKVSIVPRGQALGAAWYLPEERPITTKEQMLDEMCSLLGGRAAEELFTGHISTGAMNDLERATKSAYGMIAYAGMSDRLPNICYYNNDEYNFQKPYSDTTAKMIDEEVLKMINGQYDRAKQILTEHKEGHNRLAQLLMEREVIMAEDVEEIFGKRPWVSRTDELLDQEAKSQPKLEDMPEAVKQAQAEHEAQQRALNNNATKAEDDIESNNTAE

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias640-659Basic and acidic residues
Compositional bias665-689Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
VVIQ01000003
EMBL· GenBank· DDBJ
MUL27622.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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