A0A517PWG8 · A0A517PWG8_9PLAN

  • Protein
    ATP-dependent zinc metalloprotease FtsH
  • Gene
    ftsH4_6
  • 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.

168850100150200250300350400450500550600650
Type
IDPosition(s)Description
Binding site243-250ATP (UniProtKB | ChEBI)
Binding site465Zn2+ (UniProtKB | ChEBI); catalytic
Active site466
Binding site469Zn2+ (UniProtKB | ChEBI); catalytic
Binding site542Zn2+ (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
      ftsH4_6
    • Synonyms
      ftsH
    • ORF names
      HG66A1_55360

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • HG66A1
  • Taxonomic lineage
    Bacteria > Planctomycetota > Planctomycetia > Planctomycetales > Planctomycetaceae > Gimesia

Accessions

  • Primary accession
    A0A517PWG8

Proteomes

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Membrane

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane38-56Helical
Transmembrane155-173Helical

Keywords

Interaction

Subunit

Homohexamer.

Family & Domains

Features

Showing features for region, compositional bias, domain.

Type
IDPosition(s)Description
Region1-35Disordered
Compositional bias7-32Basic and acidic residues
Domain235-374AAA+ ATPase
Region646-688Disordered
Compositional bias664-679Basic 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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    688
  • Mass (Da)
    76,145
  • Last updated
    2019-10-16 v1
  • Checksum
    8F41ADA30FCA9720
MPNLDPKQSNRRERPTPPERNPKGDGRRPEPKGPKSNALWYLVVGGLILFITLSVVSNNKRGEKIKFGDFVKGLDDGKYNKTNVHELKFGTDYIVFQDQPKQEGSEKGTLANTTKNYYIPVWGIPQEARAQLQTKLENKSIIVDSESRPSEWESLIAVLFFPVVLLIFVIYLFRRMGGAGSPMSFGRSRGRMYAQDDIEVTFNDVAGIEEAVEELREVVEFLKTPAKYQALGGRIPKGVLLVGPPGTGKTMLAKAVAGEAGVPFYGLSGSDFVEMFVGVGAARVRDMFQQAAQRSPAIIFIDELDALGKTRGSGMPGGHDEREQTLNALLVEMDGFGSDQSVIVMGATNRPETLDPALMRPGRFDRHVLVDRPDVRGREAILKVHSAKVKMDESVNLQHIAKITPGFVGADLANLINEAALLAARNNKEAVTMRECEEGVERVVAGLEKSTRLIHEDEKNRVAYHECGHALVACSLPNVDPVHKISIVPRGLGALGYTLQRPEEEKQLVTQSELENRICVLLGGIAAEEIIYQETSTGAQNDLQRATDLARRMVTEFGMSAKLGRVHYSETRRSPFLGDTSSGSESIHSENTLREIDLEIRRIIDQCAKIAYEVLDERRELLEHLTQELLECEVMDMDQLQSILKQHQRGPQIKPGTFVDNSAENKTAEKDKEEPASDNDQSTDGTGT

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias7-32Basic and acidic residues
Compositional bias664-679Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP036266
EMBL· GenBank· DDBJ
QDT23712.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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