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A0A1A0I1Z3 · A0A1A0I1Z3_9ACTN

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.

1808100200300400500600700800
Type
IDPosition(s)Description
Binding site208-215ATP (UniProtKB | ChEBI)
Binding site430Zn2+ (UniProtKB | ChEBI); catalytic
Active site431
Binding site434Zn2+ (UniProtKB | ChEBI); catalytic
Binding site506Zn2+ (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
      A5766_16070

Organism names

Accessions

  • Primary accession
    A0A1A0I1Z3

Proteomes

Subcellular Location

Cell membrane
; Multi-pass membrane protein
Membrane

Features

Showing features for transmembrane.

TypeIDPosition(s)Description
Transmembrane114-135Helical

Keywords

Interaction

Subunit

Homohexamer.

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain200-339AAA+ ATPase
Region618-808Disordered
Compositional bias627-641Basic and acidic residues
Compositional bias643-658Pro residues
Compositional bias674-698Polar residues
Compositional bias728-775Polar residues
Compositional bias781-808Basic 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
    808
  • Mass (Da)
    87,011
  • Last updated
    2016-10-05 v1
  • MD5 Checksum
    341E16134C861376F98A801CA0AAA48C
MRMNRKTVFRNLAILAVLVLALWGWSAMRDGDRGYTGVDTSVALTQLNTKNTKFVQIDDREQQLRIETKDAIKVDGKDVTKISTKYPASAGEQVFDSVKSTGAGYQTNVTQQSVFWQIMIFLLPMLLLFGLFFFVMNRMQGGGKGGVMGFGKSKAKQLSKDMPKTTFADVAGADEAVEELYEIKDFLQNPARYQALGAKIPRGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDLFEQAKNNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGDRSGVILIAATNRPDILDPALLRPGRFDRQIPVGNPDIAGRRAILKVHAKGKPIAEDADLDGLAKRTPGMSGADLANVVNEAALLAARENKTVITAEMLEEAVDRVIGGPRRKSRIISEHEKKVVAYHESGHTLAAWAMPDLDPIYKVTILARGRTGGHALAVPEQDKDLMTRSEMIARLVMAMGGRASEELVFHEPTTGASSDIDQATKIARAMVTEYGMSAKLGAVRYGQEQGDPFLGRSMGAQSDYSAEVASEIDDEVRRLIEAAHTEAWAILSEYRDTLDVLASELLEKETLTRKDLESILSDVEKRPRITTFNEFGERTPSDKPPVKTPGERAIERGEPWPPPPPEPVREPVGAGSAPGSPSGYPGGQQPCYGTPQGPGSYPGQSYGQPYPQQPYPQGPQGGGTRPDYGAPRDWSAPGWPPQSQGDPQSHGYPQTQGYPQNGNPNGANGNQPNGYGYGNGSYGGQNGAGHNGGQHRDDSGDSGSHGDNRSHGDNRSHGDGA

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias627-641Basic and acidic residues
Compositional bias643-658Pro residues
Compositional bias674-698Polar residues
Compositional bias728-775Polar residues
Compositional bias781-808Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LZMI01000136
EMBL· GenBank· DDBJ
OBA30053.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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