A0A2M8P168 · A0A2M8P168_9CHLR

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.

163350100150200250300350400450500550600
Type
IDPosition(s)Description
Binding site187-194ATP (UniProtKB | ChEBI)
Binding site409Zn2+ (UniProtKB | ChEBI); catalytic
Active site410
Binding site413Zn2+ (UniProtKB | ChEBI); catalytic
Binding site489Zn2+ (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
      CUN51_04735

Organism names

Accessions

  • Primary accession
    A0A2M8P168

Proteomes

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Membrane

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane95-116Helical

Keywords

Interaction

Subunit

Homohexamer.

Family & Domains

Features

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

Type
IDPosition(s)Description
Domain179-318AAA+ ATPase
Coiled coil554-581
Region592-633Disordered
Compositional bias596-623Basic and acidic 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
    633
  • Mass (Da)
    69,082
  • Last updated
    2018-04-25 v1
  • Checksum
    B7CD27E724A351CD
MAIFLGVRGGGSSGSELKLSELAQQIISGTPRISAIAVAQNEVRVTYAGSSRPPAITRKDPSMPLPEQLISLGVPKELVAQLPIEYVQPNDITPFFSILVSLLPIILIAGFFFLMLRQAQGSNNQAISFGKSRARMFTGDRPTVTFDDVAGADEAKEELREVVEFLKEPDKFVQLGARIPKGVLLIGSPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFDQAKRHSPCIIFIDEIDAVGRHRGAGLGGSHDEREQTLNQILVEMDGFDTDTNVIVIAATNRPDILDPALMRPGRFDRRVVLDRPDVKGREAILRVHSRGKPLAADVDLAVLSRTTPGFVGADLENLMNEAAILAARKNKKTISMRDCEEAIYRVVLGPERKSRVISEEQKRLVAYHEAGHAIVGHFLPNCDPIRKITIVPRGISGGSVLSVPEDDMGPETRARIEDAIAQALGGRAAEAIVFGEVTTGAGGGNGSDLATVTRYARAMVTRFGMSDRLGPMIFGQKEEMVFLGREIAEQRDYSEAIAEIIDEEVKKIVDEAYQRALAVLTEHREELERVAQRLMEVETIDYEEFMQLMGESPATNRRKRPEMLPKPAEKPATQREQRDDLPPRMGTAASPA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias596-623Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PGTK01000004
EMBL· GenBank· DDBJ
PJF31297.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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